Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
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1. Normal subjects showed a highly reproducible, rapid increase in plasma adenosine 3':5'-cyclic monophosphate (cyclic AMP) after an intravenous injection of 200 MRC units of highly purified bovine parathyroid hormone. 2. No significant increase in plasma cyclic AMP was observed after administration of bovine parathyroid hormone to patients with severe chronic renal failure. 3. Even when renal function was not impaired, some patients with primary hyperparathyroidism, who had high concentrations of endogenous parathyroid hormone, showed resistance to bovine parathyroid hormone and when this was injected intravenously it caused only a small increase in plasma cyclic AMP. This resistance was reversible since there was marked improvement in the response after parathyroidectomy, when endogenous parathyroid hormone concentration had fallen. 4. It was possible to reproduce this resistance to the hormone by intravenous infusion of bovine parathyroid hormone into normal subjects. When the hormone (1000 MRC units) was infused over 2 h, after an initial increase there was a progressive decline in plasma cyclic AMP concentration and a fall in urinary cyclic AMP excretion. The response to a standard test stimulus (200 MRC units of bovine parathyroid hormone given as a rapid intravenous injection) was examined at intervals after 1000 units of bovine parathyroid hormone had been infused. Initially, the response was severely impaired; at 4 h, partial recovery had occurred and, 24 h after the infusion, recovery of the response was complete. The resistance was therefore reversible. Infusion of the amino-terminal peptide, fragment 1-34, gave the same effect as infusion of intact hormone. Region-specific assays for the hormone were used to show that the concentration of immuno-assayable hormone remained high during the infusions. 5. The mechanism of this reversible resistance to parathyroid hormone remains to be elucidated; it seems unlikely that circulating hormone fragments could account for the prolonged impairment in the responsiveness to the intact hormone. It is possible that alteration in the formation, intracellular degradation or, perhaps, release of cyclic AMP from the cells, is the cause. Changes in the characteristics of the hormone receptor sites might also explain the phenomenon.
Clin Sci Mol Med 1976 Jul
PMID:Reversible resistance to the renal action of parathyroid hormone in man. 18 Nov 94

The relationship between the immunological and biological activities of thyroid-stimulating hormone (TSH) isoforms present in the three human pituitary preparations 68/38 (1st IRP), 80/558 (2nd IRP) and 63/14 (MRC Research Standard A) was investigated. The isoforms were separated by chromatofocusing. Six peaks of immunoactivity were detected in 80/558, with pI values (means +/- S.E.M.) of 6.6 +/- 0.1, 6.2 +/- 0.1, 5.9 +/- 0.1, 5.5 +/- 0.1, 5.2 +/- 0.1 and 4.9 +/- 0.1. Four peaks, with pI values of 6.8 +/- 0.1, 5.9 +/- 0.1, 5.5 +/- 0.1 and 5.2 +/- 0.1, were observed for 68/38. Standard 63/14 had five peaks, with pI values of 6.9 +/- 0.1, 6.4 +/- 0.1, 5.9 +/- 0.1, 5.4 +/- 0.1 and 4.9 +/- 0.1. For each standard, six fractions around the peak areas and at the top and bottom of the gradient were pooled and microconcentrated to < 1.0 ml. Microconcentrated TSH samples were assayed in three TSH bioassays based upon FRTL-5 thyroid cells, utilizing cyclic AMP accumulation, iodide and thymidine uptake as end-points and standard 80/558 as reference preparation. The more acidic forms of TSH showed a higher biological:immunological (B:I) ratio for cyclic AMP accumulation with, for example, 63/14 having a maximum of 3.7 (pI 4.9) and a minimum of < 0.7 (pI 6.9). In contrast, the maximum and minimum B:I ratios for iodide uptake for 63/14 were 3.8 (pI 6.9) and < 0.8 (pI 4.6), and for thymidine uptake, maximum and minimum ratios were 7.2 (pI 6.9) and 1.1 (pI 4.6) respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
J Mol Endocrinol 1992 Dec
PMID:Different isoforms of human pituitary thyroid-stimulating hormone have different relative biological activities. 147 12

Activated macrophages participate in inflammation by eliminating foreign cells, promoting wound healing, and modulating the immune response. A murine monoclonal antibody, designated anti-rat macrophage activator (RMA), was raised against alveolar macrophages (AM) activated with interferon-gamma (IFN-gamma) and phorbol myristate acetate (PMA). The RMA antigen is expressed by resident macrophages but not by other cells. Binding to AM by anti-RMA is not competitively inhibited by the murine monoclonal antibodies MRC OX-41, OX-42, and OX-43. Surface membrane expression of RMA antigens is upregulated by lipopolysaccharide, PMA, and tumor necrosis factor-alpha but not by IFN-gamma. Stimulation of AM with anti-RMA yields distinct ultrastructural alterations, as well as de novo protein and DNA synthesis. Immunoprecipitation of [35S]methionine metabolically labeled AM yields a 120 kD protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) that is not altered by chemical reduction. We conclude that the RMA antigen is macrophage specific and that binding of anti-RMA to AM promotes functional activities in a subset of these cells.
Am J Respir Cell Mol Biol 1990 Feb
PMID:Anti-RMA: a murine monoclonal antibody that activates rat macrophages. I. Distribution and characterization of the RMA antigen. 168 87

