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)

Two cervical cancer cell lines CC7-T and Si-Ha were employed to observe the relationship between cervical cancer and prolactin. By immunocytochemical and indirect immunofluorescent assays using two prolactin monoclonal antibodies PRL-149 and PRL-151, both cell lines with added prolactin (10 ng/mL) were noted to be positive for PRL-151, but negative for PRL-149. The control cell lines from ovarian cancer and the myeloma lines were both stained negative. By using MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) assay, it was noted that CC7-T and Si-Ha grew better in the presence of various added concentrations of prolactin, ranging from 0.1 to 1,000 ng/mL, suggesting that prolactin may enhance the growth of cervical cancer. The degree of stimulation appears to depend on cell differentiation. However, prolactin levels in the cultured supernatant were undetectable by the enzyme immunoassay (EIA) method. We postulate that prolactin can bind and stimulate the growth of some cervical cancer cell lines, probably through the prolactin receptor rather than by autocrine regulation.
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PMID:Binding and growth-stimulation of cervical cancer cell lines by prolactin. 136 21

Dopamine inhibits prolactin release from pituitary cells and seems to affect the release of several other hormones as well. We report here that dopamine may have similar effects on human B lymphoma cells leading to inhibition of production or release of endogenous factors required for cell viability and proliferation. Thus, addition of dopamine to serum-free cultures of Burkitt lymphoma cells (Raji, Namalwa, Daudi and Jijoye) resulted in rapid and extensive cell death while a myeloma cell line, SKO, appeared to be refractory to this treatment. The addition of FCS or supernatant from serum-free cultures of Raji or T24 bladder carcinoma cells could, to a variable degree, counteract the effect of dopamine, suggesting that dopamine acts by inhibiting the production of essential autocrine factors. When two of the hormones known to be under dopamine control, i.e. prolactin (PRL) and thyrotropin (TSH), were tested, they were able to prevent dopamine-induced cell death if combined with heparin. We further observed that the reducing agent 2-mercaptoethanol (2-ME), which is known to inhibit the binding of TSH to its receptor, displayed similar effects to those of dopamine and was strongly inhibitory for Burkitt lymphoma but not for myeloma cells. As expected from its blocking activity at the receptor level, the effect of 2-ME could not be reversed by adding exogenous factors. Contrary to its effect on B lymphoma cells, 2-ME is essential for growth of the murine T-cell lymphoma line CTLL. However, we show here that dopamine can fully compensate for 2-ME, suggesting that TSH or another factor under dopamine control is intimately involved in the regulation of T-cell growth. This study lends further support to the notion of an active interplay between the neuroendocrine and immune systems and emphasizes PRL and TSH as important regulators of lymphoid cell function. It also shows that these hormones may contribute to the autonomous growth pattern of B lymphoma cells and suggests a potential role for dopamine in the treatment of B-cell tumours.
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PMID:Dopamine-induced lymphoma cell death by inhibition of hormone release. 141 1

The development of a sensitive and specific two-site, or sandwich, noncompetitive enzyme-linked immunosorbent assay (ELISA) for oncorhynchid growth hormone (GH) using monoclonal antibodies (MCAs) is reported. The MCAs were generated by the fusion of myeloma cells with spleen cells from mice that had been immunized with chum salmon (Oncorhynchus keta) recombinant GH. The MCAs specifically recognized the GH-secreting acidophils in the proximal pars distalis of immature male rainbow trout (Oncorhynchus mykiss) pituitaries. Affinity chromatography using one of the MCAs isolated a single protein with a molecular weight of 22,500 from a rainbow trout pituitary extract. The ELISA recognized recombinant chum salmon GH and the affinity-purified protein but did not recognize chum salmon prolactin, gonadotropin I or II, nor several mammalian hormone preparations. The ELISA recognized GH in rainbow trout, coho salmon (Oncorhynchus kisutch), and chinook salmon (Oncorhynchus tshawytscha) pituitary extracts, but not in goldfish (Carassius auratus) extracts, and recognized GH in rainbow trout, coho salmon, lake sturgeon (Acipenser fulvescens), and bowfin (Amia calva) plasma, but not in goldfish, yellow bullhead (Ictalurus natalis), or lamprey (Petromyzon marinus) plasma. The sensitivity of the ELISA was less than 1.56 ng/ml and circulating levels of GH in the plasma of coho salmon and rainbow trout plasma were measured as 75 and 35 ng equivalents/ml, respectively.
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PMID:The development of a noncompetitive enzyme-linked immunosorbent assay for oncorhynchid growth hormone using monoclonal antibodies. 187 74

