Detail of "89468-62-2"

Reference

Characterization of receptors for VIP on pancreatic acinar cell plasma membranes using covalent cross-linking

Characterization of receptors for VIP on pancreatic acinar cell plasma membranes using covalent cross-linking. McArthur, Katherine E.; Wood, Catherine L.; O'Dorisio, M. Sue; Zhou, Zhi Chao; Gardner, Jerry D.; Jensen, Robert T. (Digest. Dis. Branch, Natl. Inst. Health, Bethesda, MD 20892, USA). Am. J. Physiol., 252(3, Pt. 1), G404-G412 (English) 1987. CODEN: AJPHAP. ISSN: 0002-9513. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) VIP [37221-79-7] receptors on guinea pig pancreatic acini differ from those on all other tissues in contg. a high-affinity VIP receptor and a low-affinity VIP receptor that has a high affinity for secretin [1393-25-5]. To characterize the mol. components of these receptors, 125I-labeled VIP (125I-VIP) was covalently crosslinked to these receptors by 4 different crosslinking agents: disuccinimidyl suberate, ethylene glycol bis(succinimidyl succinate), dithiobis(succinimidyl propionate), and m-maleimidobenzoyl N-hydroxysuccinimide ester. Anal. by SDS-PAGE demonstrated a single major polypeptide band of mol. wt. (Mr) 45,000 and a minor polypeptide band of Mr 30,000 were crosslinked to 125I-VIP. Covalent crosslinking only occurred when a crosslinking agent was added, was inhibited by GTP [86-01-1], was inhibited by VIP receptor agonists or antagonists that interact with VIP receptors, and not by other pancreatic secretagogues that interact with different receptors. For inhibiting both crosslinking and binding of 125I-VIP to the major polypeptide Mr 45,000 and the minor polypeptide Mr 30,000 components, the relative potencies were VIP > helodermin [89468-62-2] > rat growth hormone-releasing factor [9034-39-3] > peptide histidine isoleucine > secretin [1393-25-5]. The apparent mol. wt. of the crosslinked polypeptides were unchanged by dithiothreitol. Thus the high-affinity VIP receptor on pancreatic acinar cell membranes consists of a single major polypeptide of Mr 45,000, and this polypeptide is not a subunit of a larger disulfide-linked structure. Furthermore, either the low-affinity VIP/secretin-preferring receptor was not covalently crosslinked under the exptl.In this experiment, several chemicals are used like 9034-39-3 and 37221-79-7 conditions or it consists of a major polypeptide with the same mol. wt. as the high-affinity VIP receptor. .

Receptors involved in helodermin action on rat pancreatic acini

Receptors involved in helodermin action on rat pancreatic acini. Dehaye, Jean Paul; Winand, Jacques; Damien, Catherine; Gomez, Francoise; Poloczek, Piotr; Robberecht, Patrick; Vandermeers, Andre; Vandermeers-Piret, Marie Claire; Stievenart, Michel; Christophe, Jean (Med. Sch., Univ. Libre Bruxelles, Brussels B-1000, Belg.). Am. J. Physiol., 251(5, Pt. 1), G602-G610 (English) 1986. CODEN: AJPHAP. ISSN: 0002-9513. DOCUMENT TYPE: Journal CA Section: 4 (Toxicology) Helodermin [89468-62-2] is a new peptide isolated from the venom of Heloderma suspectum. Its effects on rat pancreatic acini were compared with those of secretin [1393-25-5] and vasoactive intestinal peptide (VIP) [37221-79-7]. Four classes of receptors with decreasing affinity for secretin (S1, S2, S3, and S4) were 1st delineated. Occupancy of S1 and S2 by secretin was responsible for a biphasic cAMP [60-92-4] response. S3 was VIP preferring so that the VIP-induced increase in cAMP could be inhibited by VIP(10-28). S2 and S3 allowed cAMP elevation, protein phosphorylation, weak secretory effects, and potentiation of cholecystokinin octapeptide (CCK-8) [25126-32-3] when occupied by secretin and VIP, resp. A more efficient exocytosis was obsd. with secretin interacting with low-affinity receptors S4. Helodermin increased cAMP levels 14-fold, this increase being inhibited by VIP (10-28). Low concns. of helodermin stimulated amylase [9000-92-4] secretion 2-fold and potentiated secretion by CCK-8. High concns. of helodermin stimulated secretin receptors with a weak selectivity. At low concn., helodermin stimulated cAMP elevation, protein phosphorylation, amylase release, and potentiation of CCK-8 through S3, whereas at high concn. it stimulated secretion via S4.