Linked Life Data

20026305

Source:http://linkedlifedata.com/resource/pubmed/id/20026305

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-1-27
pubmed:abstractText
Proteomic analysis of matrix vesicles (MVs) isolated from 17-day-old chicken embryo femurs revealed the presence of creatine kinase. In this report we identified the enzyme functionally and suggest that the enzyme may participate in the synthesis of ATP from ADP and phosphocreatine within the lumen of these organelles. Then, ATP is converted by nucleotide hydrolyzing enzymes such as Na(+), K(+)-ATPase, protein kinase C, or alkaline phosphatase to yield inorganic phosphate (P(i)), a substrate for mineralization. Alternatively, ATP can be hydrolyzed by a nucleoside triphosphate pyrophosphatase phosphodiesterase 1 producing inorganic pyrophosphate (PP(i)), a mineralization inhibitor. In addition, immunochemical evidence indicated that VDAC 2 is present in MVs that may serve as a transporter of nucleotides from the extracellular matrix. We discussed the implications of ATP production and hydrolysis by MVs as regulatory mechanisms for mineralization.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1090-2104
pubmed:author
pubmed:copyrightInfo
Copyright 2009 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
391
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1432-6
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Active creatine kinase is present in matrix vesicles isolated from femurs of chicken embryo: Implications for bone mineralization.
pubmed:affiliation
Department of Biochemistry, Nencki Institute of Experimental Biology, 3 Pasteur S., 02-093 Warsaw, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't