Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-10-12
pubmed:abstractText
Human furin, a member of a recently discovered family of cellular endoproteases, has been identified as a membrane bound protein localized in the Golgi apparatus. Here, we report the presence of a secreted form of furin in the media of cells infected with a vaccinia virus recombinant containing the furin gene. Using the fluorogenic substrate boc-Arg-Val-Arg-Arg-MCA, endoproteolytic activity was detected in the media of infected BSC40 cells. Immunoprecipitations of [35S]-labeled proteins from infected cells revealed that the media contained a lower molecular form of furin than the cellular furin or than a previously characterized soluble furin mutant, hFUR713t. By using the direct linear plot representation of the Michaelis-Menten equation the results demonstrate that the soluble furin exhibited similar kinetics to the hFUR713t enzyme. Thus, our results suggest that membrane-bound furin undergoes post-translational processing to produce a soluble form of the enzyme that can be secreted.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
195
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1011-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Characterization of a secreted form of human furin endoprotease.
pubmed:affiliation
Department of Pharmacology, Faculty of Medicine, University of Sherbrooke, Québec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't