Amylin-induced suppression of ANP secretion through receptors for CGRP1 and salmon calcitonin. 2004

Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
Department of Physiology, Institute for Medical Sciences, Chonbuk National University Medical School, 2-20 Keum-Am-Dong-San, Jeonju 561-180, South Korea.

Amylin cosecretes with insulin from pancreatic beta-cells and shows high sequence homology with CGRP, adrenomedullin, and salmon calcitonin. This study aimed to investigate the effect of amylin on the atrial hemodynamics and ANP release from rat atria and to identify its receptor subtypes. Isolated perfused left atria from either control or streptozotocin-treated rats were paced at 1.3 Hz. The concentration of ANP was measured by radioimmunoassay and the translocation of ECF was measured by [3H]-inulin clearance. Rat amylin increased atrial contractility and suppressed the release of ANP. Rat CGRP showed similar effects but was approximately 300-fold more potent than amylin. Pretreatment with receptor antagonist for CGRP1 [rat alpha-CGRP (8-37)] or salmon calcitonin [acetyl-(Asn30, Tyr32)-calcitonin(8-32), (AC 187)] blocked the suppressive effect of ANP release and the positive inotropic effect by rat amylin. However, receptor antagonists for amylin [amylin (8-37), acetyl-amylin] did not block those effects. Amylin (8-37), acetyl-amylin, or rat alpha-CGRP (8-37) alone accentuated the release of ANP with no changes in atrial contractility. The effect of rat amylin and rat amylin (8-37) on the ANP release was attenuated in streptozotocin-treated rats. We suggest that amylin suppressed ANP release with increased atrial contractility through receptors for CGRP1 and salmon calcitonin and the attenuation of amylin and its antagonist on ANP release from streptozotocin-treated rat atria may be due to the downregulation of amylin receptor.

UI MeSH Term Description Entries
D008297 Male Males
D009320 Atrial Natriuretic Factor A potent natriuretic and vasodilatory peptide or mixture of different-sized low molecular weight PEPTIDES derived from a common precursor and secreted mainly by the HEART ATRIUM. All these peptides share a sequence of about 20 AMINO ACIDS. ANF,ANP,Atrial Natriuretic Peptide,Atrial Natriuretic Peptides,Atriopeptins,Auriculin,Natriuretic Peptides, Atrial,ANF (1-126),ANF (1-28),ANF (99-126),ANF Precursors,ANP (1-126),ANP (1-28),ANP Prohormone (99-126),ANP-(99-126),Atrial Natriuretic Factor (1-126),Atrial Natriuretic Factor (1-28),Atrial Natriuretic Factor (99-126),Atrial Natriuretic Factor Precursors,Atrial Natriuretic Factor Prohormone,Atrial Natriuretic Peptide (1-126),Atrial Pronatriodilatin,Atriopeptigen,Atriopeptin (1-28),Atriopeptin (99-126),Atriopeptin 126,Atriopeptin Prohormone (1-126),Cardiodilatin (99-126),Cardiodilatin Precursor,Cardionatrin I,Cardionatrin IV,Prepro-ANP,Prepro-CDD-ANF,Prepro-Cardiodilatin-Atrial Natriuretic Factor,Pro-ANF,ProANF,Proatrial Natriuretic Factor,Pronatriodilatin,alpha ANP,alpha-ANP Dimer,alpha-Atrial Natriuretic Peptide,beta-ANP,beta-Atrial Natriuretic Peptide,gamma ANP (99-126),gamma-Atrial Natriuretic Peptide,Natriuretic Peptide, Atrial,Peptide, Atrial Natriuretic,Peptides, Atrial Natriuretic,Prepro ANP,Prepro CDD ANF,Prepro Cardiodilatin Atrial Natriuretic Factor,Pro ANF,alpha ANP Dimer,alpha Atrial Natriuretic Peptide,beta ANP,beta Atrial Natriuretic Peptide,gamma Atrial Natriuretic Peptide
D011674 Pulse The rhythmical expansion and contraction of an ARTERY produced by waves of pressure caused by the ejection of BLOOD from the left ventricle of the HEART as it contracts. Pulses
D001794 Blood Pressure PRESSURE of the BLOOD on the ARTERIES and other BLOOD VESSELS. Systolic Pressure,Diastolic Pressure,Pulse Pressure,Pressure, Blood,Pressure, Diastolic,Pressure, Pulse,Pressure, Systolic,Pressures, Systolic
D002116 Calcitonin A peptide hormone that lowers calcium concentration in the blood. In humans, it is released by thyroid cells and acts to decrease the formation and absorptive activity of osteoclasts. Its role in regulating plasma calcium is much greater in children and in certain diseases than in normal adults. Thyrocalcitonin,Calcitonin(1-32),Calcitrin,Ciba 47175-BA,Eel Calcitonin,Calcitonin, Eel,Ciba 47175 BA,Ciba 47175BA
D003921 Diabetes Mellitus, Experimental Diabetes mellitus induced experimentally by administration of various diabetogenic agents or by PANCREATECTOMY. Alloxan Diabetes,Streptozocin Diabetes,Streptozotocin Diabetes,Experimental Diabetes Mellitus,Diabete, Streptozocin,Diabetes, Alloxan,Diabetes, Streptozocin,Diabetes, Streptozotocin,Streptozocin Diabete
D000077221 Calcitonin Gene-Related Peptide Receptor Antagonists Pharmacologic agents that block NOCICEPTIVE PAIN signaling from CALCITONIN GENE-RELATED PEPTIDE RECEPTORS. They may be useful for the treatment of pain associated with MIGRAINE DISORDERS and OSTEOARTHRITIS. CGRP Receptor Antagonist,CGRP-R Inhibitor,CGRP-R Inhibitors,Calcitonin Gene-Related Peptide Receptor Antagonist,GEPANT,CGRP Receptor Antagonists,GEPANTS,Antagonist, CGRP Receptor,Antagonists, CGRP Receptor,CGRP R Inhibitor,CGRP R Inhibitors,Calcitonin Gene Related Peptide Receptor Antagonist,Calcitonin Gene Related Peptide Receptor Antagonists,Inhibitor, CGRP-R,Inhibitors, CGRP-R,Receptor Antagonist, CGRP,Receptor Antagonists, CGRP
D000682 Amyloid A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease. Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D015536 Down-Regulation A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins. Receptor Down-Regulation,Down-Regulation (Physiology),Downregulation,Down Regulation,Down-Regulation, Receptor

Related Publications

Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
February 2000, Peptides,
Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
January 2022, Frontiers in pharmacology,
Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
January 1985, Digestion,
Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
September 1998, Neuroendocrinology,
Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
July 1995, Canadian journal of physiology and pharmacology,
Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
June 1994, The Journal of pharmacology and experimental therapeutics,
Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
October 2000, Analytical biochemistry,
Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
December 1995, Trends in pharmacological sciences,
Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
June 2007, Physiology & behavior,
Feng Lian Piao, and Chunhua Cao, and Jeong Hee Han, and Sung Zoo Kim, and Kyung Woo Cho, and Suhn Hee Kim
June 2011, Peptides,
Copied contents to your clipboard!