Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The gland-specific enzymes amylase, lysozyme and kallikrein the activities and their dependence on the speed of salivation were studied in normal persons. In these investigations the specification or standard ranges for differentiated secretion states is useful. In contrast to amylase activity, the activities of lysozyme and kallikrein weaken appreciably with increasing speed of salivation. The activity secreted, as measured in time units, increases. In the case of a diseased parotis, a comparison of enzyme activities with the standard values will show a significant reduction of lysozyme and amylase activity in the chronic processes. Acute inflammation affects the amylase activity slightly, but raises the lysozyme activity significantly. Parotid mixed tumours probably do not lead to any changes in the enzyme activities. The splitting up of amylase into isoenzymes by polyacrylamide gel electrophoresis and its possible importance for the diagnosis of pathological processes are discussed. First results of the splitting up of the parotid lysozyme are reported.
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PMID:[Enzyme diagnosis of human parotid glands and its problems]. 126 18

Stimulation of polymorphonuclear leukocytes with kallikrein demonstrated that enzyme acts selectively on the release of lysosomal enzymes of these cells. The release of collagenase, similarly to the release of lysozyme into the incubation medium increased proportionally to kallikrein concentration and the duration of incubation. Kallikrein had a small effect on beta-glucuronidase secretion. No effect on cytoplasm lactate dehydrogenase release was detected. These results suggest that kallikrein, as a soluble stimulus, predominantly induces degranulation of specific granules containing collagenase capable of degrading the connective tissue. Secretion of lysozyme and collagenase requires the presence of active kallikrein. Soybean trypsin inhibitor diminished the enzyme release.
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PMID:Influence of human plasma kallikrein on lysosomal enzyme release from polymorphonuclear leukocytes. 165 May 20

A state of the kallikrein-kinin system, activity of proteolysis inhibitors were studied simultaneously with the functional activity of neutrophils and content of lysozyme in blood serum of 21 patients with chronic kidney insufficiency. Two types of alterations in the kallikrein-kinin system were found in 13 patients maintained on hemodialysis: in four patients content of kallikrein was increased 8-fold as compared with normal level with a decrease in content of prekallikrein, while in nine patients activity of kallikrein was similar to control values but content of prekallikrein was still further decreased. Content of alpha 1-proteinase inhibitor (PI) was distinctly decreased (2-2.5-fold) in these patients, however, the decrease of the inhibitor was not observed in four patients; activity of alpha 2-macroglobulin tended to decrease. The ratio of active neutrophils and content of lysozyme were increased in blood serum of the majority of the patients. Hemodialysis, activation of the kallikrein-kinin system and stimulation of neutrophils appear to be responsible for a decrease in PI activity. The decrease in the PI activity and stimulation of the kallikrein-kinin system suggest that impairments in regulation of proteolysis could be corrected by means of exogenous proteinase inhibitors. In crisis of allogenic kidney rejection activities of PI and prekallikrein were decreased. Drastic, uneven alterations of the patterns studied were detected in pyo-inflammatory complications not related to the rejection crisis.
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PMID:[Status of the kallikrein-kinin system, proteinase inhibitors and nonspecific resistance factors in patients with chronic kidney failure on hemodialysis as well as in kidney transplant recipients]. 172 60

Using immunochemical analysis with standard antisera, leukocyte thermostable alpha-glycoprotein (LT alpha G) was shown to be distinct from lactoferrin, lysozyme, and fibronectin. The determination of peroxidase and nonspecific elastase in immune precipitates of LT alpha G gave negative results. Affinity sorption of LT alpha G onto the pus protein component was revealed. Purified LT alpha G had amidolytic activity in response to a substrate for elastase (p-nitroanilide succinyl-trialanyl). The ability of LT alpha G to cause the hydrolysis of substrates for thrombin, kallikrein, plasmin was investigated. The identity of LT alpha G and granulocyte elastase is suggested.
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PMID:[Thermostable leukocyte alpha-glycoprotein: immunochemical study and enzyme activity research]. 310 19

gamma-Seminoprotein (gamma-Sm) is a human prostate-specific antigen and a serine protease judging from the complete amino acid sequence which shows extensive homology with the kallikrein family. The enzymatic activity of gamma-Sm was defined as a chymotrypsin-like activity using reduced and S-3-(trimethylated amino)propylated lysozyme and insulin-oxidized A and B chains as substrates. The -Leu/Ser- peptide bond of lysozyme was rapidly hydrolyzed by gamma-Sm. gamma-Sm also hydrolyzed the -Phe/Glu- of lysozyme and the -Leu/Cys(SO3H)- of insulin B chain. Insulin A chain and arginyl- or lysyl-linkage of these proteins were not hydrolyzed by gamma-Sm at all.
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PMID:The chymotrypsin-like activity of human prostate-specific antigen, gamma-seminoprotein. 369

