UMLS:C0026764 - FACTA Search

Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Target Concepts:

Query: UMLS:C0026764 (multiple myeloma)
36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The expression of neutral glycosphingolipids (GSL) in 37 B-cell neoplasms [7 acute lymphocytic leukemia (ALL), 5 Burkitt's lymphoma (BL), 7 chronic lymphocytic leukemia (CLL), 5 diffuse, poorly differentiated lymphoma (DPDL), 6 diffuse histiocytic lymphoma (DHL), 3 hairy-cell leukemia (HCL), and 4 multiple myeloma (MM)] was examined. Patterns of expression of simple (GlcCer, LacCer) and globo-series GSL (Gb3, Gb4) were found for each tumor type. In addition, pre-B ALL expressed the neo-lacto series GSL, paragloboside, which was not significantly seen at later stages of maturation. As a group, leukemias expressed about 10 times higher ratios of simple GSL to Globo-series GSL as compared to lymphomas, regardless of stage of differentiation. Significant amounts of GSL of other series were not found except in one CLL which contained asialo-GM2. GSL phenotype in these cells was not grossly affected by cell genotype since pre-B ALL containing Philadelphia chromosome t(9q;22q) translocations were similar to other ALL; and DHL with t(8q;14q) translocations had GSL patterns similar to other DHL samples and dissimilar to GSL patterns found in Burkitt's lymphomas with t(8q;14q). Differences in GSL expression among the different types of B-cell neoplasm suggested that GSL patterns form a phenotypic map that may complement the traditional glycoprotein immunophenotypic map and contribute to our understanding of the biology of these diseases and B-cell differentiation.
...
PMID:Neutral glycosphingolipid expression in B-cell neoplasms. 195 88

BALB/c mice were immunized with gelonin, a 30 kD glycoprotein (type 1 RIP) from the seeds of Gelonium multiflorum. By polyethylene glycol-induced fusion of isolated spleen cells with the myeloma cell line NS-1, three different hybridomas were obtained. Two of them were found to secrete antibodies of the IgG1 subclass, whereas the third cell line produced antibodies of the IgM type. The IgG1-secreting cell lines were adapted to serum-free medium conditions, and the antibodies were isolated from the culture supernatant. The isolated antibodies recognize independent epitopes on the gelonin molecule. The toxicity of gelonin in reticulocyte lysates was not affected when the protein was incubated with the antibodies. The IgG1s exhibit average affinity constants of about 10(9) M-1 and 10(10) M-1, respectively, as determined by a solid-phase EIA using the avidin-biotin system.
...
PMID:Monoclonal antibodies to gelonin: production and characterization. 203 35

Several studies have been performed in the last ten-years on the biochemical and physiopathologic properties of angiotensin-converting enzyme (ACE). Human lung and kidney are a rich source of ACE and the enzyme is bound to the plasma-membrane of vascular endothelial cells; however, the small intestine and the choroid plexus are also particularly rich in ACE, where it is concentrated on the surface of cuboidal epithelial cells facing the cerebrospinal fluid. The ACE is a glycoprotein with a molecular weight of 150,000 daltons and it cleaves C-terminal dipeptides of several oligo-peptides, including angiotensin I and bradykinin. It catalyzes conversion of angiotensin I to angiotensin II and induces inactivation of bradykinin. Synthetic acylated tripeptides such as radiolabelled hippuryl-histidyl-leucine and hippuryl-glycyl-glycine have been found to be the most suitable substrates for determining the activity of ACE with radiochemical assays. The mean-normal values for ACE activity is 25 U/ml; there are no significant differences in ACE activity between different sexes and races, but there is significant decrease in adults. The measurement of ACE activity in sarcoidosis suggests the following results: 1) There is a relationship between the increased SACE and LACE activity and active disease and between normal ACE activity and inactive disease. 2) Normal or decreased ACE activity is useful for therapeutic evaluation of sarcoidosis. 3) Increased SACE activity can be a sensitive parameter for predicting clinical relapse of the disease. An increased SACE activity is found in a wide variety of non-sarcoid granulomatous diseases and non-granulomatous systemic diseases. A decreased SACE and LACE activity is found in non-granulomatous pulmonary diseases such as "Adult Respiratory Distress Syndrome", lung cancer and lung toxicity caused by antineoplastic drugs. Moreover, a low preoperative SACE is associated with poor prognosis in lung cancer and its levels may be useful for predicting clinical relapse of this disorder after operation. Finally, a low SACE activity is found in malignant lymphomas, leukemia and multiple myeloma. A relationship is also found between decreased enzyme activity and a poor prognosis and clinical relapse of these diseases.
...
PMID:[ACE: physiopathology and role in the diagnosis and prognosis of systemic granulomatosis, neoplasms and lung toxicity caused by antineoplastic agents]. 217 27

