Skip to content
Publicly Available Published by De Gruyter June 1, 2013

Current and future use of “dried blood spot” analyses in clinical chemistry

Sylvain Lehmann, Constance Delaby, Jérôme Vialaret, Jacques Ducos and Christophe Hirtz

Abstract

The analysis of blood spotted and dried on a matrix (i.e., “dried blood spot” or DBS) has been used since the 1960s in clinical chemistry; mostly for neonatal screening. Since then, many clinical analytes, including nucleic acids, small molecules and lipids, have been successfully measured using DBS. Although this pre-analytical approach represents an interesting alternative to classical venous blood sampling, its routine use is limited. Here, we review the application of DBS technology in clinical chemistry, and evaluate its future role supported by new analytical methods such as mass spectrometry.

Introduction

Over a century since a new blood sampling method based on the use of a dry matrix was first described by Ivar Bang [1], the interest in dried blood spot technology has continuously evolved. This alternative approach, based on collecting blood spots on blotting paper and drying them, is called “dried blood spot” or DBS. In 1963, Robert Guthrie used this technique to develop systematic neonatal screening for the metabolic disease, phenylketonuria [2]. Set up for the first time in Scotland, this use of DBS spread to the UK in the 1970s, mainly to detect any innate errors in metabolism that were treatable. Of note, the use of DBS remains almost exclusively limited to this type of neonatal screening, even though many studies demonstrate its potential application in clinical biology, as well as in research. Indeed, classical clinical chemistry methods, small molecule and lipid analysis or molecular biology approaches, are all perfectly suited to the use of DBS. However, one limitation is represented by the small blood volumes associated with DBS sampling (5–10 µL) and therefore the need for very sensitive methods. Recent technological advances, in microfluidics, multiplex immunological/genomic detection systems, and mass spectrometry, could however settle most sensitivity problems. In this overview we will summarize the pros and cons of this particular biological sampling method and evaluate its future role in clinical biology.

General DBS procedure

Collection and sampling

The collection area (finger, heel) has to be first disinfected. The skin is then punctured with a sterile lancet (Figure 1). The first blood drop is dabbed and subsequent drops are placed on blotting paper marked with circles to be filled. Once all the required circles are filled, the blotting paper is left to dry for a few hours at room temperature on a non-absorbent surface. The drying time is very important as residual humidity favors bacterial development or molds and modifies the extraction stage [3].

Figure 1 
						DBS collection process.
						Peripheral blood is collected by the patient at home. He disinfects the area (finger) and pierces the skin using a sterile lancet before blotting the blood onto high quality filter paper. The DBS is dried for 1–3 h at room temperature and mailed using the classical envelope. At the laboratory, the DBS is stored at room temperature. The sample is punched (2–6 mm) and the analytes are extracted using an appropriate buffer before analysis.

Figure 1

DBS collection process.

Peripheral blood is collected by the patient at home. He disinfects the area (finger) and pierces the skin using a sterile lancet before blotting the blood onto high quality filter paper. The DBS is dried for 1–3 h at room temperature and mailed using the classical envelope. At the laboratory, the DBS is stored at room temperature. The sample is punched (2–6 mm) and the analytes are extracted using an appropriate buffer before analysis.

Conservation

Once dry, the DBS cards are moved into a waterproof plastic bag, possibly along with a desiccant and a humidity indicator [4]. The purpose of the desiccant is to finalize the drying process, which also minimizes any risk of infection associated with sampling. Periods of storage at room temperature vary according to the biological factor, from 1 week for proteins [5], to 1 year or more for nucleic acids [6]. As far as serology is concerned, the blotting papers are usually kept at –20°C upon receipt [7]. For long-term preservation (up to several years) the blotting papers are stored either at −20°C or –80°C [8, 9].

Extraction

Extraction of the analytes from DBS specimens needs to be achieved using a standard procedure. One or more 2–8 mm diameter discs are then created with a specific punch. These small “spots” are placed in an elution buffer for variable time spans according to the procedure. The DBS extraction is then treated as a hemolyzed whole blood sample, and tested with methods often intended for plasma or serum. The elution buffer plays a major role in re-solubilizing the analytes to be tested. A wide variety of buffers are described in the literature. The most common are saline/phosphate buffers, often with added detergents (Tween, Triton…), carrier proteins and chelators [ethylene diamine tetra acetic acid (EDTA)], as well as organic buffers with methanol, acetonitrile or ethanol. For nucleic acids, standard commercial kits exist which are compatible with molecular biology tests, from polymerase chain reaction (PCR) to genomic chips [10].

Pros and cons of DBS

One of the main advantages of using DBS technology is that it allows access to samples in pre-analytical situations were standard blood collection is challenging (problem with sampling, storage). The typical DBS contains approximately 50 µL of whole blood on an average surface of 12 mm2 (Figure 2). It enables the testing of various analytes such as nucleic acids, proteins, lipids, or small organic and non-organic molecules (Table 1). Two types of DBS are mostly available: cotton paper filters of different qualities (Whatmann 903 Protein Saver Cards Whatmann, Springfield Mill, UK; Perkin Elmer 226 Spot Saver Card, Perkin Elmer, Waltham, USA) and glass microfiber filter papers (Agilent Bond Elut DMS, Santa Clara, CA, USA; Sartorius Glass Microfiber Filters, Goettingen, Germany). The main difference between the two supports is that the glass fiber does not soak up reagents, which diminishes non-specific analyte adsorption on the membrane.

Figure 2 
					Comparison of the use of classical blood sampling versus DBS sampling resulting in a 100-fold reduction in blood volume and an ease of storage.

Figure 2

Comparison of the use of classical blood sampling versus DBS sampling resulting in a 100-fold reduction in blood volume and an ease of storage.

Table 1

Overview of DBS card usage in clinical chemistry other than its use for neonatal screening.

Methods Parameter Clinical interest References
Exogeneous nucleic acid
Real-time PCR

