Linked Life Data

2636992

Source:http://linkedlifedata.com/resource/pubmed/id/2636992

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-7-11
pubmed:abstractText
Cellular proteolytic enzymes are regulated by multiple mechanisms that affect gene expression, enzyme concentration, and enzyme activity. The expression of the membrane-bound metallo-endopeptidase, meprin, in different mammalian species, strains, tissues and cell types is highly variable. Meprin is exclusively localized to the plasma membrane, and this determines the types of substrates the enzyme will encounter and the microenvironment for activity. Recent studies have revealed an inactive form of a meprin-like proteinase that can be activated in vitro by proteases, and this raises the possibility of regulation of enzyme activity at the cell surface in response to environmental stimuli. In this chapter, the current knowledge about meprin, and the meprin-like inactive forms in mouse kidney is discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0213-7119
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-37
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Regulation of a membrane-bound proteinase in mammalian cells.
pubmed:affiliation
Department of Biochemistry & Nutrition, State University, Blacksburg 24061-0308.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.