Active creatine kinase is present in matrix vesicles isolated from femurs of chicken embryo: Implications for bone mineralization.
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.
Sekrecka-Belniak
Anna
A
Department of Biochemistry, Nencki Institute of Experimental Biology, 3 Pasteur S., 02-093 Warsaw, Poland.
Balcerzak
Marcin
M
Buchet
Rene
R
Pikula
Slawomir
S
D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000096:biosynthesis; D000818:Animals; D002113:Calcification, Physiologic; D002642:Chick Embryo; D003402:Creatine Kinase / Q000378:metabolism*; D005109:Extracellular Matrix / Q000201:enzymology*; D005269:Femur; D010725:Phosphocreatine / Q000378:metabolism; D050996:Voltage-Dependent Anion Channel 2 / Q000378:metabolism
D050996:Voltage-Dependent Anion Channel 2; D010725:Phosphocreatine; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D003402:Creatine Kinase