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Query: UMLS:C0026764 (
multiple myeloma
)
36,148
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
An anterior operative procedure using a strut of fibular graft material was performed either alone or in combination with a posterior stabilization in five patients with cervical spine instability secondary to neoplastic disease. Osseous tumor was present in four of the five patients (osteoblastoma, metastatic adrenal carcinoma, metastatic renal cell carcinoma,
multiple myeloma
) and the fifth had spine instability as a result of a posterior decompression for cervical spinal cord
glioma
. The anterior approach using fibula to replace diseased vertebrae and provide axial support for the neck was a valuable therapeutic modality in this group of patients, all of whom had a limited life expectancy. Cervical spine stability obtained by operative intervention led to a reduction of neck pain and maintenance of ambulation until the neoplastic condition became terminal.
...
PMID:Anterior fibular strut graft in neoplastic disease of the cervical spine. 50 8
Brain tumors have been tested for their glial fibrillary acidic protein (GFAP) content by means of the rocket electrophoresis technique. Meningiomas and neurinomas were low in GFAP. Metastases had a low level of GFAP except when contaminated with surrounding tissue. Non-nervous tumors such as
myeloma
, myeloplaxoma and adenocarcinoma gave negative results. More detailed correlations with histological observations have been looked for in
glial tumors
. Low levels of GFAP were always associated with signs of malignancy such as mitoses and giant or atypical cells, whereas high levels of GFAP were correlated with the presence of well-preserved astrocytes.
...
PMID:Determination of glial fibrillary acidic protein (GFAP) in human brain tumors. 62 58
Utrophin, the autosomal dystrophin-related protein (DRP), is expressed in HeLa cells, smooth muscle-like BC3H1 cells from mouse brain, COS monkey kidney cells, the P388D1 monocyte-macrophage cell line and untransformed human skin fibroblasts, as well as in rat C6
glioma
and Schwannoma cells. It was undetectable, however, in the Sp2/O mouse
myeloma
cell line and in hybridoma lines derived from it. Dystrophin was not detected in any of these cell lines. Although all utrophin-containing cells were capable of forming monolayers in culture, no major effects of either attachment to substratum or length of time in culture (2-17 days) on utrophin levels were observed. After subcellular fractionation of BC3H1 or
glioma
cells, nearly all of the utrophin was found in the Triton-soluble fraction, suggesting an association with cell membranes.
...
PMID:Utrophin, the autosomal homologue of dystrophin, is widely-expressed and membrane-associated in cultured cell lines. 142 62
Six monoclonal antibodies (mABs) against human
glioma
cells (T2) were produced. T2 cells grown as solid tumors in nude mice, were dissociated and used to immunize Balb/c mice. After fusion of splenocytes with
myeloma
cells, eight hybrids secreting mABs were selected according to their ability to react immunohistochemically with T2 cells, but not with normal adult human brain. Cytotoxicity of mABs was tested using (3H)-thymidine incorporation assays in vitro. Four mABs showed complement-mediated cytotoxicity for T2 cells, other human
glioma
cells (T1), and a human melanoma cell line. Incubation with one antibody, mAb2A1, lowered (3H)-thymidine incorporation in the T2 and T1 cells to ca. 10%, and in melanoma cells to ca. 35% of control levels. Another antibody, mAb3B2, displayed a similar cytotoxicity for T2 and T1 cells, but did not show measurable cytotoxicity for melanoma cells and rat primary astrocyte cultures. Moreover, this antibody did not crossreact with haematopoietic cells from patients bearing CNS tumors or normal subjects. MAb3B2, therefore, appears to recognize and epitope associated to human gliomas, will be a useful
glioma
tumor marker and may have some potential therapeutical value.
...
PMID:Murine monoclonal antibodies cytotoxic to human glioma cells in vitro. 145 84
ZO-1 is a high molecular mass phosphoprotein peripherally associated with the cytoplasmic surface of tight junctions in epithelial and endothelial cells. We report here that ZO-1 is also present in several nonepithelial cell types in vitro that are not believed to form tight junctions, including primary cultures of astrocytes, Schwann cells, and dermal fibroblasts and the C6
glioma
, S-180 (sarcoma), and P3
myeloma
cell lines. Immunoblots of cell extracts probed with a ZO-1-specific monoclonal antibody reveal a single band that comigrates with ZO-1 from rodent epithelial cells at 225 kDa. In addition, these cells contain a single mRNA species of identical size to that previously reported for ZO-1 in epithelial tissues, as determined by Northern blots probed with a partial ZO-1 cDNA. Immunofluorescence microscopy demonstrates diverse ZO-1 distributions in these cells. In astrocytes, identified by the presence of glial fibrillary acidic protein, ZO-1 is localized at discrete sites of cell-cell contact as well as within the cell cytoplasm. In contrast, S-180 cells display diffuse staining at the cell periphery and within the cytoplasm. Dermal fibroblasts show no staining above background, although ZO-1 was detected on immunoblots of fibroblast cell extracts. Immunofluorescence staining of frozen sections of mouse brain demonstrates no detectable ZO-1 immunoreactivity outside blood vessels where endothelial cell tight junctions of the blood-brain barrier are located. These studies suggest that, although ZO-1 is found to be associated with the tight junction, it has a broader distribution than previously recognized.
...
