Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Clinical Chemistry and Laboratory Medicine (CCLM)

Published in Association with the European Federation of Clinical Chemistry and Laboratory Medicine (EFLM)

Editor-in-Chief: Plebani, Mario

Ed. by Gillery, Philippe / Greaves, Ronda / Lackner, Karl J. / Lippi, Giuseppe / Melichar, Bohuslav / Payne, Deborah A. / Schlattmann, Peter

IMPACT FACTOR 2017: 3.556

CiteScore 2017: 2.34

SCImago Journal Rank (SJR) 2017: 1.114
Source Normalized Impact per Paper (SNIP) 2017: 1.188

See all formats and pricing
More options …
Volume 44, Issue 9


Lower expression of the α2,3-sialylated fibronectin glycoform and appearance of the asialo-fibronectin glycoform are associated with high concentrations of fibronectin in human seminal plasma with abnormal semen parameters

Iwona Kątnik-Prastowska / Ewa M. Kratz / Ricardo Faundez / Anna Chełmońska-Soyta
  • Laboratory of Reproductive Immunology, Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-09-08 | DOI: https://doi.org/10.1515/CCLM.2006.193


Background: Sialic acid isoforms expressed on glycoconjugates are known to be involved in different biological functions. The aim of this study was to compare α2,3- and/or α2,6-linked sialic acid expression on fibronectin in the seminal plasma of male partners from infertile couples. The data obtained were analyzed in relation to normal and abnormal semen parameters, as well as to fibronectin concentrations.

Methods: Fibronectin concentrations were determined by ELISA using a specific monoclonal antibody. The relative degree of sialic acid linked to fibronectin glycans either by α2,3 or α2,6 isomeric linkage was estimated by lectin-fibronectin ELISA utilizing lectins from Maackia amurensis and Sambucus nigra, respectively.

Results: High seminal fibronectin concentration was more frequently associated with abnormal semen parameters. The glycans of seminal plasma fibronectin, in contrast to blood plasma fibronectin, contained sialic acid more frequently attached by α2,3 than by α2,6 isomeric linkage. The relative amounts of both α2,3- and α2,6-linked sialic acid fibronectin isoforms were lower in the seminal plasma of men suspected of infertility.

Conclusions: Seminal fibronectin showed an oncofetal type of sialylation and the distribution of hypo- and asialylated fibronectin glycoforms were associated with abnormal semen parameters and with high concentrations of fibronectin.

Clin Chem Lab Med 2006;44:1119–25.

Keywords: fibrin-heparin fibronectin domain; fibronectin glycoforms; infertility; seminal plasma; sialylation


  • 1.

    Hynes RO. The dynamic dialogue between cells and matrices: implication of fibronectin's elasticity. Proc Natl Acad Sci USA 1999; 96:2588–90.CrossrefGoogle Scholar

  • 2.

    Wierzbicka-Patynowski I, Schwarzbauer JE. The ins and outs of fibronectin matrix assembly. J Cell Sci 2003; 116:3269–76.Google Scholar

  • 3.

    Pankov R, Yamada KM. Fibronectin at a glance. J Cell Sci 2002; 115:3861–3.Google Scholar

  • 4.

    Stauffer CW, Parsons CL. Fibronectin levels in male ejaculate and evidence for its role in unexplained infertility. Urology 1989; 34:80–5.CrossrefGoogle Scholar

  • 5.

    Wennemuth G, Meinhardt A, Mallidis C, Albrecht M, Krause W, Renneberg H, et al. Assessment of fibronectin as a potential new clinical tool in andrology. Andrologia 2001; 33:43–6.Google Scholar

  • 6.

    Ffrench-Constant C. Alternative splicing of fibronectin – many different proteins but few different functions. Exp Cell Res 1995; 21:261–71.CrossrefGoogle Scholar

  • 7.

    Leitich H, Egarter C, Kaider A, Hohlagschwandtner M, Berghammer P, Husslein P. Cervicovaginal fetal fibronectin as a marker for preterm delivery: a meta-analysis. Am J Obstet Gynecol 1998; 180:1169–76.Google Scholar

  • 8.

    Hampel DJ, Köttgen B, Dudenhausen JW, Köttgen E. Fetal fibronectin as a marker for an imminent (preterm) delivery. A new technique using the glycoprotein lectin immunosorbent assay. J Immunol Methods 1999; 224:31–42.Google Scholar

  • 9.

    Krusius T, Fukuda M, Dell A, Ruoslahti E. Structure of the carbohydrate units of human amniotic fluid fibronectin. J Biol Chem 1985; 260:4110–6.Google Scholar

  • 10.