A monoclonal antibody-based immunoenzymometric assay (IEMA) for the measurement of human serum growth hormone is described. Two high-affinity and complementary monoclonal antibodies were selected from a panel of 9 obtained upon fusion of SP2/O myeloma cells with spleen cells from a Balb/c mouse immunized against human growth hormone of pituitary origin. One monoclonal antibody was immobilized by attaching it to the walls of microtiter wells and the second was biotinylated. The reaction was quantitated by the addition of streptavidin-peroxidase. The sensitivity of the assay was 0.2 mIU/l and the intra- and interassay coefficients of variation for 4.6 to 46 mIU/l were less than 8.3 and 17.3%, respectively. Cross-reaction with human placental lactogen, human prolactin and rat growth hormone was less than 0.1% (w/w). Comparison of results obtained for 180 routine serum assays by radioimmunoassay and the assay described here had a correlation coefficient of 0.94 with a mean value of 16.3 +/- 1.3 (mean +/- SEM) and 13.3 +/- 1.2 mIU/l, with the IEMA providing values 18% lower than the RIA. The discrepancy emphasizes the necessity of redefining normal ranges before immunometric assays, like the one described, can be used routinely.
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PMID:Monoclonal antibody-based immunoenzymometric assay for serum human growth hormone. 209 41

As a result of cell fusion between myeloma cell line X63.Ag8.653 and lymphocytes of BALB/c mice immunized with chorionic gonadotropin, growth hormone, prolactin, luteinizing hormone, and follicle-stimulating hormone from humans and various farm animals, 148 primary cultures of hybridoma cells were obtained. These hybridomas produced antibodies against the corresponding hormones. The specificities of the resultant monoclonal antibodies, and, in the case of monoclonal antibodies to human chorionic gonadotropin, targeting to certain antigenic regions within the hormone molecule, were characterized in detail. Monoclonal antibodies with specificities different from those previously described were identified.
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PMID:Monoclonal antibodies to human chorionic gonadotropin and certain human and animal hormones of the adenohypophysis. 212 78

Monoclonal antibodies (MCAs) directed against several salmon pituitary hormones were generated by the fusion of myeloma cells with spleen cells from mice that had been immunized with either chum salmon (Oncorhynchus keta) growth hormone (GH) or prolactin (PRL), or one of two purified protein preparations from coho salmon (O. kisutch) pituitaries. Hybridoma were cloned by limiting dilution and screened for MCA production using immunohistochemical procedures. MCAs were generated that bound specifically to GH, PRL, or gonadotropic cells. MCAs were generated that bound to either fine granular material or large globular inclusions in the cytoplasm of the "classical" strongly PAS-positive globular gonadotropic cell type found in mature fish. This suggests that these MCAs are directed against gonadotropin II (GTH II). A MCA was also generated that bound both granular and globular material in the globular gonadotrops and granular material in the weakly PAS-positive vesicular gonadotrops in pituitaries from mature fish and to a cell type in immature rainbow trout pituitaries which is tentatively identified as the gonadotropin I (GTH I) cell type. This MCA did not bind to thyrotrops in immature rainbow trout pituitaries.
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PMID:The development of monoclonal antibodies against salmon (Oncorhynchus kisutch and O. keta) pituitary hormones and their immunohistochemical identification. 227 59

Four hybridomas stably secreting monoclonal antibodies (McAbs) against human growth hormone (hGH) have been obtained by fusion of immunized mice spleen cells with myeloma SP2/0 cells. After inoculation of hybridoma cells to BALB/c mice i.p., the ascitic fluids were collected and characterized, the titre of the 4 McAbs being in the range of 0.6-10.0 X 10(5). As determined by Ouchterlony analysis, all the 4 McAbs were IgG1. They varied in affinities, with equilibrium constants from 0.53 X 10(9) to 9.0 X 10(9) L/mol. McAb-1 showed 52.5% cross-reactivity with human placental lactogen (hPL). McAb-2, McAb-3 and McAb-4 displayed no crossreactivity with hPL and human prolactin (hPRL). Antigenic determinants recognized by the 4 McAbs were mapped through their reactions with hGH fragment consisting of residues 1-43, cross-reaction with hPL, hPRL and antibody-antibody competition test. The results showed that the antigenic determinants of the McAbs are not located in the site of hGH comprising residues 1-43 but on the three non-overlapping antigenic sites of hGH. As shown in receptor assay, all the 4 McAbs exhibited specific inhibition on the binding of pregnant rabbit liver GH receptor to 125I-hGH. It seems likely that receptor-binding site is larger than the antigenic determinant or there are more than one site on hGH surface capable of binding to the hormone receptor. The McAbs could only bind with the peak 2 (MW22000) but not the peak 1 (MW 45000) of old 125I-hGH after gel filtration.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Preparation and characteristic analysis of monoclonal antibodies against human growth hormone]. 247 70