PMID:Detection of the tight junction-associated protein ZO-1 in astrocytes and other nonepithelial cell types. 153 34
Mouse
myeloma
cells were fused with spleen cells from mice that had been immunized with a human ependymoma derived cell line, KMS II. Hybridomas producing monoclonal antibodies (MAbs) were screened and cloned. Specificity of the antibody was determined by enzyme-linked immunosorbent assay (ELISA) and/or indirect immunofluorescence assay. One of the MAbs, designated Ep-C4 (subclass = IgG1), reacted with two cell lines derived from ependymoma but did not react with 17 cell lines derived from other types of brain tumor nor with 4 neuroblastoma cell lines or 19 cell lines derived from carcinoma, hematopoietic tumors and amnion. Indirect immunofluorescence and immuno-electron microscopy studies revealed that the antigen recognized by MAb Ep-C4 was located on cell surface membrane. The membrane antigen of KMS II cells, immunoprecipitated by MAb Ep-C4, was a protein of 81,000 dalton. The reactivity of MAb Ep-C4 was further examined using immunofluorescence and/or immunoperoxidase methods and frozen sections and short-term cultures of various types of brain tumors. No cross-reactivity with normal adult or fetal brain tissues was detected by absorption assay and immunoperoxidase staining. Our results suggest that the antigen defined by MAb Ep-C4 is specific for ependymoma cells, and different from the antigens of
glioma
cells or other neuroectodermal-derived cells previously described.
...
PMID:Monoclonal antibody against ependymoma-derived cell line. 154 75
Three murine monoclonal antibodies, designated GA-17, GB-4, and GC-3, were prepared by the hybridization of murine
myeloma
cells (NS-1) and spleen cells of BALB/c mice immunized with the crude membrane fraction of cultured human gliosarcoma cells (GI-1). Two of them (GA-17 and GB-4) reacted exclusively with the membrane of
glioma
cells, and the other (GC-3) reacted with the membrane of
glioma
cells and a T cell line (MOLT-4). Although these antibodies reacted with almost all of the gliomas, the reactions differed. GA-17 reacted equally well with all glioblastoma (17 cases) and low-grade astrocytoma (10 cases), whereas GB-4 reacted poorly with 7 cases of glioblastoma and GC-3 did not react with 7 cases of low-grade astrocytoma. The antigens, exclusively expressed on the cell surface, were analyzed by surface labeling with 125I followed by a cell lysis and immunoprecipitation with these antibodies. The findings obtained by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that GA-17, GB-4, and GC-3 reacted with Mr 140,000-145,000, Mr 160,000, and Mr 145,000-150,000 proteins, respectively. Some evidence has been obtained indicating that these antigens are composed of the same polypeptide chain (Mr 120,000) with the carbohydrate chains being different.
...
PMID:Human glioma-specific antigens detected by monoclonal antibodies. 158 48
Interferons are currently the most widely used biological response modifiers. They are of high clinical value in haematological malignancies (chronic myelogenous leukaemia,
multiple myeloma
, non-Hodgkin lymphoma), in solid tumours (malignant melanoma, hypernephroma, pancreas neoplasms, carcinoid tumours, Kaposi's sarcoma,
glioma
, in ovarium, cervix and bladder carcinoma, and in basalioma) and in infectious diseases (chronic hepatitis B, chronic non-A/non-B hepatitis, chronic delta hepatitis, AIDS, Papova virus and Rhinovirus infections, leishmaniasis, leprosy) and some other conditions. Although the mechanism of action of interferons has not been explained in every detail these agents are promising therapeutic means in a number of diseases.
...
PMID:Role of interferon in clinical practice. 172 32
Dilated cisternae of the ER resembling Russell Bodies (RBs) are induced in light (L) chain producing
myeloma
cell lines by transfection of a mu heavy (H) chain gene lacking the first constant domain (mu delta CH1). RBs do not appear to be tissue specific, since they are also induced in a rat
glioma
cell line transfected with mu delta CH1 and L chain genes. Efficient RB biogenesis requires H-L assembly and polymerization. The mutant Ig is partially degraded in a pre-Golgi compartment. The remnant, however, becomes an insoluble lattice when intersubunit disulphide bonds are formed. The resulting insoluble aggregate accumulates in RBs. Replacing the COOH-terminal cysteine of mu delta CH1 chains with alanine reverses the RB-phenotype: the double mutant mu ala delta CH1 chains assemble noncovalently with L and are secreted as H2L2 complexes. Similarly, secretion of mu delta CH1 chains can be induced by culturing transfectant cells in the presence of reducing agents. The presence of RBs does not alter transport of other secretory or membrane molecules, nor does it affect cell division. Resident proteins of the ER and other secretory proteins are not concentrated in RBs, implying sorting at the ER level. Sorting could be the result of the specific molecular structure of the insoluble lattice. We propose that RBs represent a general response of the cell to the accumulation of abundant, nondegradable protein(s) that fail to exit from the ER.
...
PMID:Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum. 195 67
Monoclonal antibody against 2',3'-cyclic nucleotide 3'-phosphohydrolase (CNP) was generated by fusing mouse
myeloma
cells with spleen cells from BALB/c mice immunized with delipidated white matter from rat corpus callosum. The antibody was characterized by solid-phase radioimmunoassay, immunoblot of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), immunoprecipitation from C6
glioma
cells, and indirect immunofluorescence staining of monolayer cultures containing oligodendrocytes. The monoclonal antibody bound specifically to an intracellular antigen of oligodendrocytes, but not to Schwann cells, astrocytes, neurons, or fibroblast cytoplasm. The immunoblot of SDS-PAGE of CNS myelin showed that the antibody identified two protein bands at 48,000 and 50,000 molecular weight. These proteins were not identified in peripheral nervous system myelin. The monoclonal antibody immunoprecipitated CNP enzyme activity from extracts of C6
glioma
cells. This monoclonal antibody should prove useful in further study of this myelin-specific enzyme in CNS myelin and in cells responsible for myelin production.
...
PMID:A monoclonal antibody raised to corpus callosum extract reacts with 2',3'-cyclic nucleotide 3'-phosphohydrolase. 299 39
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