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J. Biol. Chem., Vol. 263, Issue 23, 11033-11036, Aug, 1988
JD Fraser and PA Price
We have used cDNA probes for two small vitamin K-dependent bone matrix
proteins, bone Gla protein (BGP) and matrix Gla protein (MGP), to evaluate
the possibility that either of these proteins might be synthesized by the
various soft tissues previously shown to have gamma- carboxylase activity.
BGP mRNA was found in bone but not in any of the soft tissues tested, a
result which reinforces the view that plasma BGP is a specific marker for
bone metabolism. In contrast, MGP mRNA was found in all rat tissues
examined. Lung and heart have 10-fold higher levels of MGP mRNA than bone,
and kidney has a 5-fold higher level. Despite the high levels of MGP mRNA
in heart and kidney, these tissues contain 40-500-fold lower concentrations
of MGP protein than bone. Immunofluorescence was used to identify cells
that contain MGP in kidney, lung, heart, and spleen. In each tissue, MGP
was found in discrete tissue-specific cell types. In most of the soft
tissues tested, MGP is the first well characterized substrate for the
vitamin K- dependent carboxylase found to be synthesized. The exceptionally
broad tissue distribution for MGP synthesis demonstrates that the function
of MGP is not specific to connective tissues, and the low levels of MGP
antigen in soft tissues with high MGP mRNA levels indicate that MGP is
unlikely to act solely by virtue of its accumulation in an extracellular
matrix.
Lung, heart, and kidney express high levels of mRNA for the vitamin K- dependent matrix Gla protein. Implications for the possible functions of matrix Gla protein and for the tissue distribution of the gamma- carboxylase
Department of Biology, University of California, San Diego, La Jolla 92093.
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