Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The p85 glycoprotein expressed on a variety of human cell types including astrocytes and lymphocytes has not been associated with the CD44 cluster. The recent demonstration that Hermes, a glycoprotein implicated in the adhesion of lymphocytes to endothelium, belongs to the CD44 cluster raises interesting questions concerning the role of this molecule on astrocytes and on non-lymphoid cells. To obtain confirmation of the identity of p85 glycoprotein and CD44, p85 glycoprotein was purified from B-chronic lymphocytic leukemia cells by affinity to monolonal 50B4-IgG and electrophoretic elution, digested with trypsin or CNBr and fractionated by reversed-phase HPLC. The sequences of three peptides were obtained which could be aligned with the amino acid sequence deduced from the CD44 cDNA at residues 49-54, 59-66 and 309-323. These constitute the first reported peptide sequences for antigens of the CD44 cluster and confirm that p85 glycoprotein is indeed the product of the CD44 gene. Since two different cDNA clones encoding molecules with cytoplasmic tails of 72 and 5 amino acids have been isolated, the isolation of peptide 309-323 confirms the existence of a processed protein with the longer cytoplasmic domain. Using a cDNA probe, we have characterized the expression of CD44 in several normal and malignant cell types. The level of CD44 mRNA was correlated with the surface expression of CD44 antigens (50B4) in several leukemic cell lines, in astrocytoma lines and in normal granulocytes. Negative cells included the Y79 retinoblastoma line, the NALM-6 leukemic line and endothelial cells. Identical mRNA species of 5.0, 2.3 and 1.7 kb were present in all CD44-positive samples, including normal granulocytes, astrocytoma, melanoma and leukemia cell lines and leukemic cells from patients. The highest level of expression of CD44 was observed on astrocytoma lines and on acute lymphoblastic leukemia cells of immature phenotype. The presence of high levels of CD44 on malignant cells could increase the ability of these cells to adhere to matrix proteins and/or to interact with endothelium, thus potentially altering their capacity for invasiveness and metastasis.
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PMID:Confirmation by peptide sequence and co-expression on various cell types of the identity of CD44 and P85 glycoprotein. 223 56

Whereas by indirect immunofluorescence approximately 80% of freshly isolated human peripheral blood lymphocytes bound T3 (Leu 4)-specific and T11-specific monoclonal antibodies, by a more sensitive technique--the indirect antiglobulin rosetting reaction--more than 90% of these lymphocytes were T3+ (Leu 4+) and T11+; this finding suggested that some non-T cells may also express T3 and T11 determinants. In double labelling experiments most normal surface membrane immunoglobulin (smIg)-bearing lymphocytes, ie, B cells, were shown to express T3 and T11 determinants at low density. The determinants were re-expressed after stripping with trypsin. Moreover, greater than 90% of neoplastic lymphoid cells expressing monotypic smIg from six donors were T3+ and/or T11+. Together these results provide new data on the cell distribution of 'T cell markers'. These findings also indicate that the rosette test is too sensitive to distinguish between biologically distinct lymphocyte population, ie between T and B cells.
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PMID:Expression of T3 and T11 determinants on human peripheral lymphocytes as analysed by the indirect antiglobulin rosetting reaction (IARR) and indirect immunofluorescence. 241 98

Among the differentiation antigens expressed by lymphoid cells, CD1 monoclonal antibodies (MCA) distinguish a group of antigens expressed by cortical thymocytes. Some of them (OKT6 and BL6) have been shown to react with normal human skin Langerhans cells (LC). Using indirect immunofluorescence on skin sections and LC-enriched epidermal cell suspensions obtained by skin trypsinisation, we have studied the reactivity of eight new CD1 MCA. Our immunocytochemical observations indicate that four groups of CD1 MCA can be distinguished on the basis of their reactivity on LC. NA.1.84, SK9/Leu6, 10 D.12.2 and I19 identify LC in skin and in suspensions, but 4A.76 and NUT2 were negative in both. M.241 became negative after trypsinisation of epidermal cells and D47 reacted with an antigen expressed on LC only after enzymatic treatment. These results demonstrate the heterogeneity of the antigens recognized by CD1 MCA. Some of them do not react with normal human LC. Some antigens appear to be masked in the epidermis and are expressed only after trypsin treatment. Our data confirm the heterogeneity of CD1 molecules recently documented on the basis of biochemical analysis.
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PMID:Subclustering of CD1 monoclonal antibodies based on the reactivity on human Langerhans cells. 242 32

