Jump to ContentJump to Main Navigation
Show Summary Details
In This Section

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751

Online
ISSN
1437-4315
See all formats and pricing
In This Section
Volume 388, Issue 7 (Jul 2007)

Issues

Plasminogen-dependent internalization of soluble melanotransferrin involves the low-density lipoprotein receptor-related protein and annexin II

Jonathan Michaud-Levesque
  • 1Laboratoire de Médecine Moléculaire, Service d'Hémato-Oncologie, Hôpital Ste-Justine, Université du Québec à Montréal, Montréal H3C 3P8, Québec, Canada
/ Michel Demeule
  • 2Laboratoire de Médecine Moléculaire, Service d'Hémato-Oncologie, Hôpital Ste-Justine, Université du Québec à Montréal, Montréal H3C 3P8, Québec, Canada
/ Richard Béliveau
  • 3Laboratoire de Médecine Moléculaire, Service d'Hémato-Oncologie, Hôpital Ste-Justine, Université du Québec à Montréal, Montréal H3C 3P8, Québec, Canada
Published Online: 2007-07-01 | DOI: https://doi.org/10.1515/BC.2007.081

Abstract

We investigated the effect of plasminogen (Plg) on the internalization of recombinant soluble melanotransferrin (sMTf) using U87 human glioblastoma cells and murine embryonic fibroblasts (MEF) deficient in the low-density lipoprotein receptor-related protein (LRP). Using biospecific interaction analysis, both Glu- and Lys-Plg were shown to interact with immobilized sMTf. The binding of sMTf at the cell surface increased in the presence of both forms of Plg in control and in LRP-deficient MEF cells, whereas the uptake was strongly stimulated only by Lys-Plg in control MEF and U87 cells. In addition, in the presence of Lys-Plg, the internalization of sMTf was a saturable process, sensitive to temperature and dependent on the integrity of lysine residues. The addition of the receptor-associated protein, lactoferrin and aprotinin, as well as a monoclonal antibody (mAb) directed against LRP, inhibited the Lys-Plg-dependent uptake of sMTf. These results suggest an important role for LRP in this process. In addition, using binding and uptake assays in the presence of anti-annexin II mAb, we showed that annexin II might be responsible for the initial binding of sMTf in the presence of Plg. Our results suggest a Plg-mediated internalization mechanism for the clearance of sMTf via annexin II and LRP.

Keywords: annexin II; endocytosis; low-density lipoprotein receptor-related protein; plasminogen; soluble melanotransferrin

About the article

Corresponding author


Received: 2006-11-23

Accepted: 2007-04-03

Published Online: 2007-07-01



Citation Information: Biological Chemistry, ISSN (Online) 14316730, ISSN (Print) 14374315, DOI: https://doi.org/10.1515/BC.2007.081. Export Citation

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.

[1]
Lisa A. Lambert
Biochimica et Biophysica Acta (BBA) - General Subjects, 2012, Volume 1820, Number 3, Page 244
[2]
Yannève Rolland, Michel Demeule, Laurence Fenart, and Richard Béliveau
Pigment Cell & Melanoma Research, 2009, Volume 22, Number 1, Page 86

Comments (0)

Please log in or register to comment.
Log in