Premium
Gallium nitrate increases type I collagen and fibronectin mRNA and collagen protein levels in bone and fibroblast cells
Author(s) -
Bockman Richard S.,
Guidon Peter T.,
Pan Lydia C.,
Salvatori Roberto,
Kawaguchi Alan
Publication year - 1993
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240520404
Subject(s) - osteocalcin , fibronectin , gallium , type i collagen , osteoblast , fibroblast , chemistry , hydroxyproline , medicine , bone resorption , endocrinology , bone remodeling , procollagen peptidase , microbiology and biotechnology , biology , alkaline phosphatase , biochemistry , in vitro , extracellular matrix , enzyme , organic chemistry
Gallium is a Group IIIa transitional element with therapeutic efficacy in the treatment of metabolic bone disorders. Previously described antiresorptive effects of gallium on osteoclasts are not sufficient to account for the full range of effects of gallium on bone structure and metabolism. We have recently shown that gallium nitrate inhibits osteocalcin gene expression and the synthesis of osteocalcin protein, an osteoblast‐specific bone matrix protein that is though to serve as a signal to trigger osteoclastic resorption. Here we present evidence for an additional mechanism by which gallium may function to augment bone mass by altering matrix protein synthesis by osteoblastic and fibroblastic cells. Rat calvarial explants exposed to gallium nitrate for 48 h showed increased incorporation of 3 H‐proline into hydroxyproline and collagenase digestible protein. In addition, gallium treatment increased steady‐state mRNA levels for fibronectin and type I procollagen chains in primary rat calvarial osteoblast‐enriched cultures, the ROS 17/2.8 osteoblastic osteosarcoma line, and nontransformed human dermal fibroblasts. These findings suggest that the exposure of mesenchymally‐derived cells to gallium results in an altered pattern of matrix protein synthesis that would favor increased bone formation.