Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The dynamics of the blood in guinea pigs sensitized with heterogenous antirabic immunoglobulin was studied. The damage of neutrophils in the blood was found to be an index which allowed to detect changed sensitivity to heterogenous protein already at an early period (on day 6) after immunization, whereas the indirect mast cell degranulation test detected it only at a later period (on day 21). The above methods revealed that beta 1 and beta 2 globulin fractions possessed high sensitizing activity.
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PMID:[In vitro study of the sensitizing activity of an antirabies immunoglobulin and its fractions]. 8 68

The de novo megakaryocytic leukemia fulfilling the FAB criteria is still an uncommonly recognized variant of acute leukemia. Many studies have shown that the megakaryocytic leukemic events may occur at a pluripotent stem cell level and clinical observations reveal that the megakaryocytic leukemias are diverse entities. The immunophenotyping using monoclonal antibodies against platelet specific surface antigens and the ultrastructural detection of platelet peroxidase reaction do not provide sufficiently useful information to determine whether a megakaryocytic leukemia is chronic, acute, therapy-responsive or therapy-unresponsive. More sophisticated techniques are required to further characterize megakaryocytic leukemic cells. In this review, we emphasize that megakaryocytic leukemic cells can be categorized into two groups; one with the PF4 mRNA, and the other without it, and that the expression of PF4 mRNA in the blasts could be a useful marker for the identification of mature megakaryoblasts. It seems that the patients with blasts expressing PF4 mRNA will have a longer survival and a better response to chemotherapy than those without PF4. We further discuss the fact that the detection of mRNAs of the IL-6 receptor, PDGF A- and B-chains, and TGF beta 1 in megakaryocytic leukemic cells will be useful to clarify the mechanisms involved in the proliferation of megakaryocytic leukemic cells and fibroblasts in the bone marrow. Furthermore, we reviewed data showing that megakaryocytic erythroid, and mast cell lineages share the nuclear transcription factor known as GF-1 (NF-E1 or Erf-1). We suggest that characterization of megakaryocytic leukemia should be performed using monoclonal antibodies against erythroid, megakaryocytic and mast cell lineages.
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PMID:Megakaryocytic leukemia and platelet factor 4. 133 50

Human mast cells have been purified from uterine tissues, and their surface marker profile and function have been evaluated as part of ongoing studies of mast cell heterogeneity. Using a panel of antibodies, purified uterine mast cells (UMC; 81% +/- 7% purity, n = 10) were analyzed by immunofluorescence and flow cytometry for surface expression of various antigens. Consistent with previous analyses of mast cells from other tissues, UMC expressed HLA class I, IgE, c-kit receptor, CD9, CD33, CD43, CD45, and CD54, while CD11a, CD11b, CD14, CD16, CD23, and CD64 were not detected. Unlike other mast cells, UMC expressed CD11c/CD18 (p150,95) and CD32 (Fc gamma RII). Additional antigens not previously studied on mast cells included the selectin LECAM-1 (Leu-8) and several beta 1 and beta 3 integrins; expression of very late activation antigen-4 (VLA-4) (CD49d/CD29), VLA-5 (CD49e/CD29), and the vitronectin receptor (CD51/CD61) was seen. Functional studies showed that treatment of human umbilical vein endothelial cells with interleukin-1 (5 ng/mL for 4 hours) resulted in a twofold to threefold increase in adhesiveness for UMC. Purification procedures did not alter histamine release responses to anti-IgE or the calcium ionophore A23187, and treatment of UMC with an anti-CD32 monoclonal antibody (IV.3) did not induce histamine release or alter anti-IgE-induced release. These data suggest that UMC may possess unique phenotypic characteristics, and support the concept of mast cell heterogeneity.
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PMID:Immunophenotyping and functional analysis of purified human uterine mast cells. 137 Jun 42

The screening of a rat mast cell cDNA library with a probe selected to recognize those genes preferentially or exclusively expressed by mast cells identified a rat gene sequence, RF-17, that shared homology with the beta-integrins. This integrin was expressed in rat tissues enriched for mast cells and T cells. The rat RF-17 sequence was used to isolate the murine homologue from a spleen cDNA library. The murine gene encodes a protein of 806 amino acids that is the probable homologue to the human beta 7 chain. Transcripts specific for the murine gene are found in the thymus, spleen, and lung. To attempt to identify the gene product for this new integrin chain, we examined the murine T cell line TK-1, which expresses a novel integrin heterodimer, lymphocyte Peyer's patch high endothelial venule adhesion molecule (LPAM-1), of a known alpha 4 chain and an unknown beta P chain, for expression of murine beta 7 (RF-17). This cell line expresses high levels of RF-17 transcripts, suggesting that beta P is encoded by the beta 7 gene. Bone marrow cells induced to differentiate into mast cells via IL-3 express the beta 7 gene as well as the genes encoding the murine integrin alpha 4 and beta 1 proteins. Surface staining analysis indicates that these cells express an alpha 4-containing integrin complex throughout the differentiation process. These data suggest that the Peyer's patch homing LPAM-1 receptor expressed by a subset of T cells consists of the beta 7 gene product and the alpha 4 chain, and that this integrin chain complex is also found on the surface of maturing mast cells. The presence of beta 1 transcripts also suggests that these maturing mast cells possess the LPAM-2 integrin complex (alpha 4/beta 1) as well. The experimental strategy described in this manuscript has, thus, identified a novel murine beta-integrin chain that is expressed by rodent T cells and mast cells.
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PMID:Expression of murine beta 7, alpha 4, and beta 1 integrin genes by rodent mast cells. 138 90

