Linked Life Data

1885622

Source:http://linkedlifedata.com/resource/pubmed/id/1885622

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1991-10-4
pubmed:abstractText
We have cloned a rat cDNA encoding furin which is structurally related to yeast Kex2 protease. Products of 88 and 94 kDa were obtained by in vitro transcription/translation of the cDNA in the absence and presence of microsomes. When the cDNA was transfected into COS-1 cells, furin was expressed as a major glycosylated form of 94 kDa, accompanied by a minor proteolytic form of 86 kDa, and found to be localized in the Golgi complex. Proalbumin and complement pro-C3 are intracellularly processed into their mature forms by cleavage at the dibasic residues Arg-Arg, a common cleavage signal found in many pro-type precursors. In cells transfected with the cDNA of C3 or albumin alone, only about half of each proform expressed was processed by an endogenous activity of the cells. When furin was coexpressed, the proforms of both C3 and albumin were completely processed into their mature forms. In addition, co-expression of rat alpha 1-protease inhibitor mutant (Met352----Arg) resulted in inhibition of the endogenous and exogenous processing activities, as observed for the naturally occurring mutant Pittsburgh which has been identified as a specific inhibitor for the processing enzyme. Taken together, these results indicate that furin is an endoprotease localized to the Golgi complex and capable of processing proalbumin and pro-C3 into the mature forms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16954-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Functional expression of furin demonstrating its intracellular localization and endoprotease activity for processing of proalbumin and complement pro-C3.
pubmed:affiliation
Department of Biochemistry, Fukuoka University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't