Detail of "23815-89-6"

Reference

Regional distribution of neuropeptide-metabolizing peptidases in the human brain

Regional distribution of neuropeptide-metabolizing peptidases in the human brain. Martins, Antonio R.; Lachat, J. J.; Del Bel, Elaine A. (Fac. Med., Univ. Sao Paulo, Ribeirao Preto 14.100, Brazil). Neuropept. Psychosom. Processes, Int. Conf. Integr. Neurohumoral Mech., Meeting Date 1982, 175-82. Edited by: Endroczi, Elember. Akad. Kiado: Budapest, Hung. (English) 1983. CODEN: 53HNAO. DOCUMENT TYPE: Conference CA Section: 2 (Mammalian Hormones) Section cross-reference(s): 13 Bradykinin [58-82-2]-degrading kininase [62887-91-6] activity was detd. in various human brain regions and the anterior and posterior pituitary (AP and PP, resp.). The highest activities were found in the nucleus caudatus, putamen, AP, and substantia nigra; these levels were ~2-fold those of the choroid plexus, PP, and hypothalamus. Kininase activity in human brains from consumptive patients were about 25% lower in the 4 highest enzyme-contg. regions. Bradykinin products: bradykinin 1-5 [23815-89-6], bradykinin 6-9 [96158-90-6], bradykinin 1-7 [23815-87-4], Phe-Arg [1238-09-1], Ser-Pro [23827-93-2], arginine [74-79-3], proline [147-85-3], glycine [56-40-6], phenylalanine [63-91-2], and serine [56-45-1] were also detd. in brain regions. These products indicate that enzymes with a specificity similar to endopeptidase A predominate in most of brain regions. The presence of a peptidase similar to endopeptidase B is also suggested for choroid plexus, globus pallidus, and PP. Other peptidases are also discussed.

Assessment of kininases in rheumatic diseases and the effect of therapeutic agents

Assessment of kininases in rheumatic diseases and the effect of therapeutic agents. Sheikh, Iftikhar A.; Kaplan, Allen P. (Dep. Med., SUNY, Stony Brook, NY, USA). Arthritis Rheum., 30(2), 138-45 (English) 1987. CODEN: ARHEAW. ISSN: 0004-3591. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Section cross-reference(s): 2, 14 Bradykinin [58-82-2] is degraded in human plasma by a carboxypeptidase [9031-98-5] to yield desArg9-bradykinin (DBK) [15958-92-6] which is then digested by angiotensin-converting enzyme (ACE) [9015-82-1] to the pentapeptide Arg-Pro-Pro-Gly-Phe [23815-89-6] and the tripeptide Ser-Pro-Phe [23827-76-1]. The rate of kinin degrdn. by each of these enzymes was studied in patients with rheumatoid arthritis (RA) and with systemic lupus erythematosus (SLE), compared with the degrdn. rate in degenerative joint disease and normal subjects. 69-72-7 and 23827-76-1 are also in the experiment. Carboxypeptidase activity was the same in all individuals, but ACE activity was increased in the RA and SLE patients. The effects of aspirin [50-78-2], salicylate [69-72-7], auranofin [34031-32-8], penicillamine [52-67-5], and corticosteroids on kinin metab. were studied, and all of these were marked inhibitors of ACE; however, only penicillamine had any demonstrable inhibition of carboxypeptidase. These observations suggest rapid degrdn. of DBK in patients with untreated RA and SLE, whereas drugs utilized in therapy have the opposite effects. Studies to examine the role of DBK in disease manifestations are in progress. .