Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0029463 (osteosarcoma)
 16,637 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Localization of bone morphogenetic protein (BMP) in human tissues and cells is important for investigating the mechanism of bone induction. A stable cell line secreting monoclonal antibody against bovine BMP (bBMP-McAb) was obtained by the hybridoma technique. The result of immunohistochemical staining (ABC method) showed that BMP is distributed along collagen fibers of normal bone, in periosteal cells, and in mesenchymal cells of marrow stroma. Little BMP can be found in bone cells of lamellar bone or in calcified bone matrix. BMP may be abundant in human tooth anlagen such as predentin, cells of the outer and inner enamel epithelium, and cells of dental sac generating bone. BMP is found in the cytoplasm of tumor cells of osteosarcoma and chondrosarcoma. Immunohistochemical staining showed that BMP plays a role in bone fracture healing. The ability of BMP-McAb to detect BMP and to inhibit the generation of new bone also makes it potentially useful in diagnosing, treating, and providing a prognosis for osteosarcoma and other bone diseases.
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PMID:Immunohistochemical observations on bone morphogenetic protein in normal and abnormal conditions. 237 62

A human osteosarcoma cell line was established from a biopsy specimen from a 13-year-old girl. The osteosarcoma tissue was maintained in athymic nude mice (Balb C nu/nu) by serial transplantation for three years. The tumor was excised from a host mouse and digested with collagenase. The isolated cells were cultured by 98 passages in 14 months, and clones of osteosarcoma cells were obtained by limiting dilution. A clone named human osteosarcoma cell 6 (H-OS-6) that showed the osteoblastic phenotypes of productions of bone morphogenetic protein (BMP) and alkaline phosphatase and a response to human parathyroid hormone (h-PTH 1-34) was selected. The morphology of its chromosomes indicated its human origin. This human osteosarcoma cell line is unique in producing BMP under in vitro conditions.
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PMID:Establishment of a cell line producing bone morphogenetic protein from a human osteosarcoma. 254 99

A small amount of partially purified, water-soluble murine osteosarcoma-derived bone morphogenetic protein (BMP) was implanted into the dorsal muscles of mice in combination with calf skin gelatin or collagen as carriers. Changes in the ribs adjacent to the implants were then chronologically observed. On implantation of BMP with gelatin, the gelatin was rapidly absorbed and no ectopic bone formation was observed, but periosteal cellular proliferation with subsequent formation of periosteal cartilage and bone was seen in ribs adjacent to the implant. Implantation of the same amount of BMP fraction or gelatin alone as controls did not result in either any ectopic bone formation in situ or any periosteal bone formation in adjacent ribs. Implantation of BMP with collagen resulted consistently in both ectopic bone formation in situ and periosteal bone formation in adjacent ribs. These results suggest that BMP is diffusible in vivo and is capable of eliciting a response from periosteum to stimulate periosteal bone formation.
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PMID:Periosteal bone formation elicited by partially purified bone morphogenetic protein. 231 87

The bone morphogenetic activities of the primary tumors of 30 patients with osteosarcoma were assayed. This activity was demonstrated as ectopic new bone formation on implantation of freeze-dried fractions of 12 of 30 tumors into athymic nude mice. Pulmonary metastases developed in ten (83%) of the 12 patients with osteosarcomas that produced bone morphogenetic protein (BMP), and bone metastases developed in six (50%) of the patients. The mean period from diagnosis to metastasis was 4.2 months in these patients. In contrast, pulmonary metastases developed in only eight (44%) of the patients with osteosarcomas that did not produce BMP, and bone metastases developed in only two (11%) of these patients. The mean period to metastasis was 12.3 months in these patients. The incidence of metastases in the patients with osteosarcomas producing BMP was significantly higher, and the mean period to metastasis was also significantly shorter than in the other group. The five year survival rates of patients with osteosarcomas that did and did not produce BMP were 33.3% and 54.6%, respectively (P = 0.015, log-rank test). Thus the bone morphogenetic activity of primary osteosarcoma tissue seems to be closely correlated with the prognosis of the patients.
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PMID:Prognostic significance of bone morphogenetic activity in osteosarcoma tissue. 342 72

Bone morphogenetic activity of osteosarcomas from 20 patients was assayed. The activity was demonstrated as ectopic bone formation on implantation of a lyophilized fraction of the tumor into athymic nude mice in 8 of 20 cases. Osteosarcomas producing bone morphogenetic protein (BMP) differed in clinical features from those not producing BMP. They were characterized radiologically by perpendicular spicules, histologically by osteoblastic type cells, and clinically by an increased serum alkaline phosphatase level, relative resistance to preoperative chemotherapy with Adriamycin (doxorubicin) plus high-dose methotrexate, and a tendency to metastasize to other bones and the lungs.
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PMID:Clinical significance of bone morphogenetic activity in osteosarcoma. A study of 20 cases. 386 Dec 32