Murine monoclonal antibodies that distinguish glandular from squamous epithelia in human tissue were generated using a procedure that involved tolerization prior to immunization. Tolerization was achieved by injection of newborn (24 hrs old) Balb/c mice with extract of normal cervical tissue containing squamous epithelium (the tolerogen). Three weeks later, mice showing no evidence of antibodies to tolerogen in their sera were immunized with an extract of cervical tissue containing both glandular and squamous epithelia. Following immunization, the sera from mice subjected to this treatment showed strong reactivity with glandular cells but not with squamous cells in sections of frozen tissue examined by an indirect immunohistological method. Spleen cells from mice showing this pattern of serum reactivity were used as fusion partners with a mouse myeloma cell line in order to generate monoclonal antibodies. Following extensive screening, one monoclonal antibody (designated anti-GEA.49) was selected for further study on the basis of reactivity with high affinity to glandular epithelium and a complete absence of staining of squamous and connective-tissue cells. Detailed tests of specificity and patterns of reactivity indicate that the antigen detected by the antibody is expressed on the apical plasma membrane of glandular epithelia and is a glycoprotein with an apparent molecular weight of 49 kilodaltons. Both immunohistological and biochemical methods demonstrated the expression of the antigen on glandular epithelia but not on squamous epithelia from several sources, underlining the usefulness of tolerization/immunization approach for generating antibodies with particular specificity requirements.
...
PMID:Generation and characterization of a murine monoclonal antibody to cervical glandular epithelium using mice rendered tolerant to cervical squamous epithelium. 218 26

Spleen cells from inbred Biozzi mice, immunized against the human breast cancer cell line T47D, were fused with murine myeloma SP2O cells to generate monoclonal antibodies. One of these, 1BE12, of IgM isotype, reacted with five of six human breast tumor cell lines, while no binding was detectable with normal lymphocytes, RBC, or fibroblasts. The antigen recognized by monoclonal antibody 1BE12 was localized on the surface of T47D and MCF7 cells and was detected in cell-free supernatants of cultures. The antigen was found also on the surface of milk secretory cells. Immunohistochemical staining of frozen and paraffin-embedded sections of human tissues showed apical polarized reactivity in normal breast glands, while in all breast cancers staining was either cytoplasmic or membranous and heterogeneously distributed. Immunostaining was also observed in some other normal epithelia, including salivary gland, gastroduodenal mucosa, exocrine pancreas, and cervix. The antigen was not detectable in secretory endometrium, whereas proliferative endometrium was strongly stained. Colon carcinoma, and cancers of the bladder and endometrium were strongly reactive. No staining was detected in melanoma, lymphoma, mesothelioma, non-small cell lung carcinoma, and thyroid, renal, and ovarian carcinomas. Lectin absorption of MCF7 membrane extracts reduced 1BE12 binding. A large reduction in 1BE12 reactivity was observed after digestion of T47D and MCF7 membrane extracts with proteases. Treatment with sodium periodate resulted in complete loss of antigenicity, while neuraminidase treatment did not affect 1BE12 binding. These findings suggest that the 1BE12 epitope is expressed on the carbohydrate moiety of a glycoprotein and does not contain sialic acid. Immunoblotting of the perchloric acid-soluble fraction of MCF7 membrane extracts after electrophoresis in 1% agarose detected the antigen as a high molecular weight species (Mr greater than 900,000). The antigen was purified by perchloric acid extraction of MCF7 membrane preparations followed by affinity chromatography on 1BE12 antibody coupled to Sepharose-4B and gel exclusion fast protein liquid chromatography. No reactivity of the purified material was found with monoclonal antibodies directed against human milk fat globule membrane-associated mucins HMFG1 and DF3.
...
PMID:Characterization and distribution in human tissues of a glycoproteic antigen defined by monoclonal antibody 1BE12 raised against the human breast cancer cell line T47D. 222 61

