Linked Life Data

21086720

Source:http://linkedlifedata.com/resource/pubmed/id/21086720

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-11-19
pubmed:abstractText
Intracellular protein degradation is a universal feature of eukaryotic cells and vital for nutrition, protein turnover, intracellular signaling, development and other major physiological processes like antigen presentation and immunity. One of the major compartments of intracellular proteolysis is the endosome-lysosome system. The latter offers a highly orchestrated, vesicular pathway for protein transport and ultimate degradation in lysosomes. Though lysosomes are the classical organelles of complex, multi-enzymatic degradation, it is increasingly evident that endosomes conduct much more than mere transport functions. Endosomes contain significant levels of proteases like cathepsins and are sites of potent intracellular proteolysis. Further, discrete classes of endosomes harbor specific cathepsins and perform selective and exclusive functions. Hence, extra-lysosomal proteolytic machinery within the endocytic pathway enjoys spatial and temporal control over proteolytic functions. The review outlines the structural association and function(s) of major endolysosomal cathepsins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0301-1208
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-90
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Cathepsins: fundamental effectors of endolysosomal proteolysis.
pubmed:affiliation
Department of Cell and Molecular Biology, B. V. Patel Pharmaceutical Education and Research Development Centre, S.G. Highway, Thaltej, Ahmedabad 380054, India.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't