Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Monoclonal antibodies (MoAbs) against human osteosarcoma cells were obtained by the fusion of NS/1 mouse myeloma cells with spleen cells from the human osteosarcoma cell line-immunized BALB/c mice. Two hybrid clones were established and designated as 2H10 and 2D3. Both MoAbs reacted strongly with all osteosarcoma tissues but not with other bone and soft tissue tumors such as chondrosarcoma, malignant fibrous histiocytoma, liposarcoma, leiomyosarcoma, and rhabdomyosarcoma. In addition, neither MoAb reacted with tumor cell lines and tissues obtained from other cancers. Immunohistochemical analysis demonstrated that 2H10 and 2D3 reacted with endothelial cells in sarcoma tissues, but not with those of other tumors and normal tissues. 2H10 also reacted with cells on the basal layer of epidermis of the skin. 2H10- and 2D3-defined antigen has an approximate molecular weight of 75,000 under nonreducing and reducing conditions, indicating that the antigen has a single chain structure and there is no intramolecular disulfide bond. 2H10- and 2D3-defined antigen has a pI value between 5.5 and 6.2. Sequential immunoprecipitation analysis clearly demonstrated that 2H10 and 2D3 recognized the same antigen molecule. However, further analysis suggested the possibility that 2H10 and 2D3 MoAbs recognized the different antigenic determinants on the same antigen molecule.
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PMID:Monoclonal antibodies that detect different antigenic determinants of the same human osteosarcoma-associated antigen. 245 Jun 50

A monoclonal anti-testicular carcinoma antibody was obtained via the somatic cell fusion technique by immunization of BALB/c mice with freshly prepared single cell suspension from a patient with testicular embryonal carcinoma with choriocarcinoma components. The hybridoma supernates were screened against the testicular carcinoma cells used in the immunization as well as normal mononuclear white blood cells isolated from the same patient. An antibody (5F9) was selected which bound to fresh tumor cells from two patients with embryonal testicular carcinoma and failed to bind to fresh tumor cells from 24 patients (2 seminoma, 2 melanoma, 3 neck, 2 esophageal, 1 ovarian, 3 colon, 1 prostate, 2 breast, 1 liposarcoma, 3 endometrial, 1 kidney, 1 adrenal, 1 larynx and 1 bladder tumors) or cell suspensions prepared from normal liver, lung, spleen, ovary, testes, kidney, red blood cells or white blood cells. The antibody was tested for its binding to several well established cancer cell lines, and was found to bind to the BeWo human choriocarcinoma and two human embryonal carcinoma cell lines. The antibody did not react with 22 other cell lines or with hCG. The antibody was labeled with 131I and injected into nude mice bearing BeWo tumors and evaluated for tumor localization by performing whole body scans with a gamma camera 5 days later. Six mice injected with the antibody showed positive tumor localization without the need for background subtraction while six mice injected with MOPC-21, a murine myeloma immunoglobulin, demonstrated much less tumor localization. Tissue distribution studies performed after scanning showed specific tumor localization (8:1 tumor: muscle) for the monoclonal antibody and no specific localization for MOPC-21. This antibody thus has selective reactivity with the surface of tumor cells from embryonal carcinoma (testicle) and choriocarcinoma both in vitro and in vivo.
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PMID:Development and characterization of a monoclonal antibody to human embryonal carcinoma. 303 38

We report a case of clear cell myeloma misinterpreted at initial biopsy as liposarcoma. The patient had lytic skeletal lesions and monoclonal IgA, kappa, serum immunoglobulin. The tumor cells contained cytoplasmic vacuoles that produced a clear histologic appearance. The light-microscopic and ultrastructural findings are compared with those of other cases of lymphoplasmacytic disorders with prominent cytoplasmic inclusions.
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PMID:Clear cell myeloma. 397 83