    Fukuda M, Levery SB, Hakomori S. Carbohydrate structure of hamster plasma fibronectin. Evidence for chemical diversity between cellular and plasma fibronectins. J Biol Chem 1982; 257:6856–60.Google Scholar

  • 11.

    Takamoto M, Endo T, Isemura M, Kochibe N, Kobata A. Structure of asparagine-linked oligosaccharides of human placental fibronectin. J Biochem 1989; 105:742–50.Google Scholar

  • 12.

    Bernard BA, Yamada KM, Olden K. Carbohydrates selectively protect a specific domain of fibronectin against proteases. J Biol Chem 1982; 257:8549–54.Google Scholar

  • 13.

    Carsons S, Lavietes BB, Slomiany A, Diamond HS, Berkowitz E. Carbohydrate heterogeneity of fibronectins. Synovial fluid fibronectin resembles the form secreted by cultured synoviocytes but differs from the plasma form. J Clin Invest 1987; 80:1342–9.Google Scholar

  • 14.

    Garat Ch, Kheradmand F, Albertine KH, Folkesson HG, Matthay MA. Soluble and insoluble fibronectin increases alveolar epithelial would healing in vitro. Lung Cell Mol Physiol 1996; 15:L844–53.Google Scholar

  • 15.

    Romberger DJ. Fibronectin. Int J Biochem Cell Biol 1997; 29:939–43.CrossrefGoogle Scholar

  • 16.

    Wagner C, Bürger A, Radsak M, Blum S, Hug F, Hänsch GM. Fibronectin synthesis by activated T lymphocytes: up-regulation of a surface-associated isoform with signalling function. Immunology 2000; 99:532–9.Google Scholar

  • 17.

    Lilja H, Oldbring J, Rannevik G, Laurell CB. Seminal vesicle-secreted proteins and their reactions during gelation and liquefaction of human semen. J Clin Invest 1987; 80:281–5.Google Scholar

  • 18.

    Pinke LA, Swanlund DJ, Hensleigh HC, McCarthy JB, Roberts KP, Pryor JL. Analysis of fibronectin on human sperm. J Urol 1997; 158:936–41.Google Scholar

  • 19.

    Hoshi K, Sato A, Sasaki H, Tsuiki A, Yanagida K. Localization of fibronectin on the surface of human spermatozoa and relation to the sperm-egg interaction. Fertil Steril 1994; 61:542–7.CrossrefGoogle Scholar

  • 20.

    Kątnik-Prastowska I, Przybysz M, Chełmońska-Soyta A. Fibronectin fragments in human seminal plasma. Acta Biochem Polon 2005; 52:557–60.Google Scholar

  • 21.

    Hounsell E. Methods of glycoconjugate analysis. In: Gabius HJ, Gabius S, editors. Glycoscience. Status and perspectives. Weinheim: Chapman and Hall, 1997:15–29.Google Scholar

  • 22.

    Word Health Organization. WHO laboratory manual for the examination of human semen and sperm-cervical interactions. Cambridge: Cambridge University Press, 1999.Google Scholar

  • 23.

    Kątnik I, Jadach J, Krotkiewski H, Gerber J. Investigating the glycosylation of normal and ovarian cancer haptoglobins using digoxigenin-labeled lectins. Glycosyl Disease 1994; 1:97–104.Google Scholar

  • 24.

    Ferens-Sieczkowska M, Midro A, Mierzejewska-Iwanowska B, Zwierz K, Kątnik-Prastowska I. Haptoglobin glycoforms in a case of carbohydrate-deficient glycoprotein syndrome. Glycoconj J 1999; 16:573–7.Google Scholar

  • 25.

    Yamada K. Fibronectin peptides in cell migration and wound repair. J Clin Invest 2000; 105:1507–9.CrossrefGoogle Scholar

  • 26.

    Du Toit D, Bornman MS, Van der Merwe MP, du Plessis DJ. High seminal sialic acid concentrations I patients with severe teratozoospermia. Arch Androl 1992; 28:177–9.CrossrefGoogle Scholar

  • 27.

    Ichihara-Tanaka K, Titani K, Sekiguchi K. Role of the carboxyl-terminal Fib2 domain in fibronectin matrix assembly. J Cell Sci 1995; 108:906–15.Google Scholar

  • 28.

    Huleihel M, Lunenfeld E, Levy A, Potashnik G, Glezerman M. Distinct expression levels of cytokines and soluble cytokine receptors in seminal plasma of fertile and infertile men. Fertil Steril 1996; 1:135–9.Google Scholar

  • 29.