A variety of tubular marker proteins, as compared to healthy controls, are excreted at an increased rate in the urine of patients with renal damage. Beside cytoplasmic glutathione-S-transferase and lysosomal beta-N-acetyl-glucosaminidase (beta-NAG) the majority of kidney-related urine proteins derives from membrane surface components of the most vulnerable proximal tubule epithelia, among them ala-(leu-gly)-aminopeptidase, gamma-glutamyl transpeptidase (GGT), the tubular portion of angiotensinase A, the major brush border glycoprotein 'SGP-240' and adenosine-deaminase-binding protein. Urinary tissue proteins, e.g. brush border (BB) microvilli, are immunologically identical with those antigens prepared from cell membranes of the human kidney itself. BB antigens are shed into the urine of patients with glomerulonephritis, interstitial nephritis, systemic diseases, e.g. systemic lupus erythematosus (SLE), diabetes mellitus and multiple myeloma, arterial hypertension, infectious diseases (malaria, AIDS) and after operations, renal grafting and administration of X-ray contrast media, aminoglycosides or certain cytostatics (cis-platinum). Tissue proteinuria of tubular proteins is determined by enzyme-kinetic or quantitative immunological assays applying either poly- or monoclonal antikidney antibodies. Clinical, ultrastructural and histochemical studies support the idea that both 'soluble' and high-molecular-weight membrane particles (vacuolar blebs, greater than 10(6) dalton) as well as microfilamental components of the epithelial cytoskeleton contribute to tubular 'histuria' which appears as a sensitive parameter in monitoring tubular damage under clinical conditions at a very early phase.
...
PMID:Urinary proteins of tubular origin: basic immunochemical and clinical aspects. 225 76

The polyclonal antibodies to juveniles of Paragoniums westermani (PwJ-PcAbs) from sera of Wistar rats infected with Paragoniums westermani (P.w.) were purified by Sephadex G 200 chromatography. Next the shared serological antigens of P.w. metacercaria and juveniles (PwMJ-SAg) from the crude antigens of the metacercariae (M-NS-Ag) were purified with immuno-affinity chromatography on cyanogen bromide-activated cross-linked Sepharose 4B beads coupled with PwJ-PcAbs. PwMJ-SAg, a group of glycoprotein molecules shown by the staining test, were specific serological antigens of P.w. metacercariae and juveniles, identified by the immunoabsorb test and immunoelectrophoresis. By SDS-PAGE, PwMJ-SAg were fractionated to seven bands, including major bands A (27.5 K) and Bi (19.5 K), the two major serological antigen molecules. 20 sera samples from the patients with the nonpulmonary type of P. w. paragonimiasis were detected using PwMJ-SAg and M-NS-Ag by Dot-ELISA, and the difference of sensitivity between two antigens was highly statistically significant (P less than 0.001). BALB/c mice, in the early stage of infection with P. w. metacercaria, were immunized with PwMJ-SAg. The spleen cells of the mice were isolated and fused with SP2/o, a murine myeloma cell line. After three subclonal cultures, eight cell lines secreting monoclonal antibodies (McAbs) to PwMJ-SAg were prepared from 384 wells of hybridoma cells. All McAbs were IgG1 subclass.
...
PMID:Studies on specific serological antigens in metacercariae and juveniles of Paragoniums westermani and its monoclonal antibodies. 234 88

