Identification of osteopontin in isolated rabbit osteoclasts

Tezuka, Ken Ichi; Sato, Takuya; Kamioka, Hiroshi; Nijweide, Peter J.; Tanaka, Kayo; Matsuo, Tetsu; Ohta, Mitsue; Kurihara, Noriyoshi; Hakeda, Yoshiyuki; Kumegawa, Masayoshi

doi:10.1016/0006-291x(92)90832-6

Cited by 228 publications

(149 citation statements)

References 18 publications

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“…In addition, recent studies of this proteinase in the skeleton suggest that MMP-9 could exist in matrix vesicles (27), digest cartilage proteoglycans (28,29), and play important roles in chondrocyte apoptosis (30) and osteoclastic bone resorption (31)(32)(33). MMP-9 can also be produced by activated osteoclasts (34). A number of osteoclasts in rapidly destructive hip OA, which are one source of MMP-9, have been observed around necrotic bone in subchondral areas (23,24).…”

Section: Discussionmentioning

confidence: 99%

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Masuhara

Nakai

Yamaguchi

et al. 2002

Arthritis & Rheumatism

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Objective. Rapidly destructive osteoarthritis (OA) of the hip is an uncommon subset of OA that affects mainly elderly women. Previous studies indicate that elevated levels of matrix metalloproteinases (MMPs) are produced within the tissue of patients with the condition. In the present study, we sought to determine whether serum and plasma levels of MMPs and tissue inhibitors of metalloproteinases (TIMPs) are also elevated.Methods. Blood samples were obtained from 16 patients with rapidly destructive hip OA and from 20 patients with OA before total hip arthroplasty was performed. Synovial specimens were obtained during surgery. Synovial fibroblasts that had migrated sufficiently from explants were subcultured in vitro for 72 hours after confluency, and harvested supernatants were collected. Blood, tissue samples, and fibroblasts were assayed for MMPs 1, 2, 3, and 9, and TIMPs 1 and 2 by sandwich enzyme immunoassay.Results. In blood samples, the levels of MMP-3 and MMP-9 in the group with rapidly destructive hip OA were significantly higher than the normal range and were also significantly higher than those in the OA group. In tissue samples, the levels of MMP-1, MMP-3, MMP-9, and TIMP-1 in the group with rapidly destructive hip OA were significantly higher than those in the OA group. Conclusion.The results of this study show that serum and plasma levels of MMP-3 and MMP-9 are significantly increased in patients with rapidly destructive hip OA. Significantly large amounts of these MMPs produced in synovial tissues within the hip joint could contribute in part to elevation of blood levels. Detection of increased levels of MMP-3 and MMP-9 in patients with painful, disabling hip OA may be of diagnostic value for rapidly destructive hip OA.

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Section: Discussionmentioning

confidence: 99%

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Masuhara

Nakai

Yamaguchi

et al. 2002

Arthritis & Rheumatism

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“…A type 2 fibronectin collagen-binding domain was found at position 127-168 in the predicted primary sequence of the TSA305 gene product. This domain exhibits substantial homology to metalloproteinase-9 (MP-9) and matrix metalloproteinase-2 (MMP-2) of rabbit osteoclasts (Tezuka et al 1994), to gelatinase of chicken embryo fibroblasts (Aimes et al 1994), and to murine type IV collagenase (Reponen et al 1992) (see Fig. 5).…”

Section: Discussionmentioning

confidence: 99%

Complete cDNA sequence and genomic organization of a human pancreas-specific gene homologous to Caenorhabditis elegans sel-1

et al. 1999

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We have isolated the complete cDNA of a human SEL-1L gene, termed TSA305, that is abundantly expressed only in the pancreas. The cDNA contained an open reading frame of 2382 nucleotides, encoding a deduced protein of 794 amino acids whose predicted sequence showed 46% identity and 64% similarity with SEL-1 of Caenorhabditis elegans. SEL-1 is thought to be a negative regulator of the NOTCH, LIN-12, and GLP-1 receptors, which are required for differentiation and maturation of cells as well as cell-cell interactions during development in C. elegans. The degree of homology among these proteins suggests that the TSA305 gene product may be a member of the SEL-1 family and therefore involved in downregulation of mammalian Notch signaling. Direct sequencing revealed at least 20 coding exons in TSA305. We localized the gene to chromosome bands 14q24.3-q31 by radiation hybrid (RH) mapping and fluorescence in situ hybridization (FISH). The IDDM11 locus has been mapped in this region, and TSA305 may represent a candidate gene for predisposition in some families whose insulin-dependent diabetes is not linked to the HLA locus.

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“…The amino acid sequence of osteopontin is nowadays available for several species, i.e., rat (39), mouse (60), human (61), pig (62), rabbit (63), and cow (64). The referenced mammalian osteopontin sequences are identical in f33% of the residues, and in addition, many similar amino acids are conserved between the sequences.…”

Section: The Structure Of Osteopontinmentioning

confidence: 99%

The Role of Osteopontin in Tumor Progression and Metastasis in Breast Cancer

Rodrigues

Teixeira

Schmitt

et al. 2007

Cancer Epidemiology, Biomarkers &Amp; Prevention

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144

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The use of cancer biomarkers to anticipate the outlines of disease has been an emerging issue, especially as cancer treatment has made such positive steps in the last few years. Progress in the development of consistent malignancy markers is imminent because advances in genomics and bioinformatics have allowed the examination of immense amounts of data. Osteopontin is a phosphorylated glycoprotein secreted by activated macrophages, leukocytes, and activated T lymphocytes, and is present in extracellular fluids, at sites of inflammation, and in the extracellular matrix of mineralized tissues. Several physiologic roles have been attributed to osteopontin, i.e., in inflammation and immune function, in mineralized tissues, in vascular tissue, and in kidney. Osteopontin interacts with a variety of cell surface receptors, including several integrins and CD44. Binding of osteopontin to these cell surface receptors stimulates cell adhesion, migration, and specific signaling functions. Overexpression of osteopontin has been found in a variety of cancers, including breast cancer, lung cancer, colorectal cancer, stomach cancer, ovarian cancer, and melanoma. Moreover, osteopontin is present in elevated levels in the blood and plasma of some patients with metastatic cancers. Therefore, suppression of the action of osteopontin may confer significant therapeutic activity, and several strategies for bringing about this suppression have been identified. This review looks at the recent advances in understanding the possible mechanisms by which osteopontin may contribute functionally to malignancy, particularly in breast cancer. Furthermore, the measurement of osteopontin in the blood or tumors of patients with cancer, as a way of providing valuable prognostic information, will be discussed based on emerging clinical data. (Cancer Epidemiol Biomarkers Prev 2007;16(6):1087 -97)

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Identification of osteopontin in isolated rabbit osteoclasts

Cited by 228 publications

References 18 publications

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Significant increases in serum and plasma concentrations of matrix metalloproteinases 3 and 9 in patients with rapidly destructive osteoarthritis of the hip

Complete cDNA sequence and genomic organization of a human pancreas-specific gene homologous to Caenorhabditis elegans sel-1

The Role of Osteopontin in Tumor Progression and Metastasis in Breast Cancer

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