Fifteen various serum and urine parameters were evaluated as indicators of renal alterations induced by lead in 82 male workers of a battery plant chronically exposed to lead (median of blood lead concentration: 2.03 mumol/l). The control group comprised 44 non-exposed healthy volunteers (0.34 mumol/l). High-molecular-mass proteins (transferrin, immunoglobulin G (IgG), (albumin)) were determined in urine as markers of glomerular integrity; low-molecular-weight proteins and parenchymal enzymes (alpha 1-microglobulin, beta 2-microglobulin, retinol-binding protein, lysozyme, ribonuclease, N-acetyl-beta-D-glucosaminidase (NAG), alanine aminopeptidase (AAP), alkaline phosphatase (AP), gamma-glutamyltransferase (GGT)) as indicators of changes in the proximal tubule; Tamm-Horsfall glycoprotein and kallikrein as markers of the distal tubule. There was a positive correlation between tubular indicators and blood lead concentration as well as the erythrocyte protoporphyrin (EPP). About 30% of the lead-exposed workers showed an increased excretion of alpha 1-microglobulin, NAG, ribonuclease, and/or Tamm-Horsfall protein, whereas the glomerular indicators remained unchanged. The combined determination of NAG and alpha 1-microglobulin in urine could be helpful in the early detection of lead-induced changes in the nephron.
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PMID:Changed excretion of urinary proteins and enzymes by chronic exposure to lead. 752 73

The contribution of an extended interaction site in tissue kallikreins to their substrate specificity was investigated using peptides of increasing length and with different amino acids in positions P5 and P6. These substrates were constructed from a consensus dodecapeptide sequence (VASPFRSYDLDA) deduced from the hydrolysis of short synthetic peptide substrates, and from the identification of the cleavage sites in reduced-pyridylethylated lysozyme by 6 rat tissue kallikreins. Though the specificity constant kcat/Km generally increases with increasing the peptide substrate length on its N-terminal end, individual residues at P4-P6 may specifically alter this value for specific kallikreins. A seryl residue at P4 induces a 20-fold decrease in the specificity constant with rK2 and rK9, but it slightly improves this value for rK1 and rK10. A tryptophan in P6 is unfavourable for both rK1 and rK2 but not for rK9 and rK10, whereas a negatively charged residue has a negative effect for all four kallikreins. This demonstrates the importance of an extended interaction site in kallikreins, and suggests that the differing specificities of individual kallikreins are partly due to the presence of proteinase subsites which accommodate residues remote from the scissile bond in the substrate. These sites could be located in variable loops that surround the kallikrein active sites, and correspond to regions of lower structural similarity. Molecular modeling studies indicate that loop 4 may contribute to the P4-P7 specificity of kallikreins.
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PMID:Substrate specificity of tissue kallikreins: importance of an extended interaction site. 781 30

The concentrations of total protein, albumin, amylase, IgA, lactoferrin, lysozyme and kallikrein in parotid saliva from 17 children with juvenile recurrent parotitis (JRP) in a non-active phase of disease and in healthy controls of the same number, sex and age were analysed after gustatory stimulation with 1%, 2% and 6% citric acid. There was a great individual variation in all analysed variables, especially in saliva from the diseased glands. Significantly raised levels of albumin, IgA, lactoferrin and kallikrein were found in the saliva from the JRP-children compared with the controls (p < 0.01-0.001), while total protein and alpha-amylase did not differ significantly. The sialo-chemical findings are discussed in the light of histological and bacteriological findings and support the hypothesis that the etiology of juvenile recurrent parotitis is a combination of congenital malformation of portions of the salivary ducts and a set-in infection.
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PMID:Salivary factors in children with recurrent parotitis. Part 2: Protein, albumin, amylase, IgA, lactoferrin lysozyme and kallikrein concentrations. 900 Mar 29