Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Aminopeptidase from dysgerminoma was purified and characterized using L-leucine-beta-naphthylamide as substrate. The enzyme was resistant to puromycin, methionine, amastatin, bastatin, and EDTA, and it was heat labile at 60 degrees C. The enzyme showed the same electrophoretic mobility as pregnant-patient serum oxytocinase CAP1 on polyacrylamide gel electrophoresis. Km value against S-benzylcysteine-p-nitroanilide was 4.2 X 10(-4) M. Oxytocin and vasopressin competitively inhibited the enzyme activity. Molecular weight of the enzyme was estimated to be 80,000 by Sephadex G-200 column chromatography. These results suggest that aminopeptidase from dysgerminoma is an oxytocinase-like enzyme, a placenta-specific protein.
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PMID:Oxytocinase-like enzyme in an ovarian dysgerminoma: a placenta-specific protein. 408 42

We describe an 8 year-old girl with established diabetes insipidus who developed cyclophosphamide-associated antidiuresis. The patient had received cyclophosphamide as part of a high-dose chemotherapy regimen for recurrent suprasellar dysgerminoma prior to autologous bone marrow transplantation. Urinary output decreased and specific gravity increased shortly after a 1 hour i.v. infusion of 50 mg/kg cyclophosphamide and the effect lasted some 5 hours. No other drug could be implicated. This response, occurring in a patient with no ability to secrete vasopressin, suggests a direct tubular effect of one or more cyclophosphamide metabolites. Administering i.v. cyclophosphamide requires careful monitoring of fluid balance in order to avoid water intoxication. Further research is warranted both into the mechanism of this effect and the metabolite responsible for it.
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PMID:Cyclophosphamide and water retention: mechanism revisited. 1090 95