J. Lipid Res. Acyl Labeled PIP's available August 1, 2008
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Pedersen, M. E.
Right arrow Articles by Schotz, M. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pedersen, M. E.
Right arrow Articles by Schotz, M. C.
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?

Journal of Lipid Research, Vol 24, 512-521, Copyright © 1983 by Lipid Research, Inc.

ARTICLES

Immunocytochemical localization of the functional fraction of lipoprotein lipase in the perfused heart

ME Pedersen, M Cohen and MC Schotz

The functional (heparin-releasable) fraction of myocardial lipoprotein lipase (LPL) has been located at the lumen surface of capillary endothelium by means of an indirect immunocytochemical perfusion method for electron microscopy. The primary step immunoreactant was an IgG fraction of goat antiserum directed against LPL from rat heart. The second step antibody, conjugated with horseradish peroxidase, was rabbit IgG directed against goat IgG. Peroxidase reaction product, when present, appeared at the surface an in invaginations of the lumenal plasma membrane of capillary endothelium and also on chylomicrons adherent to that membrane. The highest coverage by such product occurred when the highest heparin-releasable heart LPL activity was attained after fat-feeding of rats. Coverage was low when a low level of heparin-releasable heart LPL activity was induced by carbohydrate- feeding. Coverage was very low in the perfused hearts after heparin- release of functional LPL activity. The positive association between these immunocytochemical results and actual levels of functional LPL activities indicates that functional LPL in the isolated rat heart is at the lumen surface of capillary endothelium.
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
 Arterioscler. Thromb. Vasc. Bio.Home page
C. Zheng, S. J. Murdoch, J. D. Brunzell, and F. M. Sacks
Lipoprotein Lipase Bound to Apolipoprotein B Lipoproteins Accelerates Clearance of Postprandial Lipoproteins in Humans
Arterioscler. Thromb. Vasc. Biol., April 1, 2006; 26(4): 891 - 896.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
T. Ruge, M. Bergo, M. Hultin, G. Olivecrona, and T. Olivecrona
Nutritional regulation of binding sites for lipoprotein lipase in rat heart
Am J Physiol Endocrinol Metab, February 1, 2000; 278(2): E211 - E218.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Journal of Biological Chemistry 
 Molecular and Cellular Proteomics   ASBMB Today 
Copyright © 1983 by the American Society for Biochemistry and Molecular Biology.