Three monoclonal antibodies (M110, A82, and A917) were obtained by fusing myeloma cells and spleen cells from mice immunized with partially purified rabbit mammary gland prolactin (PRL) receptors. All 3 antibodies were capable of complete inhibition of 125I-ovine prolactin (oPRL) binding to rabbit mammary PRL receptors in either particulate or soluble form. M110 showed slightly greater potency than oPRL in competing for 125I-oPRL binding. These antibodies also inhibited PRL binding to microsomal fractions from rabbit liver, kidney, adrenal, ovary, and pig mammary gland, although A82 showed poor inhibition in pig mammary gland. There was no cross-reaction of any of the 3 monoclonal antibodies (mAbs) for the other species tested: human (T-47D breast cancer cells) and rat (liver, ovary). In order to confirm that these antibodies are specific to the binding domain, antibodies were purified, iodinated, and binding characteristics were investigated. 125I-M110 and 125I-A82 binding was completely inhibited by lactogenic hormones, whereas nonlactogenic hormones did not cross-react. Competition of 125I-M110 by oPRL (ID50 = 0.44 nM) was comparable to that of 125I-oPRL by unlabeled oPRL (ID50 = 0.35 nM), while 125I-A917 binding was only partially competed (30-60%) by lactogenic hormones. Tissue and species specificity of labeled antibody binding paralleled results of binding inhibition experiments using 125I-oPRL. In addition, A82 and A917 completely inhibited 125I-M110 binding. In contrast, 125I-A82 binding was stimulated by A917 and 125I-A917 binding was stimulated by A82. These findings indicate that monoclonal antibodies can be readily prepared from partially purified PRL receptors from rabbit mammary gland; two antibodies (M110 and A82) are hormone binding site specific while the other (A917) binds a domain partially but not entirely distinct from the hormone binding site, and that all three antibodies have strong species specificity.
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PMID:Monoclonal antibodies against rabbit mammary prolactin receptors. Specific antibodies to the hormone binding domain. 299 33

In an attempt to raise monoclonal antibodies to chicken pituitary glycoprotein hormones, mice were immunized with the concanavalin A-adsorbed components of a hypophyseal extract. Fusions of these spleen cells with myeloma cells repeatedly yielded hybridoma lines secreting antibodies that recognized specifically the pituitary caudal acidophils, known as the somatotropes. This paper reveals the existence of a glycosylated counterpart of the well-established holoprotein form of chicken growth hormone, similar to what has been established for human growth hormone and prolactin.
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PMID:Glycosylated chicken growth hormone. 343 15

The hormonal mechanisms involved in the development of gynaecomastia accompanying the treatment of multiple myeloma in adult men have been investigated by studying levels of circulating testosterone (T), oestrone (EI), oestradiol (E2), sex-hormone binding globulin (SHBG), prolactin (PRL) and the gonadotrophins LH and FSH, before, during and after development of gynaecomastia in 4 men. These have been compared with 5 closely matched men who did not develop gynaecomastia during similar treatment for myeloma. Levels of circulating T fell, and levels of E1 and E2 rose during treatment periods in all subjects, and the changes were statistically significant in subjects developing gynaecomastia, which resolved as levels of sex steroid returned towards normal following cessation of treatment. We conclude that treatment of adult men for myeloma results in testicular dysfunction with a reduction in circulating T and a rise in circulating oestrogens. These changes are most marked in subjects developing gynaecomastia in whom the normal breast tissue is stimulated by a subtle, transient oestrogen:androgen imbalance in favour of oestrogens.
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PMID:Gynaecomastia complicating the treatment of myeloma. 640 38


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