The activity of natural killer (NK) cells can be augmented by incubation with interferons, or with other compounds, such as staphylococcal protein A, which stimulate interferon production. In the experiments described here we compared the patterns of lytic activity of human lymphoid effector cells, before (NK-B) and after (NK-A) short-term activation. Target cells used were K562, Clone I (a partially NK-resistant K562 variant), and those that had been preincubated with neuraminidase or trypsin. The results obtained include the following: proteases, but not neuraminidase, decreased lysis by NK-B, but not by NK-A, of both K562 and Clone I in the standard Cr-release assay. In the single cell assay, trypsin minimally decreased conjugate formation and the fraction of bound cells that were killed by NK-B, but did not reverse the increased lytic efficiency of NK-A. In the cold-target competition assay, Clone I, which does not compete as well with K562 for NK-B, did so equally well for NK-A. Trypsinized targets, regardless of their equal sensitivity to lysis by NK-A, were not as active competitors for NK-A. We conclude that the most reasonable interpretation is that K562 cells bear surface structures which can induce release of lytic mediators from NK-A under conditions that are not sufficient to stimulate NK-B. Although it appears that NK-A may respond to a smaller number of the same target molecules recognized by NK-B, the process must be better defined at the molecular level to exclude the possibility that there are qualitative differences between the proposed recognition structures for these two states of NK activity.
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PMID:Target cell specificity of human natural killer cells. II. Apparent change with activation. 243 52

Ovine lentiviruses share genome sequence, structural features, and replicative mechanisms with HIV, the etiologic agent of AIDS. A lamb model of lentivirus-induced lymphoid interstitial pneumonia, comparable to lymphoid interstitial pneumonia associated with pediatric AIDS, was used to investigate production of leukocyte-soluble mediators. Lentivirus-infected lambs and adult sheep with severe lymphoid interstitial pneumonia had significantly elevated levels of spontaneous interferon (IFN) production from pulmonary leukocytes compared with ovine lentiviruses-infected animals with mild or no lesions of lymphoid interstitial pneumonia or non-infected controls. However, peripheral blood mononuclear cells from lentivirus-infected lambs did not spontaneously release significant amounts of IFN. IFN production by pulmonary lymph node lymphocytes was enhanced in the presence of lentivirus-infected alveolar macrophages. Animals with lentivirus-induced disease and spontaneous IFN production had enhanced virus replication within tissues. The ovine lentiviruses-induced IFN had a m.w. of between 25,000 and 35,000 and was resistant to freeze/thawing procedures. The IFN activity was sensitive to trypsin and stable to low pH and heat. IFN with similar physical and biochemical properties was produced when ovine lentiviruses was added to control leukocyte cultures. IL-2 and PGE2 production and responses to mitogen by pulmonary lymph node lymphocytes of lentivirus-diseased lambs were not statistically different from control animals. Increased local production of IFN in lentivirus-infected host tissues may serve to accelerate the entry of leukocytes into virus-induced lesions promoting cell-mediated tissue damage and also provide increased numbers of cells for virus replication.
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PMID:Spontaneous interferon production by pulmonary leukocytes is associated with lentivirus-induced lymphoid interstitial pneumonia. 244 76

The production of histamine-releasing factor (HRF) by human mononuclear cells has previously been reported. In this paper we describe the production of HRF by guinea pig spleen cells, thymocytes, and PBMC. Guinea pig lymphoid cells were cultured either alone or in the presence of mitogens (PHA and Con A) or specific Ag(OVA and keyhole limpet hemocyanin) and the dialyzed cell-free supernatant was tested for histamine-releasing activity on guinea pig lung mast cells and blood basophils. Lung mast cells were isolated by enzymatic digestion and partially purified by countercurrent elutriation and discontinuous Percoll gradient centrifugation. Guinea pig spleen cells, thymocytes, and PBMC spontaneously produced significant amounts of HRF. The production was enhanced upon stimulation with PHA or specific Ag in animals immunized with Ag in CFA. Two distinct species of HRF were identified with m.w. of 50,000 to 70,000 and 5000 to 8000 by gel chromatography. HRF is a trypsin- and chymotrypsin-sensitive heat-stable protein. It does not bind to Con A-Sepharose and its production is not inhibited by tunicamycin. HRF-induced histamine release from lung mast cells is a temperature-dependent process and is complete in 10 min at 37 degrees C. Intradermal injection of HRF caused an immediate ear-swelling reaction in guinea pigs. The most severe ear-swelling reactions did not resolve within 1 h, but instead evolved over a period of 12 to 24 h.
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PMID:Production and properties of histamine-releasing factor of guinea pigs. 245 Jan 35

The physiological interferon (IFN) response involves the production of little amounts of IFN in localized lymphoid microenvironments upon induction of exogenous and endogenous inducers. The aim of this work was to demonstrate whether dietary antigens and/or alimentary lectins could induce IFN in vivo after intraduodenal administration in rabbits. For this purpose we have collected simultaneously the abdominal lymph and plasma during the experiments for about 12 hours. The results show that while both onion' (Allium cepa) and cucumber' (Cucumis sativum) homogenates are ineffective, the hydrolysate of the latter induces a marked increase of IFN in the lymph suggesting that preliminary digestion (and probably gastric digestion) is crucial for the activation of IFN inducers. The maximum IFN activity occurs 7 hours after the administration and there is no concomitant activity in the plasma. Addition of bile salts to either the homogenates or the hydrolysates in unable to modify the pattern of the response. Preliminary characterization of the IFN activity has shown it to be trypsin-sensitive acid- and heat-stable and species-specific.
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PMID:The physiological interferon response. IX. Interferon activity in rabbit lymph after intraduodenal administration of alimentary lectins. 245 25

