JBC INTERFERin siRNA transfection reagent

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
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 Hamel, F. G.
Right arrow Articles by Duckworth, W. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hamel, F. G.
Right arrow Articles by Duckworth, W. 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?

J. Biol. Chem., Vol. 263, Issue 14, 6703-6708, 05, 1988

Isolation of insulin degradation products from endosomes derived from intact rat liver

FG Hamel, BI Posner, JJ Bergeron, BH Frank and WC Duckworth
Veterans Administration Medical Center, Omaha, Nebraska 68105.

Rats were injected with [125I]iodoinsulin labeled at either the A14 or B26 tyrosine, and the animals were killed and livers subcellularly fractionated to yield light (early or neutral) endosomes and heavy (late or acidic) endosomes. 125I-Labeled material was extracted from endosomes and analyzed by Sephadex G-50 filtration and high performance liquid chromatography (HPLC). Radiolabeled material in both types of endosomes is comprised of high molecular weight, insulin-sized, and low molecular weight components, with B chain-labeled small molecular weight material in two peaks, one corresponding to iodotyrosine and one to small peptides (Mr less than 1500). As compared with A chain label, however, less of the B chain material appears in the degradation components (both high and low molecular weight fractions) suggesting that a fragment of B chain containing the B26 residue is lost from the endosomes. Analysis on HPLC shows that significant amounts of the insulin-sized and high molecular weight material have proteolytic cleavage(s) in the B chain with an intact A chain. The B chain-derived labeled peptides elute from HPLC identically with products generated by insulin protease. These results therefore show substantial insulin degradation occurring in light endosomes prior to endosomal acidification and to receptor dissociation, suggesting receptor-bound insulin is a substrate for insulin protease.
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
A. Balbis, G. Baquiran, V. Dumas, and B. I. Posner
Effect of Inhibiting Vacuolar Acidification on Insulin Signaling in Hepatocytes
J. Biol. Chem., March 26, 2004; 279(13): 12777 - 12785.
[Abstract] [Full Text] [PDF]


Home page
EndocrinologyHome page
F. G. Hamel, J. L. Upward, and R. G. Bennett
In Vitro Inhibition of Insulin-Degrading Enzyme by Long-Chain Fatty Acids and Their Coenzyme A Thioesters
Endocrinology, June 1, 2003; 144(6): 2404 - 2408.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
F. Authier, M. Metioui, S. Fabrega, M. Kouach, and G. Briand
Endosomal Proteolysis of Internalized Insulin at the C-terminal Region of the B Chain by Cathepsin D
J. Biol. Chem., March 8, 2002; 277(11): 9437 - 9446.
[Abstract] [Full Text] [PDF]


Home page
Endocr. Rev.Home page
W. C. Duckworth, R. G. Bennett, and F. G. Hamel
Insulin Degradation: Progress and Potential
Endocr. Rev., October 1, 1998; 19(5): 608 - 624.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
J.-O. Contreres, R. Faure, G. Baquiran, J. J. Bergeron, and B. I. Posner
ATP-dependent Desensitization of Insulin Binding and Tyrosine Kinase Activity of the Insulin Receptor Kinase. THE ROLE OF ENDOSOMAL ACIDIFICATION
J. Biol. Chem., August 21, 1998; 273(34): 22007 - 22013.
[Abstract] [Full Text] [PDF]


Home page
EndocrinologyHome page
V. Chesneau, R. K. Perlman, W. Li, G.-A. Keller, and M. R. Rosner
Insulin-Degrading Enzyme Does Not Require Peroxisomal Localization for Insulin Degradation
Endocrinology, August 1, 1997; 138(8): 3444 - 3451.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
T. Tjelle, A Brech, L. Juvet, G Griffiths, and T Berg
Isolation and characterization of early endosomes, late endosomes and terminal lysosomes: their role in protein degradation
J. Cell Sci., January 12, 1996; 109(12): 2905 - 2914.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1988 by the American Society for Biochemistry and Molecular Biology.