Q PCR
Human herpesvirus type 6 Differentiation active human herpesvirus type 6 infection from inherited HHV-6 [11, 12]
RT-PCR Human hepatitis C Monitoring hepatitis C virus (HCV) infection among injecting drug users [7, 13]
Real-time PCR Human hepatitis B Hepatitis B virus (HBV) DNA quantification [14]
Real-time PCR, Q-PCR Cytomegalovirus Diagnosis of human congenital cytomegalovirus infection [15, 16]
Nested PCR, RNA assays, RT-PCR HIV virus Detection of human immunodeficiency virus [8, 13, 17]
Peptides/proteines
ELISA HIV virus Human immunodeficiency virus serotyping [18]
ELISA C-reactive protein Cardiovascular risk [19]
DELFIA Free-β human chorionic gonadotrophin (free-β hCG) and PAPP-A Fetal aneuploidy risk [20]
Immuno-fluorometric assays Luteinizing hormone and follicle-stimulating hormone Circulating gonadotropin concentrations [21]
Chemiluminescent immunoassay Prostate specific antigen (PSA) Prostate cancer screening [22]
RIA Somatedin-C (IGF-1) Screening test for growth hormone deficiency [23]
ELISA Apoliproteins B Hypercholesterolemia [24]
Immune nephelometry α1-Antitrypsin α1-Antitrypsin deficiency [5]
ELISA α-Fetoprotein Open neural tube defect and Down syndrome [25]
Enzyme assays Biotinidase Biotinidase deficiency [26]
EIA Calcitonin gene-related peptide Children with autism or mental retardation [27]
LC-MS/MS Ceruloplasmin Wilson’s disease [28]
Spectrophotometry Hemoglobin Folate analysis [29]
Turbidimetric immunoassay Glycated hemoglobin A1c Diagnosis and treatment of diabetes [30]
LC-MS/MS HbA2 Diagnosis of thalassemia [31]
Non-radiochemical HPLC Hypoxanthine-guanine phosphoribosyltransferase adenine phosphoribosyltransferase adenosine deaminase Purine metabolism disorders [32]
LC-MS/MS Iduronate 2-sulfatase Diagnosis of Hunter disease [33]
ELISA, RIA Insulin-like growth factor Evaluation of growth hormone status [34]
ELISA Prolactin Diagnosis of epilepsy [35]
ELISA Transferrin receptor Iron deficiency [36]
DELFIA Thyroglobulin Thyroid status [37]
ELISA CD4 CD4+ lymphocyte counts in HIV patients [38]
ELISA Measles and rubella IgM and IgG Detection of measles and rubella IgM and IgG [39]
DELFIA Toxoplasma gondii-specific IgM and IgA Screening of congenital toxoplasmosis [40]
RIA Insulin Diagnosis of hyperglycemia/hyper-insulinemia [41]
Enzyme assays Acid α-glucosidase Glycogen storage disease II [42]
Enzyme assays 8 lysosomal enzymes Clinical differentiation among mucopolysaccharidosis, oligosaccharidosis, and mucolipidosis II and III [43]
Enzyme assays α-iduronidase activity Diagnosis of α-L-iduronidase deficiency [44]
Biochemistry Phytanic acid and pristanic acid Diagnosis of peroxisomal disorders [45]
Electro-immunodiffusion β-Lipoprotein Familial type II and combined hyperlipidemia [46]
ELISA Fumarylacetoacetase Hereditary tyrosinemia type I [47]
Luminex TGF-β1, (MCP-1, (MIP-1α, MIP-1β, NT-4, BDNF, RANTES, CRP, MMP-9… Inflammatory status [48]
Enzyme immunoassay IgE Allergic disease and repeated macro-parasitic infections [49]
ELISA IgG and IgA Nasopharyngeal carcinoma screening [50]
Enzyme assays Lysosomal b-d-galactosidase (bG; EC 3.2.1.23) Mucopolisaccharidosis type I [51]
Fluorometric immunoassay Thyroid-stimulating hormone Immunoreactive trypsin, creatine kinase MM isoenzyme Congenital hypothyroidism, congenital adrenal hyperplasia, and muscular dystrophy [52]
Column chromatography Thyroxine-binding globulin Neonatal hypothyroidism [53]
Immunoassay Trypsine immunoreactive (IRT) Cystic fibrosis [54]
ELISA Antibodies against hepatitis A Hepatitis A [55, 56]
ELISA Antibodies against hepatitis B Hepatitis B [57]
CORECELL Maternal antibody to hepatitis B Infection with HBV [58]
ELISA Anti-HCV antibodies Detection of antibodies to hepatitis C virus [59, 60]
ELISA Anti-malarial antibodies Diagnosis of malaria [61]
ELISA Pseudomonas aeruginosa antibodies Pseudomonas aeruginosa in patients with cystic fibrosis [62]
ELISA Thyroid antibody Thyroid-antibody screening [63]
ELISA Antibodies against tetanus Screening of tetanus and diphtheria toxins [64]
ELISA Antibodies against Brucella Diagnosis of human brucellosis [65]
ELISA Antibodies against cysticercus Detection of anti-cysticercus antibodies [66]
ELISA Antibody against HTLV-1 and HTLV-2 Detection of the Human T-lymphotropic virus [67]
Immuno-fluorescence Antibodies against to Coxiella burnetii, Bartonella quintana, and Rickettsia conorii Diagnosis of Rickettsial diseases [68]
ELISA Antibody against syphilis Diagnosis of syphilis [69]
Indirect hemagglutination test Antibody against Treponema Diagnosis of syphilis [70]
ELISA Antibody against Trypanosoma cruzi Diagnosis Trypanosoma cruzi infections [71]
ELISA Antibody against Trichomonas vaginalis Seroepidemiology of Trichomonas vaginalis [72]
Fluorescent Galactose-1-phosphate uridyltransferase (GALT) Galactosemia [73]
ELISA Epstein-Barr virus Epstein-Barr virus immunoglobulin G (IgG) serology [50]
EIA Rubella virus Detection of congenital Rubella virus [74]
EIA Dengue virus Dengue virus diagnosis [75]
ELISA Antibodies against hepatitis A Hepatitis A [55, 56]
ELISA Antibodies against hepatitis B Hepatitis B [57]
CORECELL Maternal antibody to hepatitis B Infection with HBV [58]
ELISA Anti-HCV antibodies Detection of antibodies to hepatitis C virus [59, 60]
Multiplex ligation-dependent probe amplification on DNA (MLPA) Detecting 22q11.2 deletions Manifestations associated with DiGeorge syndrome [76]
PCR GSTM1 et GSTT1 gene variant Researching pediatric cancer susceptibility genes [77]
ELISA multiplex Human papillomaviruses (HPV), Helicobacter pylori, hepatitis C virus (HCV), and JC polyomavirus (JCV) Infections of HPV, H. pylori, HCV, and JCV [78]
Lipids and small molecules
Densitometry Phenylalanine Phenylketonuria [2]
Enzymatic method Triglycerides Evaluation of the cardiometabolic risk [79]
LC-MS/MS Amino, organic, and fatty acid Metabolic disorders [80]
Fluorimetric HPLC method Homocysteine Homocysteinuria [81]
Enzymic methods Determination of glucose Monitoring of diabetic patients [82]
LC-MS/MS 17-OHP, androstenedione Congenital adrenal hyperplasia [83]
HPLC Retinol Retinol analysis [84]
LC-MS/MS Thyroxin (T4) and TSH Congenital hypothyroidism [85]
Chemiluminescence Free thyroxine (FT4) Assessment of thyroid status [86]
LC-MS/MS Free carnitine Inborn errors of metabolism [87]
GC-MS Methylcitrate Newborn screening for propionic acidemia [88]
GC-MS Octanoate, decanoate, cis-4-decenoic acid (C10:1) and cis-5-tetradecenoic acid Free fatty acids [89]
LC-MS/MS Succinylacetone Hepatorenal tyrosinemia [90]
FIA-ESI-MS/MS Guanidinoacetate and creatine Primary creatine disorders [91]
Xenobiotics
LC-MS HIV antiretroviral drugs

(NVP, SQV, ATV, APV, DRV, RTV, LPV, EFV, ETV)
HIV therapeutic follow-up [92, 93]
RIA Cocaine metabolite (benzoylecgonine) Information on newborns and maternal exposures to various substances, including drugs of abuse [94]
LC/MS Quinine, mefloquine, sulfadoxine, pyrimethamine, lumefantrine, chloroquine Blood levels of drugs administered for malaria and pneumonia treatment [95, 96]
Capillary gas chromatography Dichlorodiphenyldichloroethylene Newborns’ body burden of environmental pollutants [97]
Fluorescence polarization immunoassay Theophylline Therapeutic drug monitoring [98]
Genomics
PCR Mutations of factor V G1691A (FVL), prothrombin (PT) G20210A, 5′10′ methylenetetrahydrofolate reductase (MTHFR) C677T, and methionine synthase (MS) A2756G Susceptibility to venous thromboembolism [99]
Real-time PCR Mutation c.-32T>G (IVS1-13>G) Acid maltase deficiency [100]
DNA-based assay Mutation (IVS4+919G->A) Fabry disease [101]
DHPLC Substitution (c.840C>T) Spinal muscular dystrophy [102]
Specific restriction digest method Mutation (c.985A>G) Medium chain acyl-coA dehydrogenase deficiency (MCADD) [103]
PCR Mutation of cystic fibrosis transmembrane conductance regulator (CFTR) Cystic fibrosis [104]
PCR DNA mutation β-thalassemia [105]
PCR Real-time PCR SMN1 exon 7 deletions

Copy number variations of SMN1 and SMN2
Spinal muscular atrophy [106]
PCR FMR1 methylation Fragile X syndrome [107]
Multiplex ligation-dependent probe amplification on DNA (MLPA) Detecting 22q11.2 deletions Manifestations associated with DiGeorge syndrome [76]
PCR GSTM1 and GSTT1 gene variant Researching pediatric cancer susceptibility genes [77]

