Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5 Pt 1
pubmed:dateCreated
1995-6-29
pubmed:abstractText
We have examined the conversion of parathyroid hormone-related peptide (PTHRP) from its NH2-terminally extended precursor pro-PTHRP. Within pro-PTHRP, an amino acid sequence exists that can serve as a substrate for the prohormone convertase, furin. To evaluate the potential role of furin in processing of this entity, we expressed pro-PTHRP in COS-7 cells, which normally produce this enzyme. Transiently transfected COS-7 cells secreted high levels of PTHRP into conditioned culture medium. Cotransfection of these cells with antisense furin cDNA resulted in marked inhibition of furin mRNA expression and secretion of an NH2-terminal fragment of pro-PTHRP, which comigrated with synthetic pro-PTHRP-(-12-->+36) on gel-permeation high-pressure liquid chromatography. In an adenylate cyclase bioassay, condition medium containing this fragment and synthetic pro-PTHRP-(-12-->+36) both exhibited lower potency than synthetic PTHRP-(1-36) and conditioned medium containing PTHRP produced by COS-7 cells in the absence of antisense furin. These results demonstrate the capacity of furin to convert pro-PTHRP to a more active product and suggest a role for this enzyme in the normal intracellular processing of this hormone.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
E832-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Processing of pro-PTHRP by the prohormone convertase, furin: effect on biological activity.
pubmed:affiliation
Department of Medicine, McGill University, Montreal, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't