Cloning and initial characterization of mouse meltrin β and analysis of the expression of four metalloproteasedisintegrins in bone cells

Daisuke Inoue, Martha Reid, Lawrence Lum, Jörn Krätzschmar, Gisela Weskamp, Yoon Mo Myung, Roland Baron, Carl P. Blobel

Research output: Contribution to journalArticle

93 Scopus citations

Abstract

Here we report the cloning and initial biochemical characterization of the mouse metalloprotease/disintegrin/cysteine-rich (MDC) protein meltrin β and the analysis of the mRNA expression of four MDC genes (meltrin α, meltrin β, mdc9, and mdc15) in bone cells, including osteoclasts and osteoblasts. Like most other MDC proteins, the predicted meltrin β 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 β 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 β expression more than 3-fold, and both meltrin α and meltrin β expression is apparently regulated in a differentiation-associated manner in a mouse osteoblastic cell line, MC3T3E1. Collectively, these results suggest that meltrin α and meltrin β may play a role in osteoblast differentiation and/or function but are not likely to be involved in osteoclast fusion.

Original languageEnglish (US)
Pages (from-to)4180-4187
Number of pages8
JournalJournal of Biological Chemistry
Volume273
Issue number7
DOIs
StatePublished - Feb 13 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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