Linked Life Data

8073392

Source:http://linkedlifedata.com/resource/pubmed/id/8073392

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1994-9-28
pubmed:abstractText
The vitamin K-dependent clotting factors require posttranslational proteolytic processing before they are secreted by the liver into blood as mature zymogens. For most of these proteins, the sequences around the cleavage sites show a common motif (Arg-X-Lys/Arg-Arg) which define the substrate specificity for the endoprotease furin/PACE of the Golgi apparatus. In this paper, we present data which suggest that an additional Ca(++)-dependent endoprotease(s) is located in the endoplasmic reticulum, and may participate in processing of the two-chain vitamin K-dependent coagulation factor X. The single-chain 70 kDa factor X precursor in microsomes from rat liver was labeled by 14C-gamma-carboxylation and its conversion to a two-chain form followed in an incubation system with microsomal membrane fragments. A Ca(++)-dependent endoprotease(s) converted the factor X precursor to a two-chain form with a light-chain of 21 kDa. The endoprotease(s) showed little reactivity towards release of the factor X propeptide. The data provide new information about the endoprotease system in liver which participates in clotting factor proteolytic processing.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0049-3848
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
73
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
395-403
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Intracellular proteolytic processing of the two-chain vitamin K-dependent coagulation factor X.
pubmed:affiliation
Department of Medicine, Bowman Gray School of Medicine of Wake Forest University, Winston Salem, NC 27157.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.