Skip Navigation

European Heart Journal 1990 11(Supplement E):72-81; doi:10.1093/eurheartj/11.suppl_E.72
Copyright © 1990 by the European Society of Cardiology.
This Article
Right arrow Full Text (PDF)
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
Right arrow Alert me if a correction is posted
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Smith, E. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Smith, E. B.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 1990 The European Society of Cardiology

Transport, interactions and retention of plasma proteins in the intima: the barrier function of the internal elastic lamina

E. B. Smith

Department of Clinical Biochemistry, University of Aberdeen Aberdeen, U. K.

correspondence: Elspeth B. Smith, Department of Clinical Bio-chemistry, Medical School Buildings, Aberdeen Royal Infirmary, Fosterhill, Aberdeen AB9 2ZD, U.K.

This paper presents a brief overview of our current understanding of the relation between plasma macromolecules and atherogenesis. Plasma proteins enter normal intima by vesicular transport across normal endothelium, and convective transport within the intima; accumulation depends mainly on molecular size and the molecular sieve properties of the internal elastic lamina. Within the intima the proteins may be modified; particularly striking changes occur in high density lipoprotein (HDL) and in fibrinogen. Fibrinogen appears to be converted to fibrin which is then lysed, providing a continuing source of fibrin degradation products (FDP). Fibrin also seems to be associated with a tightly bound, plasmin-releasable apo-B-containing lipoprotein; work in progress suggests that much of this fraction is accounted for by lipoprotein(a).

Key Words: Human intima • atherosclerosis • endothelium • vesicular transport • low-density lipoprotein • lipoprotein(a) • high-density lipoprotein • fibrinogen/fibrin • fibrin degradation products


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Acta Biochim Biophys SinHome page
W. Yao, K. Li, and K. Liao
Macropinocytosis contributes to the macrophage foam cell formation in RAW264.7 cells
Acta Biochim Biophys Sin, September 1, 2009; 41(9): 773 - 780.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.