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

An aqueous extract of normal human skin has been shown to contain an inhibitor of certain cell mediated immune reactions. In this report, the effect of the inhibitor on cell membrane markers and antibody dependent cellular cytotoxicity was determined. Significant diminution of E rosette formation was demonstrated using as little as 0.6 microgram of the skin fraction (p less than .02). Fc receptors for both IgG and IgM were reduced by 46-96% of controls in the presence of the skin inhibitor. On the other hand, no effect on the detection of the complement receptor or surface immunoglobulin was observed, indicating some specificity of binding. In addition, the antibody dependent cell-mediated cytotoxic reaction was inhibited on the skin extract. It was shown that the inhibitor interacted with the lymphocytes, not the antibody or target cells. No effect was detectable when the skin fraction was added after the interactions of effector cells, antibody, and target cells had occurred. This was in contrast to PHA-induced cytotoxicity which could be inhibited following the preincubation of the lymphocytes with the mitogen. Thus there appears to be 2 mechanisms by which the skin fraction interferes with cellular responses: inhibition of antibody binding to Fc receptors, and interference with a step in cellular activation following mitogen stimulation. Analysis of the extract showed the inhibitor was inactivated by trypsin, and did not contain sialic acid, 5'-nucleotidase of beta-N-acetylglucosaminidase, and thus was not associated with membrane or lysosomal enzymes.
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PMID:Inhibition of cell-mediated immune reactions by an aqueous extract of normal human skin. 710 62

The effect of Basic-trypsin-inhibitor (BPTI) on the in vitro PHA-induced blastic transformation of lymphocytes is reported. Cultures of lymphocytes from healthy subjects were added with PHA, BPTI and PHA + BPTI; simple control-cultures were also performed. The blastic transformation was evaluated by morphologic method after 72 h incubation at 37 degrees C. The results are compared with Wilcoxon's test; it was observed that BPTI reduces the PHA-induced blastic transformation, but it has no effect on cultures without PHA. The hypothesis that BPTI inhibits only PHA-stimulated lymphocytes is suggested.
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PMID:[Action of the basic trypsin inhibitor on lymphocyte blastic transformation in vitro]. 732 96

The mAb A6 was produced by immunization of mice with human PHA-stimulated PBMC. Immunoprecipitation studies and staining of cell lines transfected with individual leukocyte common antigen (LCA) isoforms showed that A6 recognizes a unique epitope strongly expressed on the lower MW isoform (p180) of LCA, but also weakly expressed on the p190 isoform coded by exon B and the p205 coded by exons A and B. The epitope recognized by A6 was carbohydrate-dependent in that it was neuraminidase-sensitive, but trypsin-resistant. A6 strained most TCR-alpha beta+ cells with differential intensities, subdividing them into a bright and dim population, and strongly stained all TCR-gamma delta+ cells. A6 did not stain CD19+ B cells nor CD56+ NK cells. Anti-CD45 mAb such as UCHL1 recognizing CD45RO have been used to define memory T cells. Depletion of PBMC subsets with A6 or UCHL1 mAb dramatically decreased proliferative responses to the recall antigens anti-CD3 mAb and alloantigen and enhanced their responses to PHA. A6, unlike UCHL1, also depleted alloreactive T cells that affect primary and secondary MLC and CML. Thus, A6 was shown to recognize the lower MW isoforms of LCA which are expressed on functional T cell subsets including memory, activated, and alloreactive T cells.
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PMID:A monoclonal antibody (A6) recognizing a unique epitope restricted to CD45RO and RB isoforms of the leukocyte common antigen family identifies functional T cell subsets. 752 74