In comparison to conventional blood testing, DBS offers practical, clinical and financial advantages. Firstly, DBS collection is easy to perform and relatively painless (Figure 1). It can be carried out by the patient at home, without the need for specialized structures such as medical laboratories. This sampling procedure is far less invasive than venipuncture, therefore is better suited for patients requiring numerous blood tests, such as those with damaged/altered veins, the elderly or infants. The use of DBS also minimizes the volume of blood taken from patients. It has been shown that drying the blood spot on blotting paper damages the capsid of viruses [HIV, Cytomegalovirus (CMV), hepatitis C virus (HCV), human T-lymphotropic virus (HTLV)] [108] reducing any possible risk of contamination for medical or paramedical staff [4]. In addition, it enables the shipping of samples by regular mail with no particular risk of contamination. This represents a valuable asset for sampling in remote communities either located far away from a testing laboratory or with limited technical infrastructure available, therefore provides added value compared to standard blood sampling [59]. Through its small size and stacking capacity, DBS is also a valuable solution for reducing and facilitating storage in clinical laboratories and biobanks [109]. It is noteworthy that in case of storage, an individual bagging or a separation using a sturdy paper will be important to avoid the possibility of cross-contamination between cards [3]. These properties of DBS have been utilized in experimental research, by facilitating pharmacological studies and pharmacokinetics on small animals with very limited volumes of biological liquids. This follows the regulations aimed at protecting small animals (decreasing sample volume and sophistication of sampling methods) during pre-clinical studies [110]. Concerning sample stability, many studies have shown that most analytes from whole blood are stable at room temperature for at least 7 days. In some cases such as opiates, DBS even increases stability during storage [111], and nucleic acids are a major tool for short- and long-term preservation, as they can be isolated after several months at room temperature and several years at −20°C. [112]. From a medico-economical point of view, it is interesting to note that the use of DBS allows a significant cost reduction due to decreased requirements in trained staff, facilitated transportation, storage, and processing.

A major drawback of DBS technology resides in the nature of the biological sample itself (Figure 2). In a standard sampling procedure, either serum or plasma is analyzed, whereas DBS samples are composed of hemolyzed whole blood. Hence, interferences due to hemoglobin and the release of intracellular content could occur. The blood cells (erythrocytes, leukocytes, platelets etc.) are altered by the drying process, thus cellular hematological testing is impossible. Drying can also denature proteins and alters the enzymatic activity of blood proteins (aspartate transaminase). Any remaining cells in the samples can also change the global protein composition and therefore modify the concentration of some analytes. In some cases, clinical thresholds set up using standard blood samples need to be adapted. Hematocrit that affects blood dispersal on the blotting paper also needs to be taken into account [113]. The small volume of samples resulting from the DBS can be a disadvantage for low sensitivity assays [4] and for running multiple tests.

Use of DBS in clinical chemistry

The primary use of DBS in France is systematic neonatal screening. As blood sampling in newborns is difficult, DBS technology represents a viable alternative. DBS testing was set up in 1978 by the French Association for screening and preventing disabilities in children (http://www.afdphe.org/). Sampling of newborns enables the detection of phenylketonuria, hypothyroidism, adrenal hyperplasia, cystic fibrosis and sickle cell disease (in some areas). The extension of these tests to cover a wider number of diseases, similar as in to USA, is currently under consideration [28]. A positive result will always be confirmed or denied by further specific tests. Beyond its use for neonatal screening, many clinical analytes can be measured using DBS. These analytes are divided into four major categories as follows (see also Table 1):

Exogenous nucleic acids

The measurement of nucleic acids is typically required in the virology field. There is a growing interest in viral screening through nucleic acid detection (RNA, DNA) using DBS, as current molecular biology technologies [quantitative polymerase chain reaction (Q-PCR), reverse transcription polymerase chain reaction (RT-PCR)] are very sensitive and require only a small sample amount (<20 µL). Nevertheless, it is important to note that the amount of material available from a DBS sample is between 1 and 2 logs lower compared to a standard serum or plasma sample. The preservation of nucleic acids on blotting paper is stable for long periods [3], providing it is dried and stored away from humidity in a suitable plastic bag containing a desiccant. DBS nucleic acid detection is mainly used in screening for viral diseases such as cytomegalovirus [15], herpes simplex virus [11], hepatitis A [55], hepatitis C [13] and HIV [114].

Peptides – proteins

Concerning proteins and peptides one caveat is represented by the relative difficulty of their extraction from DBS samples, as well as the low sensitivity of certain protein dosage. The main proteins measured from DBS can be classified into two groups: standard serum proteins and antibodies. The most widely used analytical techniques are immunological assays which measure clinical analytes with good specificities and sensitivities. An example is represented by the immunoturbidimetric assay for glycated hemoglobin (to monitor glycemic balance in diabetic patients). Glycated hemoglobin measured from DBS samples correlate well with standard tests. In addition, this analyte remains stable for over 15 days on DBS [30]. DBS is also well adapted for the enzyme-linked immunosorbent assay (ELISA) detection of specific antibodies against Epstein-Barr virus [50], Rubella virus [74], dengue virus [75] or hepatitis C [7, 59] and HIV virus [13].

An interesting evolution of liquid chromatography/mass spectrometry (LC/MS) is represented by quantitative techniques for measuring peptides and proteins [115]. This approach was adapted on DBS to measure ceruloplasmin for the neonatal screening of Wilson’s disease [28] and for peptide C quantification [116]. When used in multiplex mode (multiple reaction monitoring) this mass spectrometry method has the potential to measure many analytes within only a few microliters [115]. For instance, Chambers et al. [117] have succeeded in quantifying a panel of 40 serum proteins from DBS, using this approach.

Lipids, sugars and small molecules

Phenylalanine, an amino acid measured in phenylketonuria screening of newborns, exemplifies the dosage of small molecules using DBS [2]. Small organic molecules are significantly less sensitive than proteins to the drying process which characterizes DBS samples. In addition, the major progress of liquid chromatography/mass spectrometry (LC/MS) in this field has allowed the quantification of many small molecules such as vitamin D [118] or lipids [79]. For instance, high levels of triglycerides, representing an important risk for cardiovascular and coronary diseases, can be quantified using DBS. These analytes remain stable on DBS for 30 days at room temperature and up to 90 days at 4°C. The profiling of glycans on DBS was also recently achieved using mass spectrometry [119].

Xenobiotics

In 1993, Henderson et al. [120] demonstrated the use of DBS for detecting narcotics, such as cocaine, through modification of a radioimmunoassay (RIA) commercial kit. Xenobiotic testing using DBS has since played an important role, mainly by the screening of antimalarial and antiretroviral drugs by LC/MS in isolated populations [95]. Another example is represented by the quantification of nine antiretroviral molecules in HIV using DBS. This detection method has been validated by the Food and Drug Administration (FDA) with sample stability ranging from 12 to over 90 days at room temperature [92]. In the field of toxicology, which is a major application of DBS [121], Saussereau et al. [122] have, for example, developed a new drug screening method based on LC/MS using on-line extraction for the quantification of opiates, cocainics or amphetamines. The development of these new measurement techniques, based on LC/MS for xenobiotics, will greatly increase the interest of using DBS in clinical chemistry.

Genomics

The clinical potential of DBS for genomics has been demonstrated as early as 1987 [123]. DNA micro-extraction from dried blood has allowed the detection of mutations responsible for diseases such as cystic fibrosis [124], X fragile syndrome [107], spinal muscular atrophy [106], cancers [77] and thalassemia [105]. DBS, which is a fairly inexpensive sampling and storage method, is also a good choice for genetic material biobanks [125]. For instance, the Danish national biobank for neonatal screening includes over 2 million DBS which virtually corresponds to all Danish people born since 1982.

