The Animal Reproduction Symposium Committee charged with planning the X Biennial Symposium on Animal Reproduction to be held in conjunction with the 1971 Annual Meeting of the American Society of Animal Science was ap...
The Animal Reproduction Symposium Committee charged with planning the X Biennial Symposium on Animal Reproduction to be held in conjunction with the 1971 Annual Meeting of the American Society of Animal Science was appointed at the 1969 Annual Meeting of the Society. The Committee members are: W. C. Foote, C. K. Vincent, E. K. Inskeep, H. W. Hawk, P. V. Malven, P. T. Cupps and B. N. Day, Chairman. One of the committee members is also a member of the Physiology Program Committee and this has proved to be of assistance in the coordination of the activities of the two committees. Also, in accordance with a previous recommendation, a Society member from the host institution was appointed to the *** Committee met at Purdue University in 1969 to develop the general format and a tentative budget for the Symposium. The general topic selected for the X Biennial Symposium was “Physiology of Ovulation.” It was estimated that the funds required to conduct the Symposium as planned would not exceed $2,000.
To elucidate the outcome differences between end-stage renal disease (ESRD) patients on chronic dialysis and acute kidney injury (AKI) patients requiring dialysis in the setting of intensive care unit (ICU) is interes...
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To elucidate the outcome differences between end-stage renal disease (ESRD) patients on chronic dialysis and acute kidney injury (AKI) patients requiring dialysis in the setting of intensive care unit (ICU) is interesting and important for nephrologists to assess risk of mortality and make clinical decisions. Most cohort studies addressing this issue reported hospital mortality in the latter group was greater than that of the former group (1-5). The odds ratio of hospital mortality was estimated to be 3.9 with a confidence interval of 3.5-4.4 in a study using meta-analaysis (6). The acute illness severity scores were similar (1, 5) or higher (3, 4) in the AKI patients. Therefore, it is generally presumed that more comorbidities and organ failure in the AKI patients requiring dialysis might be responsible for their grave prognosis. Furthermore, the conclusion remains unchanged even when the population of AKI patients was broadened to include those without dialysis (1, 2, 4). However, hospital mortality of ESRD patients were less favourable compared with matched patients with mild AKI, serum creatinine from 1.2 to 2.1 mg/dL (odds ratio 1.5; confidence interval 1.4-1.6) (6).
To explore guinea pigs as models of chymase biology, we cloned and expressed the guinea pig ortholog of human chymase. In contrast to rats and mice, guinea pigs appear to express just one chymase, which belongs to the...
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To explore guinea pigs as models of chymase biology, we cloned and expressed the guinea pig ortholog of human chymase. In contrast to rats and mice, guinea pigs appear to express just one chymase, which belongs to the alpha clade, like primate chymases and mouse mast cell protease-5. The guinea pig enzyme autolyzes at Leu residues in the loop where human chymase autolyzes at Phe. In addition, guinea pig alpha-chymase selects P1 Leu in a combinatorial peptide library and cleaves Ala-Ala-Pro-Leu-4-nitroanilide but has negligible activity toward substrates with P1 Phe and does not cleave angiotensin I. This contrasts with human chymase, which cleaves after Phe or Tyr, prefers P1 Phe in peptidyl 4-nitroanilides, and avidly hydrolyzes angiotensin I at Phe(8) to generate bioactive angiotensin II. The guinea pig enzyme also is inactivated more effectively by alpha(1)-antichymotrypsin, which features P1 Leu in the reactive loop. Unlike mouse, rat, and hamster alpha-chymases, guinea pig chymase lacks elastase-like preference for P1 Val or Ala. Partially humanized A216G guinea pig chymase acquires human-like P1 Phe- and angiotensin-cleaving capacity. Molecular models suggest that the wild type active site is crowded by the Ala(216) side chain, which potentially blocks access by bulky P1 aromatic residues. On the other hand, the guinea pig pocket is deeper than in Val-selective chymases, explaining the preference for the longer aliphatic side chain of Leu. These findings are evidence that chymase-like peptidase specificity is sensitive to small changes in structure and provide the first example of a vertebrate Leu-selective peptidase.
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