Proliferative activity of murine interleukin-2 (IL-2) dependent T cells (CTLL-2) was detected in the culture supernatant of canine peripheral blood lymphocytes (PBL) stimulated with phytohemagglutinin-P (PHA-P), and was defined as dog IL-2. The highest production of IL-2 was obtained under the conditions in which a PBL population of 2 x 10(6) cells/ml was stimulated with PHA-P at a concentration of 10 micrograms/ml at 38 degrees C for 48 hr. Dog IL-2 activity was significantly inhibited by heating at 65 degrees C, acidification under pH 4, alkalification over pH 10, and trypsin exposure. A peak of dog IL-2 activity was detected in the fraction with a molecular weight of approximately 31,000 by gel filtration. Long-term culture of canine lymphocytes was successful over 10 passages by using dog IL-2 with PHA-P-stimulation every 3 passages. The cultured cells mostly consisted of small- and medium-sized lymphocytes. These cells reacted to anti-dog thymocyte rabbit serum and anti-dog Thy-1 mouse monoclonal antibody. These cells were therefore considered to originate in T-lineage lymphocytes. Cytostasis of PBL from intact dogs reacting to canine transmissible venereal sarcoma cells was increased significantly when PBL was cultured for more than 30 days with homologous IL-2.
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PMID:Characterization of dog interleukin-2 activity. 811 17

A peptide inhibiting either corpuscolate or purified PKC has been identified from microsomes of PHA-activated human PBMC but it is not detectable in microsomes of resting PBMC. The peptide was obtained from a microsomal preparation in an oligomeric form that could be transformed into a monomeric form by beta-MSH. The active peptide (IN) was retained on a PC-11 chromatographic column and could be eluted with NaCl. IN is ineffective on PKC-dependent protamine phosphorylation of protamine and on Ca2+ and phospholipid-independent activity generated by mild hydrolysis with trypsin of PKC. Ca2+ binding is permissive for IN activity. IN inhibits particulate PKC in PHA-activated PBMC, but is ineffective after TPA activation. All these data indicate that IN acts at the regulatory domain of PKC.
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PMID:Identification of a novel protein kinase C inhibitor in microsomes from phytohaemagglutinin activated human peripheral blood mononuclear cells. 836 75

In many immunoinflammatory diseases, macrophages, by producing interleukin-1 (IL-1) and tumor necrosis factor alpha (TNF alpha), stimulate protease secretion in fibroblasts, thus contributing to tissue destruction. Monocyte/macrophage activation is prompted by soluble factors released by activated T cells as well as by cell-cell contact. Indeed, previous studies have shown that monocytes exposed to paraformaldehyde (PFA)-fixed, activated T cells produced high amounts of IL-1 beta. In this report, we used the T cell line HUT-78 to further characterize the T cell factor(s) responsible for monocyte activation by cell-cell contact. After subcellular fractionation, most of the activity was found in the cellular membrane fraction of PHA/PMA-stimulated HUT-78 cells, and proved to be due to glycoproteins, following trypsin digestion and tunicamycin treatment. HUT-78 cells acquired the capacity to stimulate monocytic cells after as little as 1h of stimulation. De novo protein synthesis was required for the expression of the IL-1 beta inducing factor, as shown by cycloheximide treatment. When membrane proteins of PHA/PMA-stimulated HUT-78 cells were separated on SDS-polyacrylamide gel, a peak of stimulatory activity was observed at Mr--25-35 x 10(3). By using specific cytokine inhibitors or blocking mAbs, we ascertained that cell-associated cytokines (IL-1, IL-2, IFN gamma and GM-CSF) were not involved in monocyte activation by cell contact. Anti-CD2 and -CD11a (LFA-1) mAbs partially blocked IL-1 beta production by -25% and -35%, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Cell surface glycoproteins expressed on activated human T cells induce production of interleukin-1 beta by monocytic cells: a possible role of CD69. 849 Jan 1

The acute effects of kidney bean (Phaseolus vulgaris) E2L2 lectins (PHA) given orally to conscious rats or continually infused into the duodenum of anesthetized rats on blood cholecystokinin (CCK), secretin, and gastrin and on secretion of pancreatic digestive enzymes have been evaluated. PHA increased circulating levels of CCK and secretin but did not alter gastrin. In addition, PHA induced dose-dependent secretion of trypsinogen, chymotrypsinogen, and alpha-amylase by the pancreas in vivo. This pancreas output appeared to be modulated only in part through CCK. Thus pretreatment of rats with a CCK-A receptor antagonist (L-364718) attenuated the immediate (< or = 90 min) pancreas secretory response to PHA but could not prevent a PHA-associated increase in digestive enzyme output in the longer term (after 90 min). In contrast, treatment of rats with L-364718 abolished the stimulatory effects of soyabean trypsin inhibitors on digestive enzyme secretion in both the short and long term. Additional mechanisms or hormones, such as secretin, may play a role in modulating later exocrine pancreas responses to PHA.
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PMID:Secretion of pancreatic digestive enzymes induced in rats by first-time oral exposure to kidney bean E2L2 lectin is mediated only in part by cholecystokinin (CCK). 1054 99