The morphologic events and macromolecular interactions in matrix-induced bone formation are comparable with those occurring in the development of fracture callus. Thus, bone induction by decalcified bone matrix is an experimental model for fracture healing and a new tool for research concerning the biochemistry of bone cell differentiation. Three conditions are necessary for bone cell differentiation in postnatal life: (1) a three-dimensional pattern of proliferation of mesenchymal cells; (2) anchorage-dependent microvilli extending the proliferating cells; and (3) a locally released bone morphogenetic protein (BMP). To date, BMP with a molecular weight of 17,500-18,500 daltons has been isolated from bone, and a BMP-like protein with a molecular weight of 22,000 daltons has been extracted from mouse osteosarcoma. It is difficult to separate BMP, a collagenase-resistant, trypsin-labile acidic polypeptide, from several other low molecular weight proteins.
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PMID:Postnatal new bone formation. 670 31

A selection of proteins including bone morphogenetic protein (BMP) was extracted in a disaggregated form from Dunn osteosarcoma or rat demineralized bone matrix by 4M guanidine hydrochloride (GuHCl) solution without losing its biological activity. The GuHCl extracts of Dunn osteosarcoma were divied into 4 different fractions by cesium chloride (CsCl) density gradients. Under a dissociative condition, the highest new bone yield was obtained in the low dense top one-third fraction, and BMP acitivity declined with increase in the density of each fraction. No BMP potential was observed in the surface-gel fraction under dissociative conditions. Under an associative condition (low GuHCl concentrations), BMP activity appears in the surface-gel fraction, while under a dissociative condition (high concentrations of GuHCl) BMP appears in the fraction below the surface gel. These facts suggest that under associative conditions, BMP aggregates with other low dense proteins in the surface-gel fraction and that this may be the state of aggregation of BMP in cells and matrix in nature. Present observations support the assumption that BMP is a relatively low density protein and excludes the idea of BMP activity in the collagen molecule, per se. A specific protein, with an apparent molecular weight of 63,000 daltons, is present in all fractions that exhibit BMP activity, and absent in fractions that do not exhibit this activity. BMP is not species-specific; rat BMP induces bone formation in mice. CsCl density-gradient centrifugation is an efficient tool for further purification and isolation of BMP.
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PMID:Solubilized bone morphogenetic protein (BMP) from mouse osteosarcoma and rat demineralized bone matrix. 692 47

The 4 M GuHCl soluble proteins of Dunn osteosarcoma were fractionated in two steps by means of CsCl density gradient centrifugation. Further purification of bone morphogenetic protein (BMP) was accomplished by molecular sieve techniques utilizing thin-channel diafiltration (Amicon), Sepharose CL-6B and Sephacryl S-200 gel filtration. Partially purified BMP fractions were analyzed by electrophoresis on 7.5% SDS polyacrylamide gel. The molecular weight of BMP active fractions ranges from 30,000 to a few thousand daltons. BMP may be one of the two proteins of MW of 12,500 and 16,000 daltons.
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PMID:Solubilization and purification of bone morphogenetic protein (BMP) from Dunn osteosarcoma. 693 61

A bone morphogenetic protein (BMP) fraction obtained from the organic matrix of dentin is extractable from human osteosarcoma. A fresh en-bloc specimen excised from the femur of a 16-year-old boy was extracted with 4 M guanidine hydrochloride. The GuHCl-soluble, water-insoluble protein fraction induced new bone formation when implanted into the thigh muscles of athymic nude mice.
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PMID:Human osteosarcoma-derived soluble bone morphogenetic protein. 693 75

Insulin-like growth factors (IGFs) are found in human circulation predominantly as part of a growth hormone (GH)-dependent complex of 125-150 kD, which is composed of three subunits: IGF-I or IGF-II, an acid stable IGF binding protein (IGFBP)-3, and an acid labile subunit (ALS). Although recent studies demonstrate that a number of cell types in culture secrete IGFs and IGFBP-3, very little is known with regard to the origin of circulating ALS. To test the hypothesis that human bone cells (HBCs), which produce abundant amounts of IGF-II and IGFBP-3, also produce ALS, we measured the IGF-I, IGF-II, IGFBP-3, and ALS levels using specific radioimmunoassays (RIAs) in the conditioned medium (CM) of untransformed normal HBCs and SaOS-2 osteosarcoma cells treated with various effectors (IGF-II, osteogenic protein-1 [OP-1, bone morphogenetic protein-7] and human GH) for 48 h. No detectable levels (< 3 ng/ml) of ALS were found in the CM of various HBC types under basal conditions. In contrast, CM collected from liver explants in culture contained significant amount of ALS prepared and assayed under identical conditions. The IGF-I level was also undetectable in the CM of various HBC types. In the IGF-II (3, 30 ng/ml)-treated HBC CM, the IGFBP-3 level was increased in a dose-dependent manner but neither IGF-I nor ALS could be detected. In the SaOS-2 cell culture, OP-1 (1, 100 ng/ml) increased both IGF-II and IGFBP-3 secretion but neither ALS nor IGF-I secretion. Treatment of HBCs with GH (1, 10, 100 ng/ml) had no significant effect on the secretion of either IGF-I, IGF-II, IGFBP-3, or ALS.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Evidence that human bone cells in culture secrete insulin-like growth factor (IGF)-II and IGF binding protein-3 but not acid-labile subunit both under basal and regulated conditions. 757 8


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