BALB/c mice were immunized with tyrosinase, partially purified in two stages from a human melanoma cell line. A hybridoma was obtained which produced monoclonal antibody (MoAb 1C11) reactive with 8/10 melanoma cell lines and 10/10 primary cultures of human melanocytes, neval cells, and melanomas. Immunoreactivity correlated to a certain extent with tyrosinase activity but not with melanin content. No crossreactivity was obtained with neuroblastoma, medulloblastoma, fibroblasts, keratinocytes, lymphoid cells, or murine melanomas. Purification of the antigen directly from cell lysates with a MoAb 1C11 CNBr-Sepharose affinity column gave a green-brown protein of 56 kDa with no detectable tyrosinase activity. This protein was therefore different from 60 kDa active tyrosinase, identified by enzyme activity and Western blotting with a MoAb derived previously (MoAb 5C12). Unlike 5C12, 1C11 reactivity was not destroyed by pretreatment of the antigen with periodate. Immunogold labelling showed that the 1C11-reactive antigen was associated with melanosomes, and there was close correlation between 5C12 and 1C11 reactivity in resistance to trypsin and in staining various melanocytic cell populations. MoAb 1C11 may therefore recognise a polypeptide epitope in a molecule closely linked to melanin biosynthesis.
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PMID:Monoclonal antibody against a melanosomal protein in melanotic and amelanotic human melanoma cells. 247 76

Previously, we have shown that some lymphoid cell lines adhere to fibronectin (FN)-coated substratum, whereas others do not. In this study, the adhesion of five adherent lymphoid cell lines to different FN domains was examined. These cell lines ranged in their adherence to substratum coated with FN, the cell-binding domain (CBD) fragment, or the heparin-binding domain (HBD) fragments. None of the cell lines adhered to substratum coated with the gelatin-binding domain fragment. Three of the lymphoid cell lines adhered preferentially to HBD over CBD, whereas two other lymphoid cell lines and BHK fibroblasts adhered preferentially to CBD. These results suggest that two distinct adhesive interactions occur between cells and FN and that the pattern of interaction varies among cell types. Using MOPC 315 (which adheres preferentially to HBD) as a cell model to study the cell-HBD interaction, the HBD-promoted adhesion was found to be independent of the RGD sequence and could be inhibited by anti-FN antibodies. Moreover, the MOPC 315-HBD interaction had the following characteristics: (1) adhesion was temperature dependent, (2) presence of divalent cations was necessary, (3) integrity of cellular microfilaments but not microtubules was required, (4) inhibition of protein synthesis abolished adhesion, (5) pretreatment of cells with trypsin inhibited adhesion, and (6) the adhesion was mediated by the carboxyl-terminal HBD.
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PMID:Adhesion of lymphoid cells to the carboxyl-terminal heparin-binding domains of fibronectin. 249 48

The studies presented herein describe (1) a sensitive, quantitative, and objective assay for detecting cell membrane-bound form of Fc receptors for IgE displayed on human lymphoid cells based on measuring unlabeled Fc epsilon R-bound IgE by a solid-phase RIA of cell lysate fluids; (2) the development and characterization of an IgM monoclonal antibody, termed 7E4, which is specific for human lymphocyte Fc epsilon RII (CD23) molecules; and (3) a system for reproducibly inducing de novo synthesis and expression of Fc epsilon RII proteins on human lymphocytes following exposure to the mitogenic lectin, pokeweed mitogen. The Fc epsilon RII molecules induced by exposure to PWM were proven to be present on lymphocytes, and not on other cell types in several ways, including (1) documenting sensitivity of such proteins to both acid pH and trypsin treatment, the latter manipulation being ineffective in removing Fc epsilon RII molecules on basophils and mast cells; (2) demonstrating specific reactivity of the expressed Fc epsilon RII molecules with the 7E4 monoclonal antibody, which is specific for human lymphocyte Fc epsilon RII molecules and does not react with Fc epsilon R molecules on other cell types; and (3) observing the required concomitant presence of both T and B lymphocytes during the induction process and proving that the induced Fc epsilon R+ cells are indeed B cells of the Leu-12+ phenotype by fluorescence analysis. The ability to induce expression of Fc epsilon RII molecules on human lymphocytes exposed to a mitogen such as PWM requires special technical attention to the method of preparation and isolation of human lymphoid cells from peripheral blood. This in vitro system for up-regulating Fc epsilon RII expression on human lymphocytes should provide us with an important new tool to analyze the participation of such cells in the regulatory mechanisms controlling the human IgE antibody system.
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PMID:Fc receptors for IgE (Fc epsilon R) on human lymphoid cells: inducible expression of Fc epsilon RII (CD23) on lymphocytes and detection by monoclonal anti-Fc epsilon RII antibody. 252 27


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