Conclusions

The use of DBS has many advantages in terms of sampling, transportation, storage and biosafety when compared to classical collection methods. One interesting aspect of DBS is the possibility of simplified “self/home blood sampling”. The patient will be able to independently and safely collect a blood sample. The DBS will then be sent to the laboratory by mail. As described in this review, many clinical analytes are already available on DBS, and more are to follow, thanks to innovative approaches. Indeed, development of microfluidics, multiplex immunological/genomic detection systems, mass spectrometry and automated DBS processing open new interesting clinical prospects. The detection and follow-up of metabolic, infectious and chronic diseases could therefore rely on the use of DBS. Both the patient and society could benefit from this technology. Already, several public and commercial laboratories in both Europe and USA are offering DBS kits for a broad range of analytes often grouped into panels for hormonal, metabolic or cardiovascular diseases. This evolution could dramatically change how clinical chemistry pre-analytics are handled in the future.


Corresponding author: Sylvain Lehmann, CHU Montpellier, IRB, 80 Avenue Augustin Fliche, Montpellier 34295, France, E-mail:

The authors thank Rachel Almeras, Bader Al Taweel, Domitille Héron and Thibault Fortane for their initial help in the writing of this review and Brigitte Lehmann for editing the manuscript.

Conflict of interest statement

Authors’ conflict of interest disclosure: The authors stated that there are no conflicts of interest regarding the publication of this article.

Research funding: None declared.

Employment or leadership: None declared.

Honorarium: None declared.

References

1. Bang I. Ein verfahren zur mikrobestimmung von blutbestandteilen. Biochem Ztschr 1913;49:19–39.Search in Google Scholar

2. Guthrie R, Susi A. A simple phenylalanine method for detecting phenylketonuria in large populations of newborn infants. Pediatrics 1963;32:338–43.10.1542/peds.32.3.338Search in Google Scholar PubMed

3. Mei JV, Alexander JR, Adam BW, Hannon WH. Use of filter paper for the collection and analysis of human whole blood specimens. J Nutr 2001;131:1631S–6S.10.1093/jn/131.5.1631SSearch in Google Scholar

4. Parker SP, Cubitt WD. The use of the dried blood spot sample in epidemiological studies. J Clin Pathol 1999;52:633–9.10.1136/jcp.52.9.633Search in Google Scholar PubMed

5. Costa X, Jardi R, Rodriguez F, Miravitlles M, Cotrina M, Gonzalez C, et al. Simple method for alpha1-antitrypsin deficiency screening by use of dried blood spot specimens. Eur Respir J 2000;15:1111–5.10.1034/j.1399-3003.2000.01521.xSearch in Google Scholar

6. Xu H, Zhao Y, Liu Z, Zhu W, Zhou Y, Zhao Z. Bisulfite genomic sequencing of DNA from dried blood spot microvolume samples. Forensic Sci Int Genet 2012;6:306–9.10.1016/j.fsigen.2011.06.007Search in Google Scholar PubMed

7. Tuaillon E, Mondain AM, Meroueh F, Ottomani L, Picot MC, Nagot N, et al. Dried blood spot for hepatitis C virus serology and molecular testing. Hepatology 2010;51:752–8.10.1002/hep.23407Search in Google Scholar PubMed

8. Uttayamakul S, Likanonsakul S, Sunthornkachit R, Kuntiranont K, Louisirirotchanakul S, Chaovavanich A, et al. Usage of dried blood spots for molecular diagnosis and monitoring HIV-1 infection. J Virol Methods 2005;128:128–34.10.1016/j.jviromet.2005.04.010Search in Google Scholar PubMed

9. Little RR, Wiedmeyer HM, England JD, Knowler WC, Goldstein DE. Measurement of glycosylated whole-blood protein for assessing glucose control in diabetes: collection and storage of capillary blood on filter paper. Clin Chem 1985;31:213–6.10.1093/clinchem/31.2.213Search in Google Scholar PubMed

10. Caggana M, Conroy JM, Pass KA. Rapid, efficient method for multiplex amplification from filter paper. Hum Mutat 1998;11:404–9.10.1002/(SICI)1098-1004(1998)11:5<404::AID-HUMU8>3.0.CO;2-SSearch in Google Scholar PubMed

11. Strenger V, Pfurtscheller K, Wendelin G, Aberle SW, Nacheva EP, Zohrer B, et al. Differentiating inherited human herpesvirus type 6 genome from primary human herpesvirus type 6 infection by means of dried blood spot from the newborn screening card. J Pediatr 2011;159:859–61.10.1016/j.jpeds.2011.06.032Search in Google Scholar

12. Lewensohn-Fuchs I, Osterwall P, Forsgren M, Malm G. Detection of herpes simplex virus DNA in dried blood spots making a retrospective diagnosis possible. J Clin Virol 2003;26:39–48.10.1016/S1386-6532(02)00019-7Search in Google Scholar

13. De Crignis E, Re MC, Cimatti L, Zecchi L, Gibellini D. HIV-1 and HCV detection in dried blood spots by SYBR green multiplex real-time RT-PCR. J Virol Methods 2010;165:51–6.10.1016/j.jviromet.2009.12.017Search in Google Scholar PubMed

14. Jardi R, Rodriguez-Frias F, Buti M, Schaper M, Valdes A, Martinez M, et al. Usefulness of dried blood samples for quantification and molecular characterization of HBV-DNA. Hepatology 2004;40:133–9.10.1002/hep.20275Search in Google Scholar PubMed

15. Gohring K, Dietz K, Hartleif S, Jahn G, Hamprecht K. Influence of different extraction methods and PCR techniques on the sensitivity of HCMV-DNA detection in dried blood spot (DBS) filter cards. J Clin Virol 2010;48:278–81.10.1016/j.jcv.2010.04.011Search in Google Scholar PubMed

16. Scanga L, Chaing S, Powell C, Aylsworth AS, Harrell LJ, Henshaw NG, et al. Diagnosis of human congenital cytomegalovirus infection by amplification of viral DNA from dried blood spots on perinatal cards. J Mol Diagn 2006;8:240–5.10.2353/jmoldx.2006.050075Search in Google Scholar PubMed PubMed Central

17. Yourno J, Conroy J. A novel polymerase chain reaction method for detection of human immunodeficiency virus in dried blood spots on filter paper. J Clin Microbiol 1992;30:2887–92.10.1128/jcm.30.11.2887-2892.1992Search in Google Scholar PubMed PubMed Central

18. Barin F, Plantier JC, Brand D, Brunet S, Moreau A, Liandier B, et al. Human immunodeficiency virus serotyping on dried serum spots as a screening tool for the surveillance of the aids epidemic. J Med Virol 2006;78(Suppl 1):S13–8.10.1002/jmv.20600Search in Google Scholar PubMed

19. Brindle E, Fujita M, Shofer J, O′Connor KA. Serum, plasma, and dried blood spot high-sensitivity C-reactive protein enzyme immunoassay for population research. J Immunol Methods 2010;362:112–20.10.1016/j.jim.2010.09.014Search in Google Scholar PubMed PubMed Central

20. Cowans NJ, Stamatopoulou A, Liitti P, Suonpaa M, Spencer K. The stability of free-beta human chorionic gonadotrophin and pregnancy-associated plasma protein-A in first trimester dried blood spots. Prenatal Diagn 2011;31:293–8.10.1002/pd.2709Search in Google Scholar PubMed

21. Worthman CM, Stallings JF. Measurement of gonadotropins in dried blood spots. Clin Chem 1994;40:448–53.10.1093/clinchem/40.3.448Search in Google Scholar PubMed

22. Hoffman DL. Purification and large-scale preparation of antithrombin III. Am J Med 1989;87:23S–6S.10.1016/0002-9343(89)80527-3Search in Google Scholar PubMed

23. Mitchell ML, Hermos RJ, Moses AC. Radioimmunoassay of somatomedin-C in filter paper discs containing dried blood. Clin Chem 1987;33:536–8.10.1093/clinchem/33.4.536Search in Google Scholar PubMed

24. Wang XL, Dudman NP, Blades BL, Wilcken DE. Changes in the immunoreactivity of APO A-I during storage. Clin Chim Acta 1989;179:285–93.10.1016/0009-8981(89)90091-0Search in Google Scholar PubMed

