Detail of "3483-82-7"

Reference

Chymotrypsin substrate analogs inhibit endocytosis of insulin and insulin receptors in adipocytes

Chymotrypsin substrate analogs inhibit endocytosis of insulin and insulin receptors in adipocytes. Jochen, Albert L.; Berhanu, Paulos (Health Sci. Cent., Univ. Colorado, Denver, CO 80262, USA). J. Cell Biol. 58690-81-6 and 9004-10-8 are cas registry numbers. These chemicals are also mentioned in this article., 103(5, Pt. 1), 1807-16 (English) 1986. CODEN: JCLBA3. ISSN: 0021-9525. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) To explore the possible role of proteolytic step(s) in receptor-mediated endocytosis of insulin [9004-10-8], the effects of inhibitors of various classes of proteases on the internalization process were studied in isolated rat adipocytes. Intracellular accumulation of receptor-bound 125I-insulin at 37° was quantitated after rapidly dissocg. surface-bound insulin with an acidic buffer (pH 3.0). Of the 23 protease inhibitors tested, only chymotrypsin [9004-07-3] substrate analogs inhibited insulin internalization. Internalization was decreased 62-90% by 5 different chymotrypsin substrate analogs: N-acetyl-Tyr Et ester [840-97-1], N-acetyl-Phe Et ester [2361-96-8], N-acetyl-Tyr Et ester [2382-80-1], benzoyl-Tyr Et ester [3483-82-7], and benzoyl-Tyr amide [58690-81-6]. The effect of the substrate analogs in inhibiting insulin internalization was dose-dependent, reversible, and required the full structural complement of a chymotrypsin substrate analog. Cell surface receptor no. was unaltered at 12°. However, concomitant with their inhibition of insulin internalization at 37°, the chymotrypsin substrate analogs caused a marked increase (160-380%) in surface-bound insulin, indicating trapping of insulin-receptor complexes on the cell surface. Addnl., 1 mM N-acetyl-Tyr Et ester decreased overall insulin degrdn. by 15-20% and also prevented the chloroquine-mediated increase in intracellular insulin, further indicating that surface-bound insulin was prevented from reaching intracellular chloroquine-sensitive degrdn. sites. The internalization of insulin receptors that were photoaffinity labeled on the cell surface with B2(2-nitro-4-azidophenylacetyl)-des-PheB1-insulin was also inhibited 70-90% by the 5 chymotrypsin substrate analogs, as detd. by the effects of the analogs on the accumulation of trypsin-insensitive (intracellular) 440 kilodalton intact labeled receptors. Thus, chymotrypsin substrate analogs efficiently inhibit the internalization of insulin and insulin receptors in adipocytes and implicate a possible role for endogenous chymotrypsin-like enzyme(s) or related substances in receptor-mediated endocytosis of insulin. .

Hydrolysis of N-benzoyl-L-tyrosine ethyl ester anchored in CD by a-chymotrypsin and subtilisin

Hydrolysis of N-benzoyl-L-tyrosine ethyl ester anchored in CD by a-chymotrypsin and subtilisin. Prabhu, K. Sandeep; Ramadoss, C. S. (Division of Biological Sciences, Vittal Mallya Scientific Research Foundation, Bangalore 560 004, India). 9014-01-1 and 3483-82-7 are cas registry numbers. These chemicals are also mentioned in this article. Proceedings of the International Symposium on Cyclodextrins, 8th, Budapest, Mar. 31-Apr. 2, 1996, 281-284. Edited by: Szejtli, J.; Szente, L. Kluwer: Dordrecht, Neth. (English) 1996. CODEN: 64CDAL. DOCUMENT TYPE: Conference CA Section: 7 (Enzymes) N-Benzoyl-L-tyrosine Et ester (BTEE), a water insol. substrate, was rendered sol. upon complexation with b-cyclodextrin (or its Me deriv.) and but not with g-CD. Kinetics of the hydrolysis of such CD anchored BTEE by subtilisin Carlsberg showed a 2 to 4 fold increase in both kcat and Km values, over the methanol solubilized substrate. Whereas, a-chymotrypsin hydrolyzed the CD anchored BTEE with only a marginally higher reaction rate than the methanol solubilized BTEE. .