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

To see whether urine enzyme activities could be used as an index in evaluating the disease status of leukemia patients, we examined the activities of four enzymes: arylsulfatases A(AS-A) and B(AS-B), alkaline phosphatase (AP), and lactate dehydrogenase (LDH). AP and LDH showed no consistent patterns. The activities of AS-A and AS-B correlated well with the patient's clinical status, increasing during progression of disease and decreasing toward normal activities during responses to therapy, as judged from bone marrow cellularity and differential. Among 23 untreated patients with a histologic diagnosis of acute leukemia we found increased activities of the urine enzymes in these proportions: AS-A in 23 patients (100%), AS-B in 22 (95.7%), AP in 7 (30.4%), and LDH in 10 (43.5%). Five patients in remission from acute leukemia had normal activities for all four enzymes. In one patient in remission for more than one year, a rise in urinary arylsulfatase activity preceded observable bone marrow relapse by 4 months. Unlike that of serum of urine lysozyme and serum copper, the determination of urine arylsulfatase activities appears to be a consistent, useful indicator of response to antileukemic therapy. In contrast to the determination of polyamines, the quantitation of arylsulfatase activity is achieved with greater ease and with instrumentation available in most clinical laboratories.
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PMID:A noninvasive technique for monitoring response to chemotherapy in human acute leukemia. 3

Statistics from a 64 case study showed that mucinous adenocarcinoma was apt to invade the intestinal wall and to metastasize to lymph nodes (P < 0.05). The activity of arylsulfatase and lysozyme of mucinous adenocarcinoma was stronger than that of the papillary and tubular adenocarcinoma (P < 0.05). In RR staining for electron microscopic observation, a significant decrease of proteoglycan granules was found in the surrounding matrix of mucinous adenocarcinoma, which correlated with the amount of arylsulfatase and lysozyme secreted by mucinous adenocarcinoma. These enzymes reduced the degree of sulfation in heparan sulfate and degraded proteoglycans. The proteoglycan structural barrier having been destroyed, facilitates mucinous adenocarcinoma to infiltrate and metastasize.
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PMID:[A study on the mechanism of invasion of colorectal mucinous adenocarcinoma]. 787 65

AIM:To study the distribution of arylsulfatase,beta-galactosidase and lysozyme in gastric cancer cells, and its relationship to differentiation and invasion of gastric cancer cells.METHODS: Histochemical, immunohistochemical and ruthenium red (RR) electrocytochemical technique for three types of hydrolases and proteoglycans in pericancerous matrix in 33 cases of gastric cancer were observed under light and electron microscopy.RESULTS:The expression intensities of arylsulfatase,beta-glactosidase and lysozyme in mucinous cell carcinomas were more intensive than those in well-differentiated and poorly-differentiated adenocar-cinomas (P < 0.05-0.01). The fibrous tissues smooth muscle and proteoglycans close to the cancer cells were degraded. They were found in the region far from the cancer cells. Expression of three enzymes mentioned above was low in adenocarcinoma cells, and fibrous tissues and RR granules were present and intact near the well-differentiated and poorly differentiated adenocarcinoma cells.CONCLUSION: Mucinous cell carcinoma may release various hydrolases into extra-cellular matrix, inducing degradation of pericancerous matrix and facilitating cancer cell invasion and metastasis.
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PMID:Arylsulfatase, betagalactosidase and lysozyme in gastric cancer cells and its relationship to invasion. 1181 31

Eosinophils were separated from other types of cells in horse blood or rat peritoneal fluid by centrifugation in concentrated albumin solutions. Eosinophils did not appear to be damaged by this separation procedure. A technique was also devised for isolation of cytoplasmic granules from eosinophils, thus allowing studies on enzyme content of the granules. Granules from both horse and rat eosinophils contained a number of hydrolytic enzymes, similar in variety and in concentration to those previously found in granules of rabbit polymorphonuclear leucocytes. Eosinophil granules differed from those of the rabbit granulocyte in their high content of peroxidase and the absence of lysozyme and phagocytin. On disruption of eosinophil granules by repeated freezing and thawing in saline, cathepsin, ribonuclease, arylsulfatase and beta glucuronidase were released into solution, but phosphatases were partially and peroxidase completely bound to the insoluble granule residue. Peroxidase could be extracted from the granule residue with weak acid. Eosinophil granules thus are lysosome-like structures.
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PMID:ISOLATION OF GRANULES FROM EOSINOPHIL LEUCOCYTES AND STUDY OF THEIR ENZYME CONTENT. 1407 91