ENDOSOMAL PROTEOLYSIS OF INTERNALIZED PROTEINS

Citation
F. Authier et al., ENDOSOMAL PROTEOLYSIS OF INTERNALIZED PROTEINS, FEBS letters, 389(1), 1996, pp. 55-60
Citations number
55
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
389
Issue
1
Year of publication
1996
Pages
55 - 60
Database
ISI
SICI code
0014-5793(1996)389:1<55:EPOIP>2.0.ZU;2-D
Abstract
Endosomal proteases have been implicated in the degradation of interna lized regulatory peptides involved in the control of metabolic pathway s and in the processing of intracellular antigens for cytolytic immune responses. Processing in the endocytic vesicles is regulated by chang es in endosomal acidity due to the presence of an ATP-dependent proton pump which modulates protease activity, protein unfolding and recepto r-ligand interactions, A limited number of proteases appear to reside in endosomes which do not contain the full complement of active protea ses capable of completely degrading all internalized polypeptides, Ret ention of some acid hydrolases in endosomes is apparently related to t heir association with undefined endosomal membrane receptors, The limi ted number of proteases and the pH gradient from neutral to acidic (pH 7 to 5) within endosomes make possible a selective and controlled pro cessing environment in comparison to lysosomes, The full set of endo- and exopeptidases that break down proteins to amino acids are active l ater in the pathway in lysosomes.