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)

Electrolyte disturbances in leukemia can be the result of the disease process or drug therapy. One group of electrolyte abnormalities is related to the stage of the leukemic process. Included in this group are newly diagnosed patients who may show elevated serum potassium, phosphorus, and magnesium--a result of their release from malignant cells after cytotoxic therapy or their accumulation due to urate nephropathy. Patients in remission usually have normal serum electrolyte concentrations, but acute leukemia patients during relapse may have hypokalemia, hypophosphatemia, and hypomagnesemia. This imbalance may be related to cellular uptake of these electrolytes in the presence of inadequate dietary intake. Other factors contributing to electrolyte derangements, and related to the leukemic process, include hyponatremia and hypochloremia secondary to the SIADH, hypokalemia in acute monocytic or acute myelomonocytic leukemia due to lysozyme-induced tubular damage, hypercalcemia possibly secondary to leukemic infiltration of bone or parathyroid glands (with PTH release), or production of a PTH-like substance by leukemic cells. Nonspecific factors related to the disease process which may aggravate the electrolyte imbalance include gastrointestinal loss through nausea, vomiting, and malnutrition. The drug-related electrolyte abnormalities include cyclophosphamide- and vincristine-induced SIADH; decreased serum sodium, chloride, potassium, and calcium concentrations as a result of polymyxin B nephrotoxicity; hypokalemia and hypomagnesemia secondary to amphotericin B; hypocalcemia, hypophosphatemia, and hyperphosphaturia due to L-asparaginase-induced hypoparathyroidism; hypokalemia due to a nonreabsorbable anion effect of antibiotics in the distal tubule or changes in membrane ionic transport of all cells by large doses of antibiotics. Electrolyte disturbance in leukemia thus have a multifactorial pathogenesis which can best be delineated according to the stage of the leukemic process and the drugs being used. Recognition of the cause or causes in a particular patient is essential for an effective approach to management. This review emphasizes the need for routine measurement of serum electrolytes during all phases of the leukemic process.
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PMID:Electrolyte and acid-base disturbances in the management of leukemia. 26 90

The N-terminal amino acid sequences of purified recombinant human gamma-interferon, alpha 2a-interferon and interleukin-2 expressed in E. coli were determined on an Applied Biosystems 477A Protein/Peptide Sequencer and 120A PTH Amino Acid Analyzer. From the raw chromatographic data of these samples, the identity, heterogeneity, amount of methionine-plus species remaining in the final products, and the probable process contaminants were evaluated with the help of computer methods including database searching. General methods to characterize trace contaminants in protein samples were also discussed. Among the sequenced samples, only gamma-interferon was shown to be N-terminal homogeneous. Methionine-containing species were found in interleukin-2 and alpha 2a-interferon. Chicken eggwhite lysozyme was detected in very small amounts in one batch of samples. These results provide valuable information for the development and improvement of preparation methods as well as regulatory responses to recombinant products.
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PMID:Evaluation of the purity of recombinant proteins and detection of residual protein contaminants via N-terminal microsequencing and database searching. 180 20

A metallo-endopeptidase, which appears to be an integral membrane protein of rat kidney, was purified to homogeneity by a series of standard chromatographic procedures. This enzyme significantly hydrolyzed human parathyroid hormone [hPTH(1-84)] and a synthetic substrate Suc-Leu-Leu-Val-Tyr-Mec (Suc = succinyl, Mec = 4-methyl-coumarinyl-7-amide). The purified enzyme had apparent molecular masses of 250 kDa on gel filtration, and 88 kDa and 245 kDa on sodium dodecyl sulfate/polyacrylamide gel electrophoresis under reducing and non-reducing conditions, respectively. Its pH optimum for activity was 8.0-8.5 and its isoelectric point was pH 4.9. Its activity was inhibited by EDTA, EGTA and o-phenanthroline, but not by phosphoramidon. The metal-depleted enzyme was reactivated by the addition of metal ions. The enzyme was also inhibited by chymostatin and eglin C, and by thiol compounds. Of the synthetic substrates examined, the enzyme hydrolyzed only Suc-Leu-Leu-Val-Tyr-Mec, one of the synthetic substrates for alpha-chymotrypsin. It did not hydrolyze synthetic substrates with less than four amino acid residues with tyrosine in the P1 position. The enzyme hydrolyzed hPTH and reduced hen egg lysozyme but did not hydrolyze azocasein or [3H]methyl-casein. NH2-terminal amino acid sequence analyses of the degradation products of hPTH(1-84) and reduced hen egg lysozyme by the purified enzyme revealed that the enzyme preferentially cleaved these peptides at peptide bonds flanked by hydrophilic amino acid residues. Amino acid analyses showed that the main degradation products of PTH were hPTH(17-29), hPTH(30-38) and hPTH(74-84). The ability of the enzyme to hydrolyze peptide bonds flanked by hydrophilic amino acid residues and its inability to degrade azocasein distinguish it from several other kidney endopeptidases reported, such as endopeptidase 24.11 and meprin.
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PMID:A membrane-bound metallo-endopeptidase from rat kidney hydrolyzing parathyroid hormone. Purification and characterization. 188 19