T cell glycoprotein CD4 binds to class II major histocompatibility molecules and to the human immunodeficiency virus (HIV) envelope protein gp120. Recombinant CD4 (rCD4) bound to polyclonal immunoglobulin (Ig) and 39 of 50 (78%) human myeloma proteins. This binding depended on the Fab and not the Fc portion of Ig and was independent of the light chain. Soluble rCD4, HIV gp120, and sulfated dextrans inhibited the CD4-Ig interaction. With the use of a panel of synthetic peptides, the region critical for binding to Ig was localized to amino acids 21 to 38 of the first extracellular domain of CD4. CD4-bound antibody (Ab) complexed with antigen approximately 100 times better than Ab alone. This activity may contribute to the Ab-mediated enhancement of cellular HIV interaction that appears to depend on a trimolecular complex of HIV, antibodies to gp120, and CD4.
...
PMID:Human CD4 binds immunoglobulins. 236 51

The preparation of monoclonal antibodies (MAbs) against the human milk fat globule membrane with preferential binding to breast carcinoma cells is described. Using BALB/c mouse myeloma cells; inter-specific, intra-strain, and inter-strain hybridomas were isolated that identified three different components of the human milk fat globule of approximately 46,000, and 70,000 daltons and a mucin-like glycoprotein complex (NPGP) ranging from 400,000 to over a million daltons, respectively. Three MAbs (BrE1, BrE2, BrE3) identified the latter component which consists of at least three different size molecules for which the aforementioned MAb's have different binding specificities. MAbs, BrE2 and BrE3, bound to normal breast epithelial cells but to a lesser extent than to tumors and only at the apical surface facing the lumen, while they bound breast carcinomas strongly, and often in the cytoplasm as well as on the surface. Higher concentrations of BrE3 were required to stain normal breast compared to breast tumors. BrE1 also stained breast carcinomas both on the surface and cytoplasmically but did not stain normal breast tissue. The MAb, Mc13, as well as the previously reported MAb McR2, both against the 70,000 dalton component, did not significantly stain either normal or cancerous breast tissue in histological sections but did bind significantly to cultured breast epithelial cells and to the milk fat globule membrane. The MAbs, Mc8 and Mc3, reported previously to be against the 46,000 dalton component, stained histologically only malignant breast tissue but only weakly; however, they bound strongly to intact breast carcinoma cells and breast cell membrane preparations with a radioimmunobinding assay. These MAbs should be useful in characterizing the surface of breast epithelial cells, studying surface alterations in malignancy, and possibly in breast cancer diagnosis and therapy.
...
PMID:Biochemical and histological characterization of antigens preferentially expressed on the surface and cytoplasm of breast carcinoma cells identified by monoclonal antibodies against the human milk fat globule. 236 81

Gamma seminoprotein (gamma Sm), a glycoprotein isolated from human seminal plasma with a molecular weight of 29,000 and possibly a serine protease, has been demonstrated to be one of the prostate organ-specific antigens. We established a murine monoclonal antibody (MoAb) to gamma-Sm in order to prove the presence and localization of this protein in the prostate. The hybrid clones were obtained by fusing mouse SP2/O-Ag-14 myeloma cells with splenocytes from Balb/c mouse immunized with the major fractions of gamma-Sm. The enzyme-linked immunosorbent assay was done for antibody screening. After cloning twice in soft agarose, the stable clone, termed 43-21-1-1, was finally chosen. This MoAb, IgG1(kappa), recognized gamma-Sm specifically, which was verified by an immunoblotting assay. The specificity of the MoAb was further evaluated by immunohistochemical study by the avidin biotin complex method. Periodate-lysine-paraformaldehyde-fixed surgical specimens, including the prostate associated with fibromuscular hyperplasia, seminal vesicles, bladder, testis and epididymis, were examined. Formaldehyde (10%)-fixed surgical specimens from patients with adenocarcinoma of the prostate and primary transitional cell carcinoma arising from the periurethral prostatic ducts were also examined. Positive reactions of gamma-Sm were recognized only in the cytoplasm of prostatic glandular epithelial cells and along the luminal surface. Fibrous and muscular tissues always given negative staining. Neither nonprostatic tissues nor transitional cell carcinoma of the prostate were stained positively for gamma-Sm. These results show that this MoAb (43-21-1-1) is quite specific to gamma-Sm and may be useful for the immunohistochemical study with prostatic tissue.
...
PMID:[Preparation and characterization of monoclonal antibody to gamma seminoprotein]. 240 88

<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>