25. Macri JN, Anderson RW, Krantz DA, Larsen JW, Buchanan PD. Prenatal maternal dried blood screening with alpha-fetoprotein and free beta-human chorionic gonadotropin for open neural tube defect and down syndrome. Am J Obstet Gynecol 1996;174:566–72.10.1016/S0002-9378(96)70429-5Search in Google Scholar PubMed

26. Yamaguchi A, Fukushi M, Arai O, Mizushima Y, Sato Y, Shimizu Y, et al. A simple method for quantification of biotinidase activity in dried blood spot and its application to screening of biotinidase deficiency. Tohoku J Exp Med 1987;152:339–46.10.1620/tjem.152.339Search in Google Scholar PubMed

27. Song EY, Vandunk C, Kuddo T, Nelson PG. Measurement of CGRP in dried blood spots using a modified sandwich enzyme immunoassay. J Neurosci Methods 2006;155:92–7.10.1016/j.jneumeth.2005.12.020Search in Google Scholar PubMed

28. deWilde A, Sadilkova K, Sadilek M, Vasta V, Hahn SH. Tryptic peptide analysis of ceruloplasmin in dried blood spots using liquid chromatography-tandem mass spectrometry: application to newborn screening. Clin Chem 2008;54:1961–8.10.1373/clinchem.2008.111989Search in Google Scholar PubMed

29. O′Broin SD, Gunter EW. Screening of folate status with use of dried blood spots on filter paper. Am J Clin Nutr 1999;70:359–67.10.1093/ajcn/70.3.359Search in Google Scholar PubMed

30. Lakshmy R, Gupta R. Measurement of glycated hemoglobin A1c from dried blood by turbidimetric immunoassay. J Diabetes Sci Technol 2009;3:1203–6.10.1177/193229680900300527Search in Google Scholar PubMed PubMed Central

31. Daniel YA, Turner C, Haynes RM, Hunt BJ, Dalton RN. Quantification of hemoglobin A2 by tandem mass spectrometry. Clin Chem 2007;53:1448–54.10.1373/clinchem.2007.088682Search in Google Scholar PubMed

32. Jacomelli G, Micheli V, Peruzzi L, Notarantonio L, Cerboni B, Sestini S, et al. Simple non-radiochemical HPLC-linked method for screening for purine metabolism disorders using dried blood spot. Clin Chim Acta 2002;324:135–9.10.1016/S0009-8981(02)00243-7Search in Google Scholar PubMed

33. Wang D, Wood T, Sadilek M, Scott CR, Turecek F, Gelb MH. Tandem mass spectrometry for the direct assay of enzymes in dried blood spots: application to newborn screening for mucopolysaccharidosis II (Hunter disease). Clin Chem 2007;53:137–40.10.1373/clinchem.2006.077263Search in Google Scholar PubMed

34. Diamandi A, Khosravi MJ, Mistry J, Martinez V, Guevara-Aguirre J. Filter paper blood spot assay of human insulin-like growth factor I (IGF-I) and IGF-binding protein-3 and preliminary application in the evaluation of growth hormone status. J Clin Endocrinol Metab 1998;83:2296–301.10.1210/jc.83.7.2296Search in Google Scholar PubMed

35. Fisher RS, Chan DW, Bare M, Lesser RP. Capillary prolactin measurement for diagnosis of seizures. Ann Neurol 1991;29:187–90.10.1002/ana.410290212Search in Google Scholar PubMed

36. McDade TW, Shell-Duncan B. Whole blood collected on filter paper provides a minimally invasive method for assessing human transferrin receptor level. J Nutr 2002;132:3760–3.10.1093/jn/132.12.3760Search in Google Scholar PubMed

37. Zimmermann MB, Moretti D, Chaouki N, Torresani T. Development of a dried whole-blood spot thyroglobulin assay and its evaluation as an indicator of thyroid status in goitrous children receiving iodized salt. Am J Clin Nutr 2003;77:1453–8.10.1093/ajcn/77.6.1453Search in Google Scholar PubMed

38. Mwaba P, Cassol S, Pilon R, Chintu C, Janes M, Nunn A, et al. Use of dried whole blood spots to measure CD4+ lymphocyte counts in HIV-1-infected patients. Lancet 2003;362:1459–60.10.1016/S0140-6736(03)14693-4Search in Google Scholar

39. Helfand RF, Keyserling HL, Williams I, Murray A, Mei J, Moscatiello C, et al. Comparative detection of measles and rubella IGM and IGG derived from filter paper blood and serum samples. J Med Virol 2001;65:751–7.10.1002/jmv.2100Search in Google Scholar PubMed

40. Sorensen T, Spenter J, Jaliashvili I, Christiansen M, Norgaard-Pedersen B, Petersen E. Automated time-resolved immunofluorometric assay for toxoplasma gondii-specific IGM and IGA antibodies: study of more than 130,000 filter-paper blood-spot samples from newborns. Clin Chem 2002;48:1981–6.10.1093/clinchem/48.11.1981Search in Google Scholar

41. Dowlati B, Dunhardt PA, Smith MM, Shaheb S, Stuart CA. Quantification of insulin in dried blood spots. J Lab Clin Med 1998;131:370–4.10.1016/S0022-2143(98)90188-3Search in Google Scholar PubMed

42. Chamoles NA, Niizawa G, Blanco M, Gaggioli D, Casentini C. Glycogen storage disease type II: enzymatic screening in dried blood spots on filter paper. Clin Chim Acta 2004;347:97–102.10.1016/j.cccn.2004.04.009Search in Google Scholar PubMed

43. Chamoles NA, Blanco MB, Gaggioli D, Casentini C. Hurler-like phenotype: enzymatic diagnosis in dried blood spots on filter paper. Clin Chem 2001;47:2098–102.10.1093/clinchem/47.12.2098Search in Google Scholar PubMed

44. Chamoles NA, Blanco M, Gaggioli D. Diagnosis of alpha-l-iduronidase deficiency in dried blood spots on filter paper: the possibility of newborn diagnosis. Clin Chem 2001;47:780–1.10.1093/clinchem/47.4.780Search in Google Scholar PubMed

45. ten Brink HJ, van den Heuvel CM, Christensen E, Largilliere C, Jakobs C. Diagnosis of peroxisomal disorders by analysis of phytanic and pristanic acids in stored blood spots collected at neonatal screening. Clin Chem 1993;39:1904–6.10.1093/clinchem/39.9.1904Search in Google Scholar

46. Vladutiu GD, Glueck CJ, Schultz MT, McNeely S, Guthrie R. Beta-lipoprotein quantitation in cord blood spotted on filter paper: a screening test. Clin Chem 1980;26:1285–90.10.1093/clinchem/26.9.1285Search in Google Scholar PubMed

47. Laberge C, Grenier A, Valet JP, Morissette J. Fumarylacetoacetase measurement as a mass-screening procedure for hereditary tyrosinemia type I. Am J Hum Genet 1990;47:325–8.Search in Google Scholar PubMed

48. Skogstrand K, Ekelund CK, Thorsen P, Vogel I, Jacobsson B, Norgaard-Pedersen B, et al. Effects of blood sample handling procedures on measurable inflammatory markers in plasma, serum and dried blood spot samples. J Immunol Methods 2008;336:78–84.10.1016/j.jim.2008.04.006Search in Google Scholar PubMed

49. Tanner S, McDade TW. Enzyme immunoassay for total immunoglobulin E in dried blood spots. Am J Human Biol 2007;19:440–2.10.1002/ajhb.20635Search in Google Scholar PubMed

50. Fachiroh J, Prasetyanti PR, Paramita DK, Prasetyawati AT, Anggrahini DW, Haryana SM, et al. Dried-blood sampling for epstein-barr virus immunoglobulin g (IGG) and IGA serology in nasopharyngeal carcinoma screening. J Clin Microbiol 2008;46:1374–80.10.1128/JCM.01368-07Search in Google Scholar PubMed PubMed Central