Previously we have reported that rodent mast cells synthesize the mRNA encoding the alpha and beta integrin chains (alpha 4, beta 1 and beta 7) of the lymphocyte Peyer's patch adhesion molecule (LPAM)-1 and LPAM-2 lymphocyte homing receptors, and that they possess an alpha 4-containing integrin complex on their cell surface. In this report, we have examined the expression of these integrin chain genes by mature connective tissue mast cells (CTMC) and by bone marrow-derived mast cells (BMMC) differentiated from bone marrow precursor cells in the presence of interleukin (IL)-3 and/or the c-kit ligand (also known as mast cell growth factor and stem cell growth factor). High levels of both the beta 7 and beta 1 transcripts were present in mature CTMC while those encoding the alpha 4 chain were absent. Similarly, when BMMC were grown in IL-3 for 28 days and analyzed for integrin chain transcripts, those specific for the alpha 4 chain were also diminished compared to beta 7 and beta 1 transcripts. To compare the expression of these integrin genes during mucosal mast cell and CTMC development, BMMC were derived in the presence of IL-3 alone, c-kit alone, or IL-3/c-kit together. These experiments indicated that c-kit inhibited the transcription of the beta 7 and Fc epsilon RI genes while enhancing alpha 4 transcript levels. The enhancement of alpha 4 levels, however, was abrogated with the addition of IL-3. Similarly, the c-kit-induced depression of beta 7 and Fc epsilon RI transcript levels was overcome by the addition of IL-3. These data suggest that the integrin complexes synthesized by the mast cells may differ depending upon their path of differentiation and that another alpha chain integrin may be synthesized to complex with the beta 7 and/or beta 1 chains.
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PMID:Modulation of integrin expression during mast cell differentiation. 138 93

Transforming growth factor-beta (TGF beta) promotes deposition of extracellular matrix and is associated with fibrotic conditions both in experimental animals and in humans. Although a role for mast cells has been suspected in the pathogenesis of fibrosis, no potent mediator capable of stimulating fibroblast growth or extracellular matrix deposition has been identified in mast cell supernatants. We report here the constitutive production of TGF beta 1 by four dog mastocytoma cell lines. TGF beta 1 was identified by characteristic biologic activity, blockade of biologic effect by specific neutralizing antibody, and by recognition of a band with the appropriate migration by western blot. TGF beta 1 mRNA, but not TGF beta 2 or TGF beta 3 mRNA, was also produced constitutively by all four cell lines. Quantitation by bioassay revealed baseline TGF beta secretion of approximately 1 ng/10(6) cells over 48 h. Stimulation of mastocytoma cells with phorbol ester increased the rate of release of TGF beta 1, most markedly in the first 30 min after stimulation, without increasing TGF beta 1 mRNA. Dog mastocytoma cells produced TGF beta 1 primarily in a latent form, inactive until treated with acid. Both pure TGF beta 1 and TGF beta-containing mastocytoma cell-conditioned media inhibited mitogenesis and proliferation in dog mastocytoma cell lines, suggesting that mast cell tumor lines would not grow preferentially based on their ability to produce TGF beta. These studies may make possible further investigation of the mechanism by which mast cells contribute to the induction of fibrosis.
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PMID:Dog mastocytoma cells produce transforming growth factor beta 1. 163 19

