Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30536 (PBS)
 9,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We previously reported that the intraperitoneal and intrabursal administration of bestatin, an aminopeptidase inhibitor, enhanced follicular growth and ovulation in immature mice. In this study, we examined the effect of bestatin on follicular growth and ovulation under the conditions in which the ovarian response to gonadotropins was suppressed. Immature female mice were exposed to 72-h continuous lighting (on days 20-22 of life), or to 24-h starvation (on day 20). On days 20-22, bestatin (4 mg/ml, 100 microl) or PBS (100 microl) was administered ip. 4 times and pregnant mare serum gonadotropin (PMSG, 5 IU) and hCG (5 IU) were given on days 21 and 23, respectively. The numbers of ovulated oocytes per mice were significantly attenuated by both stresses. Bestatin significantly enhanced the numbers of ovulated oocytes under both lighting (49.5+/-7.0 vs. 28.0+/-5.5) and starvation (28.6+/-2.6 vs. 20.2+/-2.0) stresses (with vs. without bestatin, P<0.05). When follicular development was stimulated by PMSG (20 IU) on day 21, the serum estradiol concentration on day 23 was also suppressed by both stresses, but enhanced by bestatin under lighting (231.3+/-36.0 vs. 111.0+/-23.0 pg/ml) and starvation (151.9+/-8.8 vs. 90.7+/-15.4 pg/ml) stresses (with vs. without bestatin, P<0.01). Northern blot analysis revealed that the expression of P450arom-mRNA in the ovaries induced by PMSG (20 IU) was increased on day 23 by treatment with bestatin under starvation stress. These results indicated that stress inhibited the ovarian response to gonadotropins and that bestatin restored the response suppressed by stress.
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PMID:Bestatin, an aminopeptidase inhibitor, promotes follicular growth and ovulation suppressed by stress in mice. 988 5

Recombinant human epidermal growth factor (rhEGF), a polypeptide of 53 amino acid residues, is subject to degradation by numerous enzymes, especially proteases, when it is applied on the skin for the treatment of open wound. Amastatin, aprotinin, bestatin, EDTA, EGTA, gabexate, gentamicin, leupeptin, and TPCK were investigated for the possible protease inhibitors, which may use to protect rhEGF from degradation by the enzymes in the skin. Skin homogenates containing protease inhibitors and rhEGF were incubated at 37 degrees C for 30 minutes. After the reaction was stopped with trifluoroacetic acid, the amount of rhEGF remaining in the sample was determined with an HPLC method. The percentages of rhEGF degraded, at the skin/PBS ratio of 0.25, in the mouse, rat, and human skin homogenate were 85%, 70%, and 46%, respectively. The degree of degradation of rhEGF in the cytosolic fraction was higher than that in the membrane fraction and these enzyme reactions were completed in 30 minutes. Bestatin, EGTA, and TPCK showed significant inhibitory effects on the degradation of rhEGF in the two fractions (p<0.05), while the other protease inhibitors had no significant inhibitory effects or, even resulted in deleterious effects. Therefore, the formulation containing one or several inhibitors among these effective inhibitors would be a promising topical preparation of rhEGF for the treatment of open wound.
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PMID:Effect of protease inhibitors on degradation of recombinant human epidermal growth factor in skin tissue. 1897 9