51. Chamoles NA, Blanco MB, Iorcansky S, Gaggioli D, Specola N, Casentini C. Retrospective diagnosis of GM1 gangliosidosis by use of a newborn-screening card. Clin Chem 2001;47:2068–9.10.1093/clinchem/47.11.2068Search in Google Scholar

52. Xu YY, Pettersson K, Blomberg K, Hemmila I, Mikola H, Lovgren T. Simultaneous quadruple-label fluorometric immunoassay of thyroid-stimulating hormone, 17 alpha-hydroxyprogesterone, immunoreactive trypsin, and creatine kinase MM isoenzyme in dried blood spots. Clin Chem 1992;38:2038–43.10.1093/clinchem/38.10.2038Search in Google Scholar

53. Dussault JH, Morissette J, Letarte J, Guyda H, Laberge C. Thyroxine-binding globulin capacity and concentration evaluated from blood spots on filter-paper in a screening program for neonatal hypothyroidism. Clin Chem 1980;26:463–5.10.1093/clinchem/26.3.463Search in Google Scholar

54. Kirby LT, Applegarth DA, Davidson AG, Wong LT, Hardwick DF. Use of a dried blood spot in immunoreactive-trypsin assay for detection of cystic fibrosis in infants. Clin Chem 1981;27:678–8.10.1093/clinchem/27.5.678Search in Google Scholar PubMed

55. de Almeida LM, Azevedo RS, Guimaraes AA, Coutinho Eda S, Struchiner CJ, Massad E. Detection of antibodies against hepatitis a virus in eluates of blood spotted on filter-paper: a pilot study in Rio De Janeiro, Brazil. Trans R Soc Trop Med Hyg 1999;93:401–4.10.1016/S0035-9203(99)90133-5Search in Google Scholar PubMed

56. Gil A, Gonzalez A, Dal-Re R, Dominguez V, Astasio P, Aguilar L. Detection of antibodies against hepatitis a in blood spots dried on filter paper. Is this a reliable method for epidemiological studies? Epidemiol Infect 1997;118:189–91.10.1017/S0950268896007297Search in Google Scholar PubMed

57. Villar LM, de Oliveira JC, Cruz HM, Yoshida CF, Lampe E, Lewis-Ximenez LL. Assessment of dried blood spot samples as a simple method for detection of hepatitis B virus markers. J Med Virol 2011;83:1522–9.10.1002/jmv.22138Search in Google Scholar PubMed

58. Tappin DM, Greer K, Cameron S, Kennedy R, Brown AJ, Girdwood RW. Maternal antibody to hepatitis B core antigen detected in dried neonatal blood spot samples. Epidemiol Infect 1998;121:387–90.10.1017/S0950268898001393Search in Google Scholar PubMed PubMed Central

59. Judd A, Parry J, Hickman M, McDonald T, Jordan L, Lewis K, et al. Evaluation of a modified commercial assay in detecting antibody to hepatitis C virus in oral fluids and dried blood spots. J Med Virol 2003;71:49–55.10.1002/jmv.10463Search in Google Scholar PubMed

60. Parker SP, Khan HI, Cubitt WD. Detection of antibodies to hepatitis C virus in dried blood spot samples from mothers and their offspring in Lahore, Pakistan. J Clin Microbiol 1999;37:2061–3.10.1128/JCM.37.6.2061-2063.1999Search in Google Scholar PubMed PubMed Central

61. Corran PH, Cook J, Lynch C, Leendertse H, Manjurano A, Griffin J, et al. Dried blood spots as a source of anti-malarial antibodies for epidemiological studies. Malar J 2008;7:195–207.10.1186/1475-2875-7-195Search in Google Scholar PubMed PubMed Central

62. Thanasekaraan V, Wiseman MS, Rayner RJ, Hiller EJ, Shale DJ. Pseudomonas aeruginosa antibodies in blood spots from patients with cystic fibrosis. Arch Dis Child 1989;64:1599–603.10.1136/adc.64.11.1599Search in Google Scholar PubMed PubMed Central

63. Hofman LF, Foley TP, Henry JJ, Naylor EW. The use of filter paper-dried blood spots for thyroid-antibody screening in adults. J Lab Clin Med 2004;144:307–12.10.1016/j.lab.2004.09.009Search in Google Scholar PubMed

64. Hong HA, Ke NT, Nhon TN, Thinh ND, van der Gun JW, Hendriks JT, et al. Validation of the combined toxin-binding inhibition test for determination of neutralizing antibodies against tetanus and diphtheria toxins in a vaccine field study in Vietnam. Bull World Health Organ 1996;74:275–82.Search in Google Scholar

65. Takkouche B, Iglesias J, Alonso-Fernandez JR, Fernandez-Gonzalez C, Gestal-Otero JJ. Detection of brucella antibodies in eluted dried blood: a validation study. Immunol Letters 1995;45:107–8.10.1016/0165-2478(94)00247-OSearch in Google Scholar

66. Peralta RH, Macedo HW, Vaz AJ, Machado LR, Peralta JM. Detection of anti-cysticercus antibodies by ELISA using whole blood collected on filter paper. Trans R Soc Trop Med Hyg 2001;95:35–6.10.1016/S0035-9203(01)90324-4Search in Google Scholar PubMed

67. de la Fuente L, Toro C, Soriano V, Brugal MT, Vallejo F, Barrio G, et al. HTLV infection among young injection and non-injection heroin users in Spain: prevalence and correlates. J Clin Virol 2006;35:244–9.10.1016/j.jcv.2005.06.006Search in Google Scholar

68. Fenollar F, Raoult D. Diagnosis of Rickettsial diseases using samples dried on blotting paper. Clin Diagn Lab Immunol 1999;6:483–8.10.1128/CDLI.6.4.483-488.1999Search in Google Scholar PubMed

69. Stevens R, Pass K, Fuller S, Wiznia A, Noble L, Duva S, et al. Blood spot screening and confirmatory tests for syphilis antibody. J Clin Microbiol 1992;30:2353–8.10.1128/jcm.30.9.2353-2358.1992Search in Google Scholar PubMed

70. Backhouse JL. Dried blood spot technique for detecting treponema infection. Trans R Soc Trop Med Hyg 1998;92:469–76.10.1016/S0035-9203(98)91098-7Search in Google Scholar PubMed

71. Zicker F, Smith PG, Luquetti AO, Oliveira OS. Mass screening for trypanosoma cruzi infections using the immunofluorescence, ELISA and haemagglutination tests on serum samples and on blood eluates from filter-paper. Bull World Health Organ 1990;68:465–71.Search in Google Scholar PubMed

72. Mason PR, Fiori PL, Cappuccinelli P, Rappelli P, Gregson S. Seroepidemiology of trichomonas vaginalis in rural women in Zimbabwe and patterns of association with HIV infection. Epidemiol Infect 2005;133:315–23.10.1017/S0950268804003127Search in Google Scholar PubMed PubMed Central

73. Fujimoto A, Okano Y, Miyagi T, Isshiki G, Oura T. Quantitative beutler test for newborn mass screening of galactosemia using a fluorometric microplate reader. Clin Chem 2000;46:806–10.10.1093/clinchem/46.6.806Search in Google Scholar PubMed

74. Hardelid P, Williams D, Dezateux C, Cubitt WD, Peckham CS, Tookey PA, et al. Agreement of rubella IGG antibody measured in serum and dried blood spots using two commercial enzyme-linked immunosorbent assays. J Med Virol 2008;80:360–4.10.1002/jmv.21077Search in Google Scholar PubMed

75. Balmaseda A, Saborio S, Tellez Y, Mercado JC, Perez L, Hammond SN, et al. Evaluation of immunological markers in serum, filter-paper blood spots, and saliva for dengue diagnosis and epidemiological studies. J Clin Virol 2008;43:287–91.10.1016/j.jcv.2008.07.016Search in Google Scholar PubMed

76. Sorensen KM, Agergaard P, Olesen C, Andersen PS, Larsen LA, Ostergaard JR, et al. Detecting 22q11.2 deletions by use of multiplex ligation-dependent probe amplification on DNA from neonatal dried blood spot samples. J Mol Diagn 2010;12:147–51.10.2353/jmoldx.2010.090099Search in Google Scholar