    Voskuyl AE, Emeis JJ, Hazes JM, Van Hogezand RA, Biemond I, Breedveld FC. Levels of circulating cellular fibronectin are increased in patients with rheumatoid vasculitis. Clin Exp Rheumatol 1998; 16:429–34.Google Scholar

  • 30.

    Vallejo V, Reyes-Leyva J, Hernandez J, Ramirez H, Delannoy P, Zenteno E. Differential expression of sialic acid on porcine organs during the maturation process. Comp Biochem Physiol B Biochem Mol Biol 2000; 126:415–24.Google Scholar

  • 31.

    Grosso M, Vitarelli E, Giuffre G, Tuccari G, Barresi G. Expression of Tn, sialosyl-Tn and T antigens in human foetal large intestine. Eur J Histochem 2000; 44:359–63.Google Scholar

  • 32.

    Orczyk-Pawiłowicz M, Floriański J, Zalewski J, Kątnik-Prastowska I. Relative amounts of sialic acid and fucose of amniotic fluid glycoconjugates in relation to pregnancy age. Glycoconj J 2005; 22:433–42.Google Scholar

  • 33.

    Takano T, Miyauchi A, Matsuzuka F, Kuma K, Amino N. Expression of oncofetal fibronectin messenger ribonucleic acid in fibroblasts in the thyroid: a possible cause of false positive results in molecular-based diagnosis of thyroid carcinomas. J Clin Endocrinol Metab 2000; 85:765–8.Google Scholar

  • 34.

    Tuo W, Bazer FW. Expression of oncofetal fibronectin in porcine conceptuses and uterus through gestation. Reprod Fertil Dev 1996; 8:1207–13.CrossrefGoogle Scholar

  • 35.

    Ugarova TP, Ljubimov AV, Deng L, Plow EF. Proteolysis regulates exposure of the IIICS-1 adhesive sequence in plasma fibronectin. Biochemistry 1996; 35:10913–21.Google Scholar

  • 36.

    Schauer R. Sialic acids: fascinating sugars in higher animals and man. Zoology 2004; 107:49–64.Google Scholar

About the article

Corresponding author: Prof. Dr. Iwona Kątnik-Prastowska, Department of Chemistry and Immunochemistry, Wrocław Medical University, Bujwida 44a, 50-345 Wrocław, Poland Phone: +48-71-3281648, Fax: +48-71-3281649,

Received: 2006-03-24

Accepted: 2006-06-02

Published Online: 2006-09-08

Published in Print: 2006-09-01

Citation Information: Clinical Chemistry and Laboratory Medicine (CCLM), Volume 44, Issue 9, Pages 1119–1125, ISSN (Online) 1437-4331, ISSN (Print) 1434-6621, DOI: https://doi.org/10.1515/CCLM.2006.193.

Export Citation

©2006 by Walter de Gruyter Berlin New York.Get Permission

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

Jana Vitku, Lucie Kolatorova, and Richard Hampl
Basic and Clinical Andrology, 2017, Volume 27, Number 1
Mayank Saraswat, Sakari Joenväärä, Anil Kumar Tomar, Sarman Singh, Savita Yadav, and Risto Renkonen
Journal of Proteome Research, 2016, Volume 15, Number 3, Page 991
Ewa Żurawska-Płaksej, Ewa Maria Kratz, Mirosława Ferens-Sieczkowska, Maria Knapik-Kordecka, and Agnieszka Piwowar
Glycoconjugate Journal, 2016, Volume 33, Number 1, Page 29
Ewa M. Kratz, Anna Kałuża, Mariusz Zimmer, and Mirosława Ferens-Sieczkowska
Disease Markers, 2015, Volume 2015, Page 1
Mirosława Ferens-Sieczkowska, Beata Kowalska, and Ewa Maria Kratz
Biomarkers, 2013, Volume 18, Number 1, Page 10
A. M. Attia, A. Hassan, A. Zalata, M. Hagag, K. E. Yousef, and T. Mostafa
Andrologia, 2011, Volume 43, Number 6, Page 387
Iwona Kątnik-Prastowska and Magdalena Orczyk-Pawiłowicz
Biochemical Society Transactions, 2011, Volume 39, Number 1, Page 355
Maja M. Kosanović and Miroslava M. Janković
Asian Journal of Andrology, 2010, Volume 12, Number 3, Page 363
Magdalena Przybysz, Dorota Maszczak, Krzysztof Borysewicz, Jacek Szechiński, and Iwona Kątnik-Prastowska
Glycoconjugate Journal, 2007, Volume 24, Number 9, Page 543

Comments (0)

Please log in or register to comment.
Log in