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J Biol Chem, Vol. 273, Issue 7, 4180-4187, February 13, 1998
and
Analysis of the Expression of Four MetalloproteaseDisintegrins in
Bone Cells
,,, and
From the Here we report the cloning and initial
biochemical characterization of the mouse
metalloprotease/disintegrin/cysteine-rich (MDC) protein meltrin Department of Orthopaedics and Cell Biology,
Yale University School of Medicine, New Haven, Connecticut 06510 and
the ¶ Cellular Biochemistry and Biophysics Program,
Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New
York, New York 10021
and
the analysis of the mRNA expression of four MDC genes
(meltrin 
, meltrin , mdc9, and mdc15) in
bone cells, including osteoclasts and osteoblasts. Like most other MDC
proteins, the predicted meltrin protein consists of a signal sequence, prodomain, metalloprotease domain with a predicted catalytic site, disintegrin domain, cysteine-rich region, epidermal growth factor
repeat, transmembrane domain, and cytoplasmic domain with putative
signaling motifs, such as potential SH3 ligand domains. Northern blot
analysis indicates that meltrin is widely expressed, with the highest expression in bone, heart, and lung. RNase protection studies revealed expression of all four MDC genes analyzed here in
osteoblasts, whereas only mdc9 and mdc15
mRNAs were detectable in osteoclast-like cells generated in
vitro. Treatment of primary osteoblasts with 10 nM
calcitriol increased meltrin expression more than
3-fold, and both meltrin and meltrin expression is apparently regulated in a differentiation-associated
manner in a mouse osteoblastic cell line, MC3T3E1. Collectively, these results suggest that meltrin and meltrin
may play a role in osteoblast differentiation and/or function but
are not likely to be involved in osteoclast fusion.
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