Haemangiosarcoma of bone is a very rare primary tumour with a variable history and differing radiographic and histological appearances. In some cases the lesion has similar features to the so-called "adamantinoma of long bones" in which the histogenesis is also unknown. Such a lesion is described which occurred in the shaft of the right humerus of a 31-year-old man. Radiographically a centrally located area of osteolysis was seen without marginal sclerosis, but with erosion of the bony cortex. A biopsy was performed 16 months after the first radiographic examination and showed malignant tumour tissue which was difficult to classify histomorphologically. Several different neoplasms such as Ewing's sarcoma, myeloma, liposarcoma, malignant fibrous histiocytoma or a bone metastasis were suggested. Finally, a haemangiosarcoma or so-called "adamantinoma of long bones" was considered. The tumour was completely removed by en-bloc resection. Careful histomorphological investigation of the tumour tissue by means of light microscopy, cytology and electronmicroscopy showed a vascular pattern characteristic of a haemangiosarcoma. Using cytophotometric DNA measurements of the tumour cells, the lesion could be classified as being of low-grade malignancy. This is confirmed since there has now been a 4-year follow up with no local recurrence or metastasis. There are many similarities between a well-differentiated haemangiosarcoma and an "adamantinoma of long bones". The differential diagnosis and the histogenesis of the latter lesion is discussed.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Haemangiosarcoma of bone. 404 May 2

The occurrence of skeletal malignancies has been documented among 234 young adult beagles given single intravenous injections of monomeric 239Pu citrate. Occurrence has also been documented among 132 comparable control group animals surviving the minimum latent time period of 2.79 y for radiation-induced bone cancer, who were maintained for lifespan observation. Injected amounts ranged from about 0.02-106 kBq kg-1 body mass with factors of 2 or 3 between dose levels. There were 84 radiographically apparent bone tumors in 76 plutonium-injected dogs and one tumor in a control group dog. Most of these were osteosarcomas except for seven chondrosarcomas, one liposarcoma, and one plasma cell myeloma of bone. The relationship between percent of dogs at any dose level with bone malignancy and average skeletal dose at the presumed time of tumor initiation of 1 y before death appeared to be linear below about 1.3 Gy average skeletal dose. The observed data can be approximated by the expression A = 0.76 + 75 D, where A = percent of dogs with bone cancer at any dose level, D = average skeletal dose in Gy (for doses up to 1.3 Gy) at tumor initiation, and 0.76 represents the percent tumor response in the control animals not given plutonium. Similar analysis of our corresponding data for beagles given 226Ra, excluding the two highest dose levels (approximately 100% occurrence), yielded the expression A = 0.76 + 4.7 D, where D = the average skeletal dose in Gy (for doses up to 20 Gy) at 1 y before death. The ratio of coefficients indicates the effectiveness for bone cancer induction of 239Pu relative to 226Ra, or [(75 +/- 22.5)(4.7 +/- 0.47)-1] = 16 +/- 5 for a single, brief intake of either nuclide into blood.
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PMID:Bone cancer occurrence among beagles given 239Pu as young adults. 841 14

Pigpen is a 67-kDa Sepharose-binding molecule isolated from mammalian endothelial and retinal pigmented epithelial cells. The protein is distributed nonhomogeneously in the nucleus, exhibiting diffuse staining throughout (excluding nucleoli), together with a small number of intensely stained focal points, or granules, and punctate staining along the nuclear envelope. Pigpen was absent or greatly attenuated in the nonepithelial cell types we examined, including fibroblasts, myeloma, and astroglia. cDNA sequence analysis revealed a positively charged molecule with an RNP-CS RNA-binding domain, 19 RGG repeats, and a consensus tyrosine phosphorylation site in the C-terminus. The amino terminal portion of the molecule is characterized by 7 glutamine-rich hexapeptide repeats similar to those found in the transactivation domain of known transcription activators. Pigpen has a high level of identity with the FUS gene product, TLS (Translocated in Liposarcoma; Crozat et al, 1993; Rabbits et al., 1993), a new member of the EWS family of proteins. Expression of pigpen is regulated during the transition between active and quiescent endothelial cell phenotypes. Both mRNA and overall protein levels are maintained at a steady level in actively growing cells. The number of nuclear granules increases as cultures approach confluency. When cells reach confluency, overall expression is sharply reduced and the number of nuclear focal points declines gradually. We observed that reactivation of endothelial cells locally by wounding of confluent cultures resulted in a spatially restricted reactivation of pigpen expression. This pattern of expression, taken together with structural data, suggests that pigpen may function in the growth and differentiation of endothelial cells during angiogenesis.
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PMID:A nuclear protein regulated during the transition from active to quiescent phenotype in cultured endothelial cells. 863 1

