Linked Life Data

16076374

Source:http://linkedlifedata.com/resource/pubmed/id/16076374

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-8-3
pubmed:abstractText
Fibroblast Growth Factor (FGF) 23 has been shown to play important roles in the development of hypophosphatemic rickets/osteomalacia. Complementary DNA predicts that the FGF23 protein is composed of 251 amino acids and N-terminal 24 amino acids seem to be a signal peptide. In vitro experiments indicate that a part of the FGF23 protein is processed between arginine179 and serine180. When full-length, N-terminal and C-terminal processed fragments of FGF23 were injected into mice, only the full-length FGF23 reduced serum phosphate levels indicating that the processing of FGF23 abolished its effect to cause hypophosphatemia. This processing was shown to be prevented by an inhibitor of furin indicating that the cleavage is mediated by subtilisin-like proprotein convertase. In addition to this processing, FGF23 protein seems to have O-linked glycosylation. Further studies are necessary to clarify the importance of O-glycosylation for FGF23 activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1744-9979
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
319-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Post-translational modification of Fibroblast Growth Factor 23.
pubmed:affiliation
Division of Nephrology and Endocrinology, Department of Internal Medicine, University of Tokyo Hospital, Bunkyo-ku, Tokyo, Japan. fukumoto-tky@umin.ac.jp
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't