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

Smoking habits have no differentiating effect on the functional activity of protease inhibitor (alpha 1PI) in the serum and bronchoalveolar lavage fluid (BALF). In the BALF, the trypsin-inhibitory capacity TIC/alpha 1PI ratio is significantly greater in patients with emphysema than in non-emphysematous subjects. PIC/alpha 1PI ratios that are greater than 1 demonstrate the existence of additional antiproteases in the lower respiratory tract.
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PMID:[Trypsin and pancreatic elastase-inhibitory capacity of serum and bronchoalveolar lavage fluid of smokers, ex-smokers and nonsmokers]. 236 87

P-glycoprotein (PGP), an active efflux pump of antitumor agents in multidrug-resistant tumor cells, exists in brain capillary endothelium and could be functionally involved in the blood-brain barrier. To study the regulatory mechanism of PGP expression in brain capillary endothelium, various mouse tissue matrices were tested for their abilities to enhance the expression of PGP in mouse brain capillary endothelial cells (MBEC), which express relatively small amounts of PGP. Of the four tissue matrices we examined, PGP expression in MBEC cultured on the brain matrix increased 2.0-fold. The PGP-inducing activity was similarly detected in bovine brain matrix, and the activity was enriched in the fraction of pl 9.0 by isoelectric focusing. The fraction, named PIC-fraction (PGP-inducing component), increased the PGP expression in MBEC 3.5-fold. By Northern blot analysis, a 3.3-fold enhancement of mdr gene expression was observed in MBEC cultured on the PIC-fraction. The PGP-inducing activity of the PIC-fraction was reduced by the treatment with trypsin but not with collagenase, suggesting that a proteinaceous factor distinct from type I collagen might be responsible for the PGP-inducing activity of PIC-fraction. Although the PIC-fraction increased the PGP expression in other mouse brain capillary endothelial cells, the PIC-fraction did not increase PGP expression in mouse aortic endothelial cells and KB carcinoma cell lines expressing various amounts of PGP. These observations suggest that PGP expression in brain capillary endothelium is specifically regulated by a tissue-specific factor in the brain matrix.
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PMID:Enhanced expression by the brain matrix of P-glycoprotein in brain capillary endothelial cells. 784 16

1. Using two-dimensional electrophoresis (IEF, pH 3.5-6.0 and PAGE, 11.5% T, pH 7.9) the caprine plasma proteinase inhibitors were classified into six distinct classes, designated PIA, PIB, PIC, PID, PIE and PIF. Differentiation of the six inhibitors was based on electrophoretic criteria, their abilities to inhibit bovine trypsin and chymotrypsin and their crossreactions with antisera to human alpha 1-antitrypsin and alpha 1-antichymotrypsin. 2. Polymorphic variants were identified for five of the protein systems (PIA, PIB, PIC, PID and PIE) and the electrophoretic data indicated that the variants were controlled by allelic genes. PIF proteins were poorly resolved and invariant. 3. Treatment of selected plasmas with neuraminidase demonstrated that the microheterogeneity observed in the PIA, PIB, PIC and PID proteins was attributable to sialic acid additions. 4. The inhibitory activities of all six caprine proteinase inhibitors were unaffected by chemical oxidation with chloramine-T.
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PMID:Caprine plasma proteinase inhibitors--I. Partial characterization. 844 83

Hepatic fibrosis often occurs in alcoholic liver diseases without accompanying tissue necrosis or inflammation. However, the precise mechanism of this fibrosis has not been fully clarified. In the present study, using the hepatoblastoma cell line HepG2 as a model for hepatocytes, we identified a factor that stimulates collagen synthesis of fibroblasts in a conditioned medium of HepG2 cells after treatment with ethanol. Type 1 procollagen peptide (PIC) in a culture of human fibroblast IMR-90 markedly increased after incubation with the conditioned medium of ethanol-treated HepG2 cells. The stimulating activity on the production of PIC by IMR-90 remained after the dialysis and evaporation of the conditioned medium of HepG2 cells, indicating this factor was not as volatile from low molecular substances such as acetaldehyde, acetate, or lactate. The activity of this factor diminished with heat or trypsin treatment. A gel chromatographic analysis disclosed that the molecular weight of this factor was approximately 8000 Da. These results suggest that a polypeptide factor secreted from HepG2 cells by treatment with ethanol stimulates collagen synthesis of fibroblasts.
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PMID:Detection of activity in the conditioned medium of ethanol-treated HepG2 cells which stimulates collagen synthesis in IMR-90 cells. 865 93