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)

The cytogenetic analysis of a patient with selective deficit of IgA and decrease in IgM, IgE, and IgG is presented. Using trypsin-Giemsa banding the karyotype showed monosomy 22 (45,XX,-22). The interest of this case lies in the rarity of the illness and in the association of monosomy 22 with hypogammaglobulinaemia and selective deficit of IgA, particularly as this chromosome is known to contain genes coding for immunoglobulin chains.
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PMID:Monosomy 22 with humoral immunodeficiency: is there an immunoglobulin chain deficit? 684 39

Sera from 14 patients with an IgA M-component, six of whom had myelomatosis and eight with benign monoclonal gammopathy (BMG) were analysed. All six sera from patients with high IgA (greater than 40 g/l) and total protein (greater than 100 g/l) concentrations were hyperviscous (HV). Four of these six patients also had hyperviscosity syndrome (HVS). There was no correlation between the quantity of IgA dimers or polymers and the presentation of HV and HVS. The binding between IgA and albumin and alpha 1-anti-trypsin was not covalent. Differences in the microenvironment of S-S bonds or of aromatic amino acids between isolated monoclonal monomeric and dimeric IgA were demonstrated with circular dichroism. Besides that, differences in hydrophobicity (exposure of aromatic amino acids) between IgA from normal serum and monomeric and dimeric IgA from a myeloma serum were revealed using hydrophobic interaction chromatography. The significance of hydrophobic interactions involving IgA and the influence of such forces on the circulation of the molecules are discussed.
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PMID:Factors affecting IgA related hyperviscosity. 685 Dec 49

A case of familial deficiency in alpha-1-antitrypsin connected with Pi-0Z gene led to the finding of a new Gcler variant partly deficient, the electrofocusing pattern of which, located between that of G and I variants, was modified after neuraminidase digestion. A study of three generations shows that Gcler variant is transmitter according to an autosomally codominant mode. Moreover serum trypsin inhibitory capacity and concentration of ten proteins have been measured in this family. Except the known relation between serum alpha-1-antitrypsin level and trypsin inhibitory, capacity, only serum IgA showed a significant correlation with serum alpha-1-antitrypsin in the deficient group with Pi-Z allele.
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PMID:Familial alpha-1-antitrypsin dificiency with Pi-Z and a new Pi-Gcler variant. 696 5

Serum IgE levels can be measured by reverse passive antiglobulin haemagglutination (RPAH) of trypsin-treated human or sheep red cells coupled to sheep IgG anti-human IgE by chromic chloride. The results show a high correlation with those obtained by the radioactive single radial immunodiffusion method. Interfering anti-sheep IgG factors can be easily removed by absorption with small amounts of whole sheep or bovine serum cross-linked with glutaraldehyde. Standardisation with the British standard for IgE shows that the detection limit of the RPAH method is 0.5 IU/ml (1.2 ng/ml). The system is therefore comparable in sensitivity to the paper radio-immunosorbent test, and has the advantages of being simple, rapid and cheap. The RPAH method can be used to measure any class of immunoglobulin. For IgA the detection limit is found to be 10(-4) IU/ml (1.4 ng/ml).
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PMID:Measurement of human serum IgE and IgA by reverse passive antiglobulin haemagglutination. 697 Jan 83

Intralesional plasma cells and serological responses were investigated in 20 Brazilian cases of cutaneous leishmaniasis. Plasma cell numbers varied from less than 10% to more than 50% of cells in inflammatory infiltrates, in general with greater numbers of such cells present in lesions of longer duration. Direct fluorescence examination with anti-IgG, -IgA and -IgM sera of trypsin-treated sections of formalin-fixed biopsy tissue revealed that most intralesional plasma cells contained IgG. Russell bodies were detected in eight cases, in seven of which these bodies fluoresced only with anti-IgM serum. There was no correlation between serum levels of total IgG, IgA and IgM (detected by radial immunodiffusion) or antileishmanial antibodies (detected by class-specific indirect immunofluorescence and by direct agglutination with and without 2-mercaptoethanol) and numbers of intralesional plasma cells of the same globulin class. No striking or consistent alterations in complement components were noted in the serum of these patients.
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PMID:Intralesional plasma cells and serological responses in human cutaneous leishmaniasis. 704 25

Several methods to demonstrate human immunoglobulin (Ig) A in glycol methacrylate (GMA)-embedded colon are explored. Following routine fixation in neutral buffered formalin, the tissue was dehydrated and embedded in GMA. Two-micron thick sections were heat-fixed (70 to 80 degrees C) to glass slides and then soaked in either xylene or acetone to etch the GMA. Following rehydration of the sections in serial alcohols and water, tissues were treated with phosphate buffered saline (PBS) and/or a variety of enzymes (trypsin, protease V, protease VI, pepsin, and papain) for varying periods of time. After an overnight soak in PBS the tissues were stained with fluorescein-conjugated anti-human IgA and then rinsed with PBS. This technique demonstrated excellent fluorescence of the IgA-containing plasma cells and of the discrete IgA-containing vesicles normally found in the surface epithelial cells of colon. Results were best with tissues etched with xylene and digested with 0.25 mg/ml protease V in PBS, pH 7.4, for 2 hr at 37 degrees C, followed by an overnight soak in PBS. Almost no fluorescence was seen in sections not digested with enzymes. The present method offers a simple convenient technique to perform immunofluorescence for immunoglobulin antigens on GMA-embedded tissue.
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PMID:Detection of immunoglobulin A by immunofluorescence in glycol methacrylate-embedded human colon. 704 38