77. Klotz J, Bryant P, Wilcox HB, Dillon M, Wolf B, Fagliano J. Population-based retrieval of newborn dried blood spots for researching paediatric cancer susceptibility genes. Paediatr Perinat Epidemiol 2006;20:449–52.10.1111/j.1365-3016.2006.00749.xSearch in Google Scholar PubMed

78. Waterboer T, Dondog B, Michael KM, Michel A, Schmitt M, Vaccarella S, et al. Dried blood spot samples for seroepidemiology of infections with human papillomaviruses, helicobacter pylori, hepatitis C virus, and JC virus. Cancer Epidemiol Biomarkers Prev 2012;21:287–93.10.1158/1055-9965.EPI-11-1001Search in Google Scholar PubMed

79. Quraishi R, Lakshmy R, Prabhakaran D, Mukhopadhyay AK, Jailkhani B. Use of filter paper stored dried blood for measurement of triglycerides. Lipids Health Disease 2006;5:20.10.1186/1476-511X-5-20Search in Google Scholar

80. Zytkovicz TH, Fitzgerald EF, Marsden D, Larson CA, Shih VE, Johnson DM, et al. Tandem mass spectrometric analysis for amino, organic, and fatty acid disorders in newborn dried blood spots: a two-year summary from the New England newborn screening program. Clin Chem 2001;47:1945–55.10.1093/clinchem/47.11.1945Search in Google Scholar PubMed

81. Accinni R, Campolo J, Parolini M, De Maria R, Caruso R, Maiorana A, et al. Newborn screening of homocystinuria: quantitative analysis of total homocyst(e)ine on dried blood spot by liquid chromatography with fluorimetric detection. J Chromatogr B Analyt Technol Biomed Life Sci 2003;785:219–26.10.1016/S1570-0232(02)00852-8Search in Google Scholar

82. Burrin JM, Price CP. Performance of three enzymic methods for filter paper glucose determination. Ann Clin Biochem 1984;21( Pt 5):411–6.10.1177/000456328402100513Search in Google Scholar PubMed

83. Lacey JM, Minutti CZ, Magera MJ, Tauscher AL, Casetta B, McCann M, et al. Improved specificity of newborn screening for congenital adrenal hyperplasia by second-tier steroid profiling using tandem mass spectrometry. Clin Chem 2004;50:621–5.10.1373/clinchem.2003.027193Search in Google Scholar PubMed

84. Erhardt JG, Craft NE, Heinrich F, Biesalski HK. Rapid and simple measurement of retinol in human dried whole blood spots. J Nutr 2002;132:318–21.10.1093/jn/132.2.318Search in Google Scholar PubMed

85. Chace DH, Singleton S, Diperna J, Aiello M, Foley T. Rapid metabolic and newborn screening of thyroxine (t4) from dried blood spots by MS/MS. Clin Chim Acta 2009;403:178–83.10.1016/j.cca.2009.02.012Search in Google Scholar

86. Pacchiarotti A, Bartalena L, Falcone M, Buratti L, Grasso L, Martino E, et al. Free thyroxine and free triiodothyronine measurement in dried blood spots on filter paper by column adsorption chromatography followed by radioimmunoassay. Horm Metab Res 1988;20:293–7.10.1055/s-2007-1010818Search in Google Scholar PubMed

87. Schulze A, Schmidt C, Kohlmuller D, Hoffmann GF, Mayatepek E. Accurate measurement of free carnitine in dried blood spots by isotope-dilution electrospray tandem mass spectrometry without butylation. Clin Chim Acta 2003;335:137–45.10.1016/S0009-8981(03)00292-4Search in Google Scholar PubMed

88. Kuhara T, Ohse M, Inoue Y, Yorifuji T, Sakura N, Mitsubuchi H, et al. Gas chromatographic-mass spectrometric newborn screening for propionic acidaemia by targeting methylcitrate in dried filter-paper urine samples. J Inherit Metab Dis 2002;25:98–106.10.1023/A:1015620609075Search in Google Scholar PubMed

89. Kimura M, Yoon HR, Wasant P, Takahashi Y, Yamaguchi S. A sensitive and simplified method to analyze free fatty acids in children with mitochondrial beta oxidation disorders using gas chromatography/mass spectrometry and dried blood spots. Clin Chim Acta 2002;316:117–21.10.1016/S0009-8981(01)00741-0Search in Google Scholar PubMed

90. Allard P, Grenier A, Korson MS, Zytkovicz TH. Newborn screening for hepatorenal tyrosinemia by tandem mass spectrometry: analysis of succinylacetone extracted from dried blood spots. Clin Biochem 2004;37:1010–5.10.1016/j.clinbiochem.2004.07.006Search in Google Scholar PubMed

91. Carducci C, Santagata S, Leuzzi V, Artiola C, Giovanniello T, Battini R, et al. Quantitative determination of guanidinoacetate and creatine in dried blood spot by flow injection analysis-electrospray tandem mass spectrometry. Clin Chim Acta 2006;364:180–7.10.1016/j.cca.2005.06.016Search in Google Scholar PubMed

92. D′Avolio A, Simiele M, Siccardi M, Baietto L, Sciandra M, Bonora S, et al. HPLC-MS method for the quantification of nine anti-HIV drugs from dry plasma spot on glass filter and their long-term stability in different conditions. J Pharm Biomed Anal 2010;52:774–80.10.1016/j.jpba.2010.02.026Search in Google Scholar PubMed

93. Koal T, Burhenne H, Romling R, Svoboda M, Resch K, Kaever V. Quantification of antiretroviral drugs in dried blood spot samples by means of liquid chromatography/tandem mass spectrometry. Rapid Commun Mass Spectrom 2005;19:2995–3001.10.1002/rcm.2158Search in Google Scholar PubMed

94. Henderson LO, Powell MK, Hannon WH, Miller BB, Martin ML, Hanzlick RL, et al. Radioimmunoassay screening of dried blood spot materials for benzoylecgonine. J Anal Toxicol 1993;17:42–7.10.1093/jat/17.1.42Search in Google Scholar PubMed

95. Blessborn D, Romsing S, Bergqvist Y, Lindegardh N. Assay for screening for six antimalarial drugs and one metabolite using dried blood spot sampling, sequential extraction and ion-trap detection. Bioanalysis 2010;2:1839–47.10.4155/bio.10.147Search in Google Scholar PubMed

96. Lindkvist J, Malm M, Bergqvist Y. Straightforward and rapid determination of sulfadoxine and sulfamethoxazole in capillary blood on sampling paper with liquid chromatography and UV detection. Trans R Soc Trop Med Hyg 2009;103:371–6.10.1016/j.trstmh.2008.11.031Search in Google Scholar PubMed

97. Burse VW, DeGuzman MR, Korver MP, Najam AR, Williams CC, Hannon WH, et al. Preliminary investigation of the use of dried-blood spots for the assessment of in utero exposure to environmental pollutants. Biochem Mol Med 1997;61:236–9.10.1006/bmme.1997.2603Search in Google Scholar PubMed

98. Li PK, Lee JT, Conboy KA, Ellis EF. Fluorescence polarization immunoassay for theophylline modified for use with dried blood spots on filter paper. Clin Chem 1986;32:552–5.10.1093/clinchem/32.3.552Search in Google Scholar PubMed

99. Conroy JM, Trivedi G, Sovd T, Caggana M. The allele frequency of mutations in four genes that confer enhanced susceptibility to venous thromboembolism in an unselected group of New York State newborns. Thromb Res 2000;99:317–24.10.1016/S0049-3848(00)00254-1Search in Google Scholar

100. Bobillo Lobato J, Sanchez Peral BA, Duran Parejo P, Jimenez Jimenez LM. Detection of c. -32t>g (ivs1-13t>g) mutation of pompe disease by real-time PCR in dried blood spot specimen. Clin Chim Acta 2013;418C:107–8.10.1016/j.cca.2012.12.015Search in Google Scholar PubMed

