Linked Life Data

18171086

Source:http://linkedlifedata.com/resource/pubmed/id/18171086

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-1-22
pubmed:abstractText
Alpha2-macroglobulin (alpha2M) is a major human blood glycoprotein best known for its ability to inhibit a broad spectrum of proteases by a unique trapping method. This action induces an "activated" conformation of alpha2M with an exposed binding site for the low-density lipoprotein receptor, facilitating clearance of alpha2M/protease complexes from the body. This report establishes that protease activation also modulates a potent chaperone-like action of alpha2M that has broad specificity for proteins partly unfolded as a result of heat or oxidative stress. Protease-mediated activation of alpha2M abolishes its chaperone-like activity. However, native alpha2M is able to form soluble complexes with stressed proteins and then subsequently become activated by interacting with a protease, providing a potential mechanism for the in vivo clearance of alpha2M/stressed protein/protease complexes. We propose that alpha2M is a newly discovered and unique member of a small group of abundant extracellular proteins with chaperone properties that patrol extracellular spaces for unfolded/misfolded proteins and facilitate their disposal.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1176-85
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Protease activation of alpha2-macroglobulin modulates a chaperone-like action with broad specificity.
pubmed:affiliation
School of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, NSW 2522, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't