{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,8,30]],"date-time":"2025-08-30T16:36:45Z","timestamp":1756571805139},"reference-count":48,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,2,4]],"date-time":"2005-02-04T00:00:00Z","timestamp":1107475200000},"content-version":"vor","delay-in-days":4052,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal Cellular Physiology"],"published-print":{"date-parts":[[1994,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Osteoclast abnormalities that characterize osteopetrosis, a disorder of bone resorption, may derive from aberrant signals from the osteoblast or the bone matrix. In the present studies, both synthesis and the bone matrix content of the major bone phosphoprotein component, osteopontin, were found to be elevated in three osteopetrotic rat mutations (<jats:italic>ia, op<\/jats:italic>, and <jats:italic>tl<\/jats:italic>). In whole bone, a twofold increase in the content of the characteristic amino acid O\u2010phosphoserine for osteopontin occurred in <jats:italic>op<\/jats:italic> and <jats:italic>tl<\/jats:italic> mutant long bone, but a smaller (15%) and more variable increase was observed in <jats:italic>ia<\/jats:italic> mutant rat long bone. Extraction of the bone matrix components and partial purification by reverse phase chromatography showed a twofold increase in a phosphoprotein fraction relative to other noncollagenous components. Amino acid analysis and staining characteristics of SDS\u2010PAGE fractionated proteins indicated this to be osteopontin. Organ cultures of calvarial bone from 4 day <jats:italic>ia<\/jats:italic> osteopetrotic mutant and normal rats in the presence of <jats:sup>3<\/jats:sup>H\u2010proline showed increased synthesis of this 60 kD protein, which was stimulated by vitamin D. Preparation of total cellular RNA from bone of 2\u2010 and 6\u2010weekold mutants and normal rats supported increased synthesis of osteopontin as reflected by hybridization with osteopontin cDNA probe, showing significantly higher levels of mRNA transcripts in <jats:italic>ia<\/jats:italic> (3\u20135 fold), <jats:italic>tl<\/jats:italic> (1.4\u20132 fold), and <jats:italic>op<\/jats:italic> (6\u201325 fold) mutant bone compared to normal littermates. The changes in osteopontin mRNA levels in mutant bone were also examined in relation to other growth and phenotype\u2010expressed genes. The findings of increased accumulation of osteopontin in osteopetrotic bone and increased synthesis by osteoblasts are interesting in light of the previously reported decrease in bone osteocalcin content (Endocrinology, 126:966, 1990), confirmed here by decreased osteocalcin mRNA transcripts. Such aberrations in the composition of skeletal extracellular matrix could be a reflection of or a contributing factor to the osteoclast abnormalities of some of these osteopetrotic disorders. \u00a9 1994 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jcp.1041580114","type":"journal-article","created":{"date-parts":[[2005,2,26]],"date-time":"2005-02-26T05:02:30Z","timestamp":1109394150000},"page":"110-120","source":"Crossref","is-referenced-by-count":15,"title":["Abnormalities of phosphoprotein gene expression in three osteopetrotic rat mutations: Elevated mrna transcripts, protein synthesis, and accumulation in bone of mutant animals"],"prefix":"10.1002","volume":"158","author":[{"given":"V.","family":"Shalhoub","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B.","family":"Bettencourt","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. 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