101. Chien YH, Lee NC, Chiang SC, Desnick RJ, Hwu WL. Fabry disease: incidence of the common later-onset alpha-galactosidase a ivs4+919g–>a mutation in Taiwanese newborns–superiority of DNA-based to enzyme-based newborn screening for common mutations. Mol Med 2012;18:780–4.10.2119/molmed.2012.00002Search in Google Scholar PubMed PubMed Central

102. Abdallah MW, Larsen N, Grove J, Bonefeld-Jorgensen EC, Norgaard-Pedersen B, Hougaard DM, et al. Neonatal chemokine levels and risk of autism spectrum disorders: findings from a Danish historic birth cohort follow-up study. Cytokine 2012;61:370–6.10.1016/j.cyto.2012.11.015Search in Google Scholar PubMed

103. McCandless SE, Chandrasekar R, Linard S, Kikano S, Rice L. Sequencing from dried blood spots in infants with “false positive” newborn screen for MCAD deficiency. Mol Genet Metab 2013;108:51–5.10.1016/j.ymgme.2012.10.016Search in Google Scholar PubMed PubMed Central

104. Cordovado SK, Hendrix M, Greene CN, Mochal S, Earley MC, Farrell PM, et al. CFTR mutation analysis and haplotype associations in CF patients. Mol Genet Metab 2012;105: 249–54.10.1016/j.ymgme.2011.10.013Search in Google Scholar PubMed PubMed Central

105. Karthipan SN, George E, Jameela S, Lim WF, Teh LK, Lee TY, et al. An assessment of three noncommercial DNA extraction methods from dried blood spots for beta-thalassaemia mutation identification. Int J Lab Hematol 2011;33:540–4.10.1111/j.1751-553X.2011.01304.xSearch in Google Scholar PubMed

106. Harahap NI, Harahap IS, Kaszynski RH, Nurputra DK, Hartomo TB, Pham HT, et al. Spinal muscular atrophy patient detection and carrier screening using dried blood spots on filter paper. Genet Test Mol Biomarkers 2012;16:123–9.10.1089/gtmb.2011.0109Search in Google Scholar PubMed

107. Coffee B, Keith K, Albizua I, Malone T, Mowrey J, Sherman SL, et al. Incidence of fragile X syndrome by newborn screening for methylated FMR1 DNA. Am J Hum Genet 2009;85:503–14.10.1016/j.ajhg.2009.09.007Search in Google Scholar PubMed PubMed Central

108. Resnick L, Veren K, Salahuddin SZ, Tondreau S, Markham PD. Stability and inactivation of HTLV-III/LAV under clinical and laboratory environments. J Am Med Assoc 1986;255:1887–91.10.1001/jama.1986.03370140085029Search in Google Scholar

109. McDade TW, Williams S, Snodgrass JJ. What a drop can do: dried blood spots as a minimally invasive method for integrating biomarkers into population-based research. Demography 2007;44:899–925.10.1353/dem.2007.0038Search in Google Scholar PubMed

110. Burnett JE. Dried blood spot sampling: practical considerations and recommendation for use with preclinical studies. Bioanalysis 2011;3:1099–107.10.4155/bio.11.68Search in Google Scholar PubMed

111. Garcia Boy R, Henseler J, Mattern R, Skopp G. Determination of morphine and 6-acetylmorphine in blood with use of dried blood spots. Ther Drug Monit 2008;30:733–9.10.1097/FTD.0b013e31818d9fdbSearch in Google Scholar PubMed

112. Hollegaard MV, Grauholm J, Borglum A, Nyegaard M, Norgaard-Pedersen B, Orntoft T, et al. Genome-wide scans using archived neonatal dried blood spot samples. BMC Genomics 2009;10:297–303.10.1186/1471-2164-10-297Search in Google Scholar PubMed PubMed Central

113. O′Mara M, Hudson-Curtis B, Olson K, Yueh Y, Dunn J, Spooner N. The effect of hematocrit and punch location on assay bias during quantitative bioanalysis of dried blood spot samples. Bioanalysis 2011;3:2335–47.10.4155/bio.11.220Search in Google Scholar PubMed

114. Snijdewind IJ, van Kampen JJ, Fraaij PL, van der Ende ME, Osterhaus AD, Gruters RA. Current and future applications of dried blood spots in viral disease management. Antiviral Res 2012;93:309–21.10.1016/j.antiviral.2011.12.011Search in Google Scholar PubMed

115. Lehmann S, Hoofnagle A, Hochstrasser D, Brede C, Glueckmann M, Cocho JA, et al. Quantitative clinical chemistry proteomics (QCCP) using mass spectrometry: general characteristics and application. Clin Chem Lab Med 2012:1–16.10.1515/cclm-2012-0723Search in Google Scholar PubMed

116. Johansson J, Becker C, Persson NG, Fex M, Torn C. C-peptide in dried blood spots. Scand J Clin Lab Invest 2010;70:404–9.10.3109/00365513.2010.501113Search in Google Scholar PubMed

117. Chambers AG, Percy AJ, Yang J, Camenzind AG, Borchers CH. Multiplexed quantitation of endogenous proteins in dried blood spots by multiple reaction monitoring mass spectrometry. Mol Cell Proteomics 2012;12:781–91.10.1074/mcp.M112.022442Search in Google Scholar PubMed PubMed Central

118. Newman MS, Brandon TR, Groves MN, Gregory WL, Kapur S, Zava DT. A liquid chromatography/tandem mass spectrometry method for determination of 25-hydroxy vitamin D2 and 25-hydroxy vitamin D3 in dried blood spots: a potential adjunct to diabetes and cardiometabolic risk screening. J Diabetes Sci Technol 2009;3:156–62.10.1177/193229680900300118Search in Google Scholar PubMed PubMed Central

119. Ruhaak LR, Miyamoto S, Kelly K, Lebrilla CB. N-glycan profiling of dried blood spots. Anal Chem 2012;84:396–402.10.1021/ac202775tSearch in Google Scholar PubMed PubMed Central

120. Henderson LO, Powell MK, Hannon WH, Bernert JT, Jr., Pass KA, Fernhoff P, et al. An evaluation of the use of dried blood spots from newborn screening for monitoring the prevalence of cocaine use among childbearing women. Biochem Mol Med 1997;61:143–51.10.1006/bmme.1997.2609Search in Google Scholar PubMed

121. Stove CP, Ingels AS, De Kesel PM, Lambert WE. Dried blood spots in toxicology: from the cradle to the grave? Crit Rev Toxicol 2012;42:230–43.10.3109/10408444.2011.650790Search in Google Scholar PubMed

122. Saussereau E, Lacroix C, Gaulier JM, Goulle JP. On-line liquid chromatography/tandem mass spectrometry simultaneous determination of opiates, cocainics and amphetamines in dried blood spots. J Chromatogr B Analyt Technol Biomed Life Sci 2012;885–886:1–7.10.1016/j.jchromb.2011.11.035Search in Google Scholar PubMed

123. McCabe ER, Huang SZ, Seltzer WK, Law ML. DNA microextraction from dried blood spots on filter paper blotters: potential applications to newborn screening. Hum Genet 1987;75:213–6.10.1007/BF00281061Search in Google Scholar PubMed

124. Makowski GS, Aslanzadeh J, Hopfer SM. In situ PCR amplification of guthrie card DNA to detect cystic fibrosis mutations. Clin Chem 1995;41:477–9.10.1093/clinchem/41.3.477aSearch in Google Scholar PubMed

125. Sjoholm MI, Dillner J, Carlson J. Assessing quality and functionality of DNA from fresh and archival dried blood spots and recommendations for quality control guidelines. Clin Chem 2007;53:1401–7.10.1373/clinchem.2007.087510Search in Google Scholar PubMed

Received: 2013-03-26
Accepted: 2013-04-19
Published Online: 2013-06-01
Published in Print: 2013-10-01

©2013 by Walter de Gruyter Berlin Boston

Scroll Up Arrow