A primary cell culture system was developed for the cells of lymphoid organ tissue of kuruma shrimp, Penaeus japonicus. Minced tissues of lymphoid organs were seeded and incubated at 30 degrees C in medium 199 supplemented with 20% foetal bovine serum, a salt mixture and a lactalbumin hydrolysate (0.1 g/l). Fibroblast-like cells and epithelioid-like cells survived for 54 days. Cells did not survive after trypsin, collagenase or hyaluronidase treatment used for cell dissociation. Mitogens (Con A, PHA-P, Pokeweed) and insulin did not enhance cell proliferation. When penaeid rod-shaped DNA virus (PRDV) was inoculated into the lymphoid organ cell culture, a cytopathic effect was observed within 8 days. On the other hand, large granular haemocytes that were fractionated using a Percoll continuous density gradient were not infected with PRDV in vitro within 10 days, which was the longest period of haemocyte maintenance.
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PMID:Primary culture of lymphoid organ cells and haemocytes of kuruma shrimp, Penaeus japonicus. 1062 78

beta1-6 GlcNAc branching, a product of N-acetylglucosaminyltransferase V (GnT-V), is a key structure that is associated with malignant transformations and cancer metastasis. Although a number of reports concerning tumor metastasis-related glycoproteins that contain beta1-6 GlcNAc branching have appeared, the precise function of beta1-6 GlcNAc branching on glycoproteins remains to be elucidated. We previously reported on the importance of beta1-6 GlcNAc branching on matriptase in terms of proteolytic degradation in tumor metastasis. We report here that matriptase purified from GnT-V transfectant (beta1-6 GlcNAc matriptase) binds strongly to L4-PHA, which preferentially recognizes beta1-6 GlcNAc branches of tri- or tetraantennary sugar chains, indicating that the isolated matriptase contains beta1-6 GlcNAc branching. The beta1-6 GlcNAc matriptase was resistant to autodegradation, as well as trypsin digestion, compared with matriptase purified from mock-transfected cells. Furthermore, N-glycosidase-F treatment of beta1-6 GlcNAc matriptase greatly reduced its resistance to degradation. An analysis of matriptase mutants that do not contain potential N-glycosylation sites clearly shows that the beta1-6 GlcNAc branching on N-glycans attached to Asn 772 in the serine protease domain plays a major role in trypsin resistance. This is the first example of a demonstration of a direct relationship between beta1-6 GlcNAc branching and a biological function at the protein level.
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PMID:Addition of beta1-6 GlcNAc branching to the oligosaccharide attached to Asn 772 in the serine protease domain of matriptase plays a pivotal role in its stability and resistance against trypsin. 1455 Dec 20

We developed an easy and fast method to isolate extracellular matrix tenascin-X (TNX) from various tissues in mice based on TNX antibody affinity purification. We purified approximately 350-kDa cellular interstitial TNX (iTNX) from the spleen, liver and kidney as well as 200-kDa serum TNX (sTNX). Since the nature and significance of glycosylation in TNX remains to be elucidated, glycobiochemical properties of purified TNX were characterized by lectin blot analysis. Lectin blots by Con A, LCA, PHA-E4, RCA120 or WGA revealed the presence of N-glycan in the cellular TNX and especially complex-type N-glycan in the serum TNX. In addition, the iTNX from liver and kidney also possessed O-glycan based on the reaction to PNA. The binding to AAL indicated that iTNX from the three tissues possesses fucose linked alpha1,6 to a pentasaccharide core, whereas sTNX does not. The reaction to SSA but not to MAM suggested the presence of sialic acid linked alpha2,6 to galactose in both cellular and serum TNX. Lectin blots of trypsin-treated iTNX from the spleen also demonstrated that WGA alone reacts to the t300 product derived from the amino-terminal 300-kDa portion.
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PMID:Distinct glycosylation in interstitial and serum tenascin-X. 1726 79


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