Structure, expression, and regulation of the major noncollagenous matrix proteins of bone
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Structure, expression, and regulation of the major noncollagenous matrix proteins of bone. / Young, M F; Kerr, J M; Ibaraki, K; Heegaard, Anne-Marie; Robey, P G.
In: Clinical Orthopaedics and Related Research, No. 281, 1992, p. 275-94.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Structure, expression, and regulation of the major noncollagenous matrix proteins of bone
AU - Young, M F
AU - Kerr, J M
AU - Ibaraki, K
AU - Heegaard, Anne-Marie
AU - Robey, P G
PY - 1992
Y1 - 1992
N2 - The noncollagenous proteins (NCPs) that predominate the bone matrix have recently been the focus of intense investigation because of their potential influence on cell attachment, Ca2+ and hydroxyapatite binding, and the mineralization of bone tissue. With the advent of molecular biology, all of the major NCPs of bone have been cloned and their amino acid sequences completely determined. While each of the proteins has distinct structural properties, some proteins appear to be part of gene families. Examples include the small proteoglycans, decorin and biglycan, as well as the gamma carboxyglutamic acid proteins, such as matrix gla protein and osteocalcin (bone gla protein). Some of the NCPs that are clearly not members of any known gene family still share several common characteristics. One such example of this "convergent evolution" is bone sialoprotein and osteopontin. Both are highly posttranslationally modified glycoproteins that share the cell attachment amino acid sequence RGD (arginine-glycine-aspartic acid), which facilitates the attachment of bone cells in vitro, yet they are clearly not related genetically. Using cDNAs and antisera as probes, the precise temporal localization of NCP expression has been determined, and it has been shown that NCPs are produced in skeletal, and in most cases, nonskeletal tissue as well. This observation implies that the functions of the NCPs are not necessarily limited to bone tissue. Many of the promoters for these genes have been isolated and functional domains determined by a combination of chloramphenicol acetyltransferase assay, gel shift, and footprint analyses. The most extensively studied promoter in the NCP category is osteocalcin, whose sensitivity to 1,25-dihydroxycholecalciferol has been delineated in detail. Future studies on the individual and cooperative activities of the NCPs in bone are likely to involve site-directed mutagenesis of cloned DNA and a combination of in vitro and in vivo functional analyses.
AB - The noncollagenous proteins (NCPs) that predominate the bone matrix have recently been the focus of intense investigation because of their potential influence on cell attachment, Ca2+ and hydroxyapatite binding, and the mineralization of bone tissue. With the advent of molecular biology, all of the major NCPs of bone have been cloned and their amino acid sequences completely determined. While each of the proteins has distinct structural properties, some proteins appear to be part of gene families. Examples include the small proteoglycans, decorin and biglycan, as well as the gamma carboxyglutamic acid proteins, such as matrix gla protein and osteocalcin (bone gla protein). Some of the NCPs that are clearly not members of any known gene family still share several common characteristics. One such example of this "convergent evolution" is bone sialoprotein and osteopontin. Both are highly posttranslationally modified glycoproteins that share the cell attachment amino acid sequence RGD (arginine-glycine-aspartic acid), which facilitates the attachment of bone cells in vitro, yet they are clearly not related genetically. Using cDNAs and antisera as probes, the precise temporal localization of NCP expression has been determined, and it has been shown that NCPs are produced in skeletal, and in most cases, nonskeletal tissue as well. This observation implies that the functions of the NCPs are not necessarily limited to bone tissue. Many of the promoters for these genes have been isolated and functional domains determined by a combination of chloramphenicol acetyltransferase assay, gel shift, and footprint analyses. The most extensively studied promoter in the NCP category is osteocalcin, whose sensitivity to 1,25-dihydroxycholecalciferol has been delineated in detail. Future studies on the individual and cooperative activities of the NCPs in bone are likely to involve site-directed mutagenesis of cloned DNA and a combination of in vitro and in vivo functional analyses.
KW - Biglycan
KW - Bone Matrix
KW - Calcium-Binding Proteins
KW - Decorin
KW - Extracellular Matrix Proteins
KW - Gene Expression
KW - Genetic Techniques
KW - Glycoproteins
KW - Humans
KW - Integrin-Binding Sialoprotein
KW - Osteocalcin
KW - Osteonectin
KW - Osteopontin
KW - Phosphoproteins
KW - Platelet Membrane Glycoproteins
KW - Proteins
KW - Proteoglycans
KW - Sialoglycoproteins
KW - Thrombospondins
M3 - Journal article
C2 - 1499220
SP - 275
EP - 294
JO - Clinical Orthopaedics and Related Research
JF - Clinical Orthopaedics and Related Research
SN - 0009-921X
IS - 281
ER -
ID: 38426752