Sections of primary lung carcinomas, lung metastases, mesotheliomas, and lung metastases of some rare mesenchymal tumors were incubated with different cytokeratin (CK), vimentin, desmin, and tissue polypeptide antigen (TPA) antibodies and with antibodies reactive with different hormones (ACTH, PTH, alpha-HCG, Calcitonin CT), CEA, carcinoma-associated antigen (CA1), secretory component (SC), neuron-specific enolase (NSE), alpha-1-antitrypsin (alpha-1-AT), lysozyme (lyso), and S-100 protein (S 100). CK antibodies derived from a 49 kD (reactive with simple epithelia [SE]) and a 67 kD CK polypeptide fraction (reaction with complex epithelia [CE] were useful differentiation markers for the four major groups of lung carcinomas. In one half of small cell carcinomas a positive reaction with NSE antibodies was found. S 100 and SC were good markers for papillary and bronchioloalveolar adenocarcinomas, whereas CEA was less important because of its reactivity with different types of lung carcinomas. To discern clear cell carcinomas of lung and renal origin a positive reaction with vimentin antibodies (some renal but not lung types) and with CA1 (no renal but all lung types) seemed to be useful. All hormone antibodies were of no importance as markers for difficult differential diagnosis, because positive reactivities were found in cases from every major carcinoma group. In addition, a Ca2+-activated adenosine triphosphatase (ATPase) was found in mesotheliomas but not in papillary adenocarcinomas.
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PMID:Immunohistochemical and histochemical markers of primary lung cancer, lung metastases, and pleural mesotheliomas. 243 80

A 53-year-old man was admitted to Osaka City University Hospital on July 21, 1998, for investigation of symptomatic hypercalcemia. Laboratory data on admission revealed that serum Ca had increased to around 12.6 mg/dl and there was a significant increase in urinary Ca excretion. The serum phosphate level remained normal. Although the serum PTH level was below the detection limit, serum 1,25-dihydroxyvitamin D (1,25(OH)2D) was increased. Diagnosis of sarcoidosis was supported by a negative tuberculin test and by the elevated levels of serum angiotensin-converting enzyme (ACE), lysozyme activity, and CD4/CD8 ratio in bronchoalveolar lavage specimen; there was however no imaging evidence of sarcoidosis such as bilateral hilar lymphnode enlargement on chest X-ray, high resolution CT or 67Ga citrate scintigraphy. Biopsy specimens from the cervical lymphnode revealed no epitheloid cell granulomas or giant cells. Administration of prednisolone achieved a decrease in serum ACE and 1,25(OH)2D levels, followed by restoration of serum Ca and urinary Ca excretion to the normal range, and finally by an increase of serum PTH to the normal level. These observations suggested that the hypercalcemia could be explained by extrarenal production of 1,25(OH)2D. We report here on this rare case of sarcoidosis with initial symptoms of symptomatic hypercalcemia resulting from extrarenal production of 1,25(OH)2D.
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PMID:Sarcoidosis initially manifesting as symptomatic hypercalcemia with the absence of organic involvement. 1213 77

We report the case of a 54-year-old woman who presented on May 28, 2001 with sarcoidosis overlapping with rheumatoid arthritis. She had experienced morning stiffness 2 years previously and was diagnosed as having rheumatoid arthritis. She had been treated with bucillamine and loxoprofen for 3 months. In October 2000, she developed proteinurea. The patient discontinued treatment with bucillamine and loxoprofen. Proteinurea persisted, and the patient's renal function declined. On admission, subcutaneous nodules were palpable in the patient's legs. The patient's serum creatinine and calcium levels were 2.49 mg/dl and 11.6 mg/dl, respectively. Intact-PTH was suppressed, and PTHrP was not elevated. Despite the presence of hypercalcemia, the patient's serum 1 alpha 25(OH)2D3 was not suppressed. Serum ACE and lysozyme levels were elevated beyond the normal ranges. A renal biopsy was performed, and non-caseous epithelioid granuloma was found in the renal interstitium. Based on the histological findings, the patient was diagnosed as having sarcoidosis. Following treatment with prednisolone, the patient's serum calcium levels returned to normal and her renal function improved.
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PMID:[A case of sarcoidosis overlapping with rheumatoid arthritis]. 1280 76