Moloney murine leukemia virus (MoMuLV)-induced rat T-cell lymphomas express discrete 1.8-, 2.2-, and 4-kb mRNA transcripts hybridizing under conditions of reduced stringency to a probe derived from a region upstream of the first exon of the Tpl-1/Ets-1 gene. Screening a cDNA library from one rat T-cell lymphoma with this genomic probe yielded 15 cDNA clones which were derived from 10 different genes. One of these genes, defined by the cDNA clone pRcT7a, was expressed as a 1.8-kb mRNA transcript in spleen and thymus but not in other normal rat tissues. Expression of the gene defined by the pRcT7a cDNA clone in a series of MoMuLV-induced rat T-cell lymphomas showed a perfect correlation with the expression of the rat leukocyte antigen MRC OX-44. Because of this observation, the pRcT7a clone was sequenced and it was shown to identify a gene coding for a 219-amino-acid protein. The homology between pRcT7a and the Tpl-1 probe used for its detection mapped within the 3' untranslated region of the pRcT7a cDNA clone. The pRcT7a protein, which exhibits four putative transmembrane regions and three putative glycosylation sites, contains a region which is nearly identical in sequence to a peptide derived from the rat leukocyte antigen MRC OX-44. This finding suggested that the pRcT7a cDNA clone defines the gene coding for OX-44. To confirm this finding, a pRcT7a construct in the retrovirus vector pZipNeo was introduced into the OX-44- T-cell lymphoma line 2788. Immunostaining with the MRC OX-44 monoclonal antibody followed by flow cytometry revealed that following gene transfer, the 2788 cells became OX-44+. Sequence comparisons revealed that pRcT7a/MRC OX-44 is a member of a family of genes which includes the melanoma-specific antigen ME491; the human leukocyte antigen CD37; the protein TAPA-1, which is expressed on the surface of human T cells and appears to be involved in growth regulation; the human gastrointestinal tumor antigen CO-029; and the Schistosoma mansoni-associated antigen Sm23.
Mol Cell Biol 1991 May
PMID:The rat leukocyte antigen MRC OX-44 is a member of a new family of cell surface proteins which appear to be involved in growth regulation. 201 81

Using the non-crossreactive mAb MRC-OX3 and MRC-OX6, two serologically distinct RT1.B-specific (I-A equivalent) alpha, beta heterodimers have previously been described by us as residing at the cell surface of LEW rat spleen cells. The two-chain elements were suggested to represent stable conformation isomers, diverged by dissociation of the mature gamma-chain from a mAb MRC-OX6 reactive biosynthetic intermediate, composed of terminally glycosylated alpha-, beta- and gamma-chains. In this study we addressed the question of whether or not the presence of terminally glycosylated invariant gamma-chain was obligatory for the formation of the two MRC-OX3 and MRC-OX6 reactive two-chain complexes. The synthesis of RT1.B-specific alpha, beta heterodimers was therefore initiated, in the absence of accompanying invariant gamma-chains, by microinjecting hybrid-selected RT1.B alpha- and beta-specific mRNA into oocytes of Xenopus laevis for translation. Class II molecules produced were analyzed by affinity chromatography of radioactive-labeled oocyte detergent lysates using the appropriate monoclonal immunoadsorbents for identification. Although rat gamma-chain mRNA was excluded in this assay system, distinct MRC-OX3 and MRC-OX6 reactive two-chain complexes were detected by two-dimensional gel electrophoresis. These findings clearly indicate that the formation of the two RT1.B-specific alpha, beta heterodimers is independent of the presence of the rat invariant gamma-chain.
Mol Immunol 1989 Feb
PMID:Translation in Xenopus laevis oocytes of hybrid selected LEW rat RT1.B alpha- and beta-chain transcripts results in serologically discrete class II polypeptide chain complexes. 246 90

Normal human fibroblasts (MRC-5, KMS-6) were compared to transformed derivatives induced by SV40 (MRC-5V1) or gamma rays (KMST-6) for the expression of nuclear proteins that interact with the genome of minute virus of mice (MVMp), using the southwestern blot technique. A protein of 100-104 kDa apparent molecular weight was found to form a specific complex with MVMp DNA and to have an especially high affinity for the 3' terminal portion of the viral genome. This protein (p102) was differentially expressed by normal and transformed cells, i.e., its availability or DNA binding activity (or both) was much reduced in the transformants. A high level of p102 cosegregated with resistance to MVMp in cell hybrids between normal human and transformed mouse fibroblasts. Taken altogether these data suggest that the p102 protein may be a candidate for a transformation-sensitive cellular marker and for a negative regulator of parvovirus replication.
Mol Carcinog 1989
PMID:Identification of a transformation-sensitive nuclear protein from normal human fibroblasts that specifically interacts with minute virus of mice DNA and correlates with cell resistance to the parvovirus. 255 56