A cell-ELISA was developed using monolayers of glutaraldehyde-fixed normal as well as Plasmodium berghei-infected mouse erythrocytes for quantification and characterization of anti-erythrocytic autoantibodies in murine malaria. Testing normal (NMS) and peak parasitaemic sera (PPS) on erythrocyte monolayers treated with trypsin, sodium meta periodate, neuraminidase or heat, and competitive inhibition of antibodies with soluble sialic acid, revealed that some anti-erythrocytic antibodies (which increase during the parasitaemic phase of infection) recognize N-acetyl neuraminic acid (NANA) residues on host erythrocytes. High levels of antibodies to NANA covalently conjugated to bovine serum albumin (BSA) were detectable in PPS. Such antibodies could be significantly absorbed out by preincubation of PPS with mouse erythrocytes (MRBC). Antibodies in PPS, when affinity-purified on a column of Fetuin-Agarose, were found to be reactive to normal as well as parasitized erythrocyte monolayers. Immunoglobulin isotyping and IgG subgroup typing revealed that most of the anti-erythrocytic autoantibodies in NMS were IgM and IgA, while in PPS there was an appreciable increase in IgG2a and IgG3. Affinity-purified anti-NANA antibodies reacted with DNA when tested in an ELISA. There was a significant positive correlation between anti-erythrocytic antibody and DNA-binding levels in NMS as well as PPS. The DNA-binding antibodies in PPS could be effectively absorbed out by preincubation of sera with fresh MRBC. Affinity determination of anti-erythrocytic antibodies eluted from MRBC revealed binding characteristics in the following order: MRBC > single-stranded DNA > double-stranded DNA.
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PMID:Murine malaria: anti-erythrocytic antibodies recognize N-acetyl neuraminic acid residues. 750 18

Colostrum samples from 49 Jersey cows were analyzed for concentrations of trypsin inhibitor, IgG, IgM, IgA, TS, fat, specific gravity, and N fractions. Colostrum (100 ml) was sampled from each cow as soon as possible after parturition. Mean concentrations of IgG, IgM, and IgA were 84.6, 3.4, and 4.5 g/L, respectively. Mean concentration of trypsin inhibitor was 56 mg of trypsin inhibited/dl of colostrum. Concentration of trypsin inhibitor was unaffected by lactation number and averaged 60, 53, and 54 mg of trypsin inhibited/dl of colostrum for cows in first, second, and third or later lactations, respectively. Colostral trypsin inhibitor and IgG were correlated (.54), although correlations between trypsin inhibitor and IgM and IgA were not significant. Trypsin inhibitor in colostrum was also positively correlated with fat, total N, protein N, noncasein N, and TS in colostrum. Variation in concentration of trypsin inhibitor from first-milking colostrum was closely related to colostral IgG concentration and may serve to protect IgG and other proteins from proteolytic degradation in the intestine of the neonatal calf.
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PMID:Concentrations of trypsin inhibitor and immunoglobulins in colostrum of Jersey cows. 759 51

Sixteen German Shepherd Dogs from 4 litters were IgA-deficient on the basis of at least 1 of 2 serum IgA determinations, and all had small intestinal bacterial overgrowth, as documented by quantitated small intestinal bacterial culture in another study. These dogs were fed 2 diets that differed principally in their protein source (chicken vs beef, milk, and wheat). All dogs were fed each diet for 2 weeks before the study began. Next, all dogs were fed the chicken-based diet for 2 months. Then, half the dogs (group 1) were randomly assigned to continue eating the chicken-based diet, while the other half (group 2) ate a diet containing beef, milk, and wheat proteins. The small intestine was biopsied at the beginning of the study and after dogs had eaten the assigned diet for 2 and 4 months. At 2 months, group-2 dogs had more colonic mucosal mast cells, but this difference did not persist at 4 months. At the end of the study (ie, 4 months), although all dogs were clinically normal, group-2 dogs had significantly (P = 0.010) decreased numbers of jejunal villus plasma cells. However, these histologic changes were not considered clinically important. There were no significant differences in blood eosinophil counts, serum trypsin-like immunoreactivity, or cobalamin, folate, or IgA concentration. Clinical differences were not detected between the 2 groups, before or after the study. Changes were seen in serum IgM and IgG concentrations.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Changes in the intestinal mucosal cell populations of German shepherd dogs fed diets containing different protein sources. 777 2

Classically, the polymeric immunoglobulin receptor and its ligand, IgA, are thought to be sorted from basolateral early endosomes into transcytotic vesicles that directly fuse with the apical plasma membrane. In contrast, we have found that in MDCK cells IgA is delivered from basolateral endosomes to apical endosomes and only then to the apical cell surface. When internalized from the basolateral surface of MDCK cells IgA is found to accumulate under the apical plasma membrane in a compartment that is accessible to two apically added membrane markers: anti-secretory component Fab fragments, and avidin internalized from the biotinylated apical pole of the cell. This accumulation occurs in the presence of apical trypsin, which prevents internalization of the ligand from the apical cell surface. Using a modification of the diaminobenzidine density-shift assay, we estimate that approximately 80% of basolaterally internalized IgA resides in the apical endosomal compartment. In addition, approximately 50% of basolaterally internalized transferrin, a basolateral recycling protein, has access to this apical endosomal compartment and is efficiently recycled back to the basolateral surface. Microtubules are required for the organization of the apical endosomal compartment and it is dispersed in nocodazole-treated cells. Moreover, this compartment is largely inaccessible to fluid-phase markers added to either pole of the cell, and therefore seems analogous to the recycling endosome described in nonpolarized cells. We propose a model in which transcytosis is not a specialized pathway that uses unique transcytotic vesicles, but rather combines portions of pathways used by non-transcytosing molecules.
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PMID:Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. 813 76


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