Integrins are multifunctional recognition molecules and are expressed on various hematopoietic cells. In the present study expression of integrins on the cell surface of human mast cells and human basophils was investigated by using monoclonal antibodies (mAbs) and indirect immunofluorescence. Human mast cells were obtained from lung (n = 5), uterus (n = 5) and skin (n = 4). Human blood basophils were obtained from normal donors (n = 2). In addition, HMC-1 cells (human mast cell line) and KU-812 cells (a basophil cell line) were analyzed. Primary mast cells were found to react with mAbs directed against the common beta chain of beta 1 integrins (CD 29), the alpha chain of VLA-4 (CD 49 d) and VLA-5 (CD 49 e), the beta chain of beta 3 integrins (CD 61), and the alpha chain of the vitronectin receptor (VNR) (CD 51). Mast cells were not recognized by mAbs to beta 2 integrins (CD 18, CD 11 a, CD 11 b, CD 11 c), the alpha chain of VLA-2 (CD 49 b), and VLA-6 (CD 49 f). No differences in expression of integrins on human mast cells obtained from different organs were found. HMC-1 cells and primary mast cells expressed an almost identical pattern of integrins. Human basophils and KU-812 cells were found to react with mAbs directed against beta 1-integrins (CD 29, CD 49 b, CD 49 d, CD 49 e) and beta 2-integrins (CD 18, CD 11 a, CD 11 b, CD 11 c). Together, mast cells and blood basophils express a unique pattern of integrins. These cell surface structures may be involved in the distribution of basophils and tissue mast cells and their accumulation and function in inflammed tissues.
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PMID:Differential expression of cell surface integrins on human mast cells and human basophils. 164 54

Fc gamma R expressed by mouse mast cells were characterized as functional binding sites, as membrane proteins, and as products of the two genes known to encode murine Fc gamma RII. Peritoneal mast cells, bone marrow-derived mast cells (BMMC), and the mastocytoma cells P815 were found to bear trypsin-resistant, 2.4G2+, low-affinity receptors binding mouse monoclonal IgG1, IgG2a, and IgG2b, i.e., Fc gamma RII. BMMC and P815 Fc gamma RII appeared as heterogeneous membrane proteins that, when deglycosylated, had m.w. corresponding to those of the three known products of the alpha and beta Fc gamma R genes, and differed by their respective contents in BMMC and P815 cells. Heterogeneous Fc gamma R transcripts were also found in BMMC and in P815 RNA. P815 cells contained alpha, beta 1, and beta 2 Fc gamma R transcripts, whereas BMMC contained alpha and beta 1 Fc gamma R transcripts. These data disclose an unexpected molecular heterogeneity of murine mast cell Fc gamma R. Although they appear as a single population of receptors when viewed by external ligands, mast cell Fc gamma R comprise three Fc gamma RII subtypes, encoded by the three known transcripts of the alpha and beta Fc gamma R genes, and differing by their intracytoplasmic portion. The different distributions of Fc gamma RII transcripts and corresponding Fc gamma RII subtypes in different types of mast cells may be determinant for triggering the various biologic activities of these cells.
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PMID:Molecular heterogeneity of murine mast cell Fc gamma receptors. 213 78

The original form of beta beta enolase (EC 4.2.1.11) in tissue is modified to two more electrophoretically distinct forms when incubated with human serum. The three postsynthetic forms are designated beta beta 3, beta beta 2, and beta beta 1, in order of increasing anodal mobility and increasing modification. Serum and carboxypeptidases A and B all produce identical modifications of beta beta enolase but exhibit very different pH-activity profiles. A purified human serum protein previously named "modifying protein," which is responsible for the modification of creatine kinase-M and alpha-enolase subunits, modifies beta beta enolase and also has a pH-activity profile identical to that for serum. Thus we conclude that the modifying protein is not identical to either carboxypeptidase A or B; it may, however, be an as-yet-undescribed carboxypeptidase. With increased modification, both alpha alpha and beta beta enolase decrease in apparent activation energy; gamma gamma enolase shows no evidence of modification, and its apparent activation energy remains stable. Measurement of activation energy is an easy tool for screening for postsynthetic modifications in an enzyme.
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PMID:Postsynthetic modification of human enolase isoenzymes. 359 9

beta-Adrenoceptor stimulating agents possess anti-allergic effects in vitro and in vivo. To study the mechanism of action further we compared in 10 atopic subjects the effects on allergen-induced cutaneous reactions of intradermally (i.d.) injected prenalterol (1-10 microgram) terbutaline (2.5-250 ng) and KWD 2131 (100 ng-2.5 microgram), i.e. compounds with preferential actions on beta 1-, beta 2-adrenoceptors and on beta-adrenoceptors not fitting this classification. All injections were given according to a double-blind design. Terbutaline and KWD 2131 produced a dose-dependent inhibition of the skin reactions induced by injecting horse dander allergen 5 min later. Terbutaline was about 20 times as potent as KWD 2131 whereas prenalterol was inactive. Propranolol fully blocked the anti-allergic effect produced by terbutaline. The results suggest that the cutaneous anti-allergic effect of beta-adrenoceptor-stimulating drugs is mediated via activation of beta 2-adrenoceptors, possibly on the mast cell, resulting in inhibition of mediator release.
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PMID:Cutaneous responses to allergen after local pretreatment with beta-adrenoceptor stimulating and blocking agents. 610 25


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