Mouse monoclonal antibodies (MAbs) have been prepared against rat T cell blasts. One MAb called MRC OX-40 recognized an antigen that differed from any previously described in that its expression was detected only on T blasts that also expressed the CD4 antigen. The OX-40 MAb did not detect an activation determinant of CD2 or CD4 molecules but recognized a distinct chain of mol. wt 50,000. The OX-40 MAb augmented T cell proliferation at late stages on in vitro responses. Other MAbs without obvious counterparts in other species were MRC OX-48 and MRC OX-49,50 which recognized cell surface molecules of mol. wts of about 95,000 and 90,000, respectively. The OX-48 antigen was not expressed on resting lymphocytes but was found on a subset of T and B blasts and also on other leucocytes. The OX-49,50 antigen was found on most haemopoietic cells but was expressed at greatly increased levels after lymphocyte activation and this was also the case for MRC OX-47 antigen which is of unknown Mr. The MRC OX-39 MAb was found to bind the rat IL-2 receptor; expression of this antigen was detected on thymic dendritic cells as well as on T blasts. The phenotype of rat T blasts compared to resting cells was also examined and changes in expression of L-CA, Thy-1, OX-2 and CD8 antigens were seen in addition to the changes found with the above MAbs.
Mol Immunol 1987 Dec
PMID:Antigens of activated rat T lymphocytes including a molecule of 50,000 Mr detected only on CD4 positive T blasts. 282 30

Monoclonal antibodies MRC OX-45 and OX-46 detect identical or juxtaposed antigenic determinants on a novel rat membrane molecule that plays a possible role in macrophage suppression of antigen-induced T-cell responses. These antibodies react with most mature hematopoietic cells and their bone-marrow precursors, vascular endothelium and some connective tissue. The OX-45 antigens were purified from brain (mainly endothelium) and spleen by immunoaffinity chromatography, and were found to be glycoproteins with apparent Mr 43,000 and 45,000, respectively, as determined by SDS-PAGE analysis. The amino acid compositions of the two preparations were very similar but with no distinguishing features. The broad pattern of distribution was not the result of fortuitous cross-reaction of the MAbs as a single N-terminal sequence was obtained from mixed spleen populations of cells. Carbohydrate compositions of the brain and spleen molecules differed both in absolute amount (22 and 41% by weight, respectively) and in the ratios of various saccharides reflecting overall differences in the patterns of glycosylation between the two tissues. MRC OX-45 IgG showed an heterogeneity in the Mr of its H chain due to the attachment, in some molecules, of carbohydrate structures to the Fd fragment.
Mol Immunol 1986 Sep
PMID:MRC OX-45 antigen: a leucocyte/endothelium rat membrane glycoprotein of 45,000 molecular weight. 353 34

A single dose of synthetic salmon calcitonin administered to rats (20 MRC U/kg body weight) stimulated the activity of ornithine decarboxylase in the brain, liver, kidney, testis and ovaries by 3-, 15-, 5-, 2- and 2-fold respectively after 4 h of the treatment. The increase in the enzyme activity in the brain, testis and ovaries was accompanied by a comparable increase in the enzyme protein content. Hepatic and renal ornithine decarboxylase concentration increased only by 2-fold. These results suggest that calcitonin influences polyamine biosynthesis through a tissue-specific regulation of the activity and/or the number of ornithine decarboxylase molecules.
Mol Cell Endocrinol 1987 Aug
PMID:Calcitonin induces ornithine decarboxylase in various rat tissues. 365 6

A cDNA cloning approach was used to study the regulation of gene expression in human T lymphocytes upon mitogen stimulation. Poly(A)+ mRNA was prepared from phytohemagglutinin A (PHA) and 12-O-tetradecanoyl phorbol 13-acetate (TPA) activated human T cells and a cDNA clone library was constructed. After screening by colony hybridization with [32P]cDNA probes made from resting and activated T cell mRNA, several clones whose mRNA increased at least 10 to 20-fold upon stimulation were isolated. Northern blot analysis of the mRNA from various cell types using these cDNA clones as probes revealed that one of the cDNA clones, pNC5A, encoded a gene expressed only in PHA and TPA-stimulated human T lymphocytes and in a human neoplastic T cell line HUT102-SH9. Less than 20 copies of this mRNA species per cell was detected in resting human T lymphocytes, B lymphocytes and monocytes and in two other T cell lymphoma lines (CEM and MOLT4), two B lymphoblastoid cell lines (WIL2-729-HF2 and HFB-1), a myeloid cell line (HL60) and a human embryonic lung fibroblast cell line (MRC-5). Hybrid selection translation and sodium dodecyl sulfate/polyacrylamide gel electrophoretic analysis of the translated product indicated that a polypeptide of 30,000 to 32,000 Mr is encoded by this particular cDNA clone. Thus, this cDNA clone may define a novel gene that is expressed only in activated human T cells.
Mol Biol Med 1984 Apr
PMID:A cDNA clone encoding a product of activated human T lymphocytes. 633 9


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