JBC Biosymposia, Inc.

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bendixen, E.
Right arrow Articles by Sottrup-Jensen, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bendixen, E.
Right arrow Articles by Sottrup-Jensen, L.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 270, Number 30, Issue of July 28, pp. 17929-17933, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Location of the Major -(-Glutamyl)lysyl Cross-linking Site in Transglutaminase-modified Human Plasminogen

(Received for publication, May 8, 1995)

Em Bendixen ,  Peter C. Harpel ,  Lars Sottrup-Jensen

From the  (1)Department of Molecular Biology, University of Aarhus, DK-8000 C, Denmark and the (2)Division of Hematology, Mount Sinai Medical Center, New York, New York 10029

Tissue and plasma transglutaminases cross-link human plasminogen into high molecular weight complexes (Bendixen, E., Borth, W., and Harpel, P. C.(1993) J. Biol. Chem. 268, 21962-21967). A major cross-linking site in plasminogen involved in the tissue transglutaminase-mediated polymerization process has been identified. The -(-glutamyl)lysyl bridges of the polymer are formed between Lys-298 and Gln-322. Both the acyl donor Gln residue and the acyl acceptor Lys residue are located in the kringle 3 domain of plasminogen, i.e. cross-linking of plasminogen by tissue transglutaminase involves neither the catalytic domain nor the lysine-dependent binding sites of plasminogen. This study documents that kringle 3 contains a novel functional site with the potential to participate in transglutaminase-mediated cross-linking interactions with plasma, cell-surface, and extracellular proteins.



Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Z. Valnickova and J. J. Enghild
Human Procarboxypeptidase U, or Thrombin-activable Fibrinolysis Inhibitor, Is a Substrate for Transglutaminases. EVIDENCE FOR TRANSGLUTAMINASE-CATALYZED CROSS-LINKING TO FIBRIN
J. Biol. Chem., October 16, 1998; 273(42): 27220 - 27224.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.