aP2 gene product (aP2 protein) expression has been shown to be a useful diagnostic marker for identification of lipoblasts and fetal fat cells in soft tissue tumours. A monoclonal antibody was developed by a mouse spleen cell-myeloma hybridoma technique to an 18 amino acid segment of the aP2 protein and was used to investigate the immunohistochemical expression of this protein in benign and malignant tumours of adipocytic differentiation and a wide variety of other soft tissue tumours. We found that aP2 protein was expressed by lipoblasts in liposarcomas and lipoblastomas and by brown fat cells in hibernomas and normal periadrenal fat. Other benign adipose tissue tumours and benign and malignant soft tissue tumours were distinguished from liposarcoma by absence of staining for aP2 protein. Immunohistochemical identification of the aP2 protein is likely to prove a useful means of distinguishing liposarcoma from other malignant mesenchymal and epithelial neoplasms, some of which contain cells that morphologically resemble lipoblasts.
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PMID:Development of a monoclonal antibody to the aP2 protein to identify adipocyte precursors in tumours of adipose differentiation. 1044 62

Reported herein is a case of retroperitoneal angiomyolipoma associated with amyloid deposition, masquerading as well-differentiated liposarcoma. A 16 x 13 cm lipomatous tumor was resected from the perirenal retroperitoneum of a 71-year-old woman. Microscopically, the tumor was exclusively composed of mature adipose tissue and abnormal thick blood vessels, but bundles of smooth muscle were lacking. In addition, amyloid was deposited between fat cells. Initially, well-differentiated liposarcoma was highly suspected. However, there were a few epithelioid cells with clear vacuolated cytoplasm within the vessel walls, which were immunoreactive for smooth muscle markers and HMB-45. Real-time polymerase chain reaction failed to demonstrate the amplification of the murine double-minute type 2 gene and cyclin-dependent kinase 4 gene in this tumor. Therefore, the tumor was diagnosed as lipomatous angiomyolipoma. After the diagnosis, it was found that the patient had multiple myeloma and cardiac amyloidosis, suggesting that the amyloid deposition within the tumor was a complication of the myeloma. Lipomatous angiomyolipoma may be a diagnostic pitfall of retroperitoneal lipomatous tumors.
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PMID:Retroperitoneal lipomatous angiomyolipoma associated with amyloid deposition masquerading as well-differentiated liposarcoma. 1698 23

BMS-754807 is a potent and reversible inhibitor of the insulin-like growth factor 1 receptor/insulin receptor family kinases (Ki, <2 nmol/L). It is currently in phase I development for the treatment of a variety of human cancers. BMS-754807 effectively inhibits the growth of a broad range of human tumor types in vitro, including mesenchymal (Ewing's, rhabdomyosarcoma, neuroblastoma, and liposarcoma), epithelial (breast, lung, pancreatic, colon, gastric), and hematopoietic (multiple myeloma and leukemia) tumor cell lines (IC50, 5-365 nmol/L); the compound caused apoptosis in a human rhabdomyosarcoma cell line, Rh41, as shown by an accumulation of the sub-G1 fraction, as well as by an increase in poly ADP ribose polymerase and Caspase 3 cleavage. BMS-754807 is active in vivo in multiple (epithelial, mesenchymal, and hematopoietic) xenograft tumor models with tumor growth inhibition ranging from 53% to 115% and at a minimum effective dose of as low as 6.25 mg/kg dosed orally daily. Combination studies with BMS-754807 have been done on multiple human tumor cell types and showed in vitro synergies (combination index, <1.0) when combined with cytotoxic, hormonal, and targeted agents. The combination of cetuximab and BMS-754807 in vivo, at multiple dose levels, resulted in improved clinical outcome over single agent treatment. These data show that BMS-754807 is an efficacious, orally active growth factor 1 receptor/insulin receptor family-targeted kinase inhibitor that may act in combination with a wide array of established anticancer agents.
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PMID:BMS-754807, a small molecule inhibitor of insulin-like growth factor-1R/IR. 1999 72