Characterization of binding sites for amylin, calcitonin, and CGRP in primate kidney

Research output: Contribution to journalArticleResearchpeer-review

24 Citations (Scopus)

Abstract

Analysis of receptor distributions for 125I-labeled amylin, 125I- labeled calcitonin, and 125I-labeled calcitonin gene-related peptide (CGRP) in Macaca fascicularis kidney by in vitro autoradiography revealed distinct patterns of binding for each peptide. 125I-rat amylin bound primarily to the cortex, being associated with the distal tubule, including apparent binding to the juxtaglomerular apparatus. 125I-salmon calcitonin displayed high-density binding in the cortex with low-density binding to the medulla. Emulsion autoradiography indicated that binding was associated with both distal tubule and thick ascending limb of the loop of Henle. Intense binding was also found often over juxtaglomerular apparatus. 125I-rat CGRP-α exhibited low- to moderate density binding to the inner medulla/papilla with high-density binding over small-, medium-, and large- caliber arteries. Weak binding to the glomerulus was also seen, but no binding was associated with cortical tubules. Competition binding studies, performed with each of the radioligands, revealed peptide specificity profiles for CGRP and calcitonin receptors that were similar to those described in rat. However, the monkey amylin receptors differed from those in rat, exhibiting relatively higher affinity for calcitonin peptides but reduced affinity for CGRP peptides. These studies suggest potential roles for amylin, calcitonin, and CGRP in primate renal function.

Original languageEnglish
Pages (from-to)F51-F62
JournalAmerican Journal of Physiology - Renal Physiology
Volume274
Issue number1 43-1
Publication statusPublished - 1 Jan 1998
Externally publishedYes

Keywords

  • Autoradiography
  • Calcitonin gene-related peptide
  • G protein-coupled receptor

Cite this

@article{3ec3e256931246cea932074df9573b54,
title = "Characterization of binding sites for amylin, calcitonin, and CGRP in primate kidney",
abstract = "Analysis of receptor distributions for 125I-labeled amylin, 125I- labeled calcitonin, and 125I-labeled calcitonin gene-related peptide (CGRP) in Macaca fascicularis kidney by in vitro autoradiography revealed distinct patterns of binding for each peptide. 125I-rat amylin bound primarily to the cortex, being associated with the distal tubule, including apparent binding to the juxtaglomerular apparatus. 125I-salmon calcitonin displayed high-density binding in the cortex with low-density binding to the medulla. Emulsion autoradiography indicated that binding was associated with both distal tubule and thick ascending limb of the loop of Henle. Intense binding was also found often over juxtaglomerular apparatus. 125I-rat CGRP-α exhibited low- to moderate density binding to the inner medulla/papilla with high-density binding over small-, medium-, and large- caliber arteries. Weak binding to the glomerulus was also seen, but no binding was associated with cortical tubules. Competition binding studies, performed with each of the radioligands, revealed peptide specificity profiles for CGRP and calcitonin receptors that were similar to those described in rat. However, the monkey amylin receptors differed from those in rat, exhibiting relatively higher affinity for calcitonin peptides but reduced affinity for CGRP peptides. These studies suggest potential roles for amylin, calcitonin, and CGRP in primate renal function.",
keywords = "Autoradiography, Calcitonin gene-related peptide, G protein-coupled receptor",
author = "Chai, {Siew Yeen} and George Christopoulos and Cooper, {Mark E.} and Sexton, {Patrick M.}",
year = "1998",
month = "1",
day = "1",
language = "English",
volume = "274",
pages = "F51--F62",
journal = "American Journal of Physiology - Renal Physiology",
issn = "1522-1466",
publisher = "American Physiological Society",
number = "1 43-1",

}

Characterization of binding sites for amylin, calcitonin, and CGRP in primate kidney. / Chai, Siew Yeen; Christopoulos, George; Cooper, Mark E.; Sexton, Patrick M.

In: American Journal of Physiology - Renal Physiology, Vol. 274, No. 1 43-1, 01.01.1998, p. F51-F62.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Characterization of binding sites for amylin, calcitonin, and CGRP in primate kidney

AU - Chai, Siew Yeen

AU - Christopoulos, George

AU - Cooper, Mark E.

AU - Sexton, Patrick M.

PY - 1998/1/1

Y1 - 1998/1/1

N2 - Analysis of receptor distributions for 125I-labeled amylin, 125I- labeled calcitonin, and 125I-labeled calcitonin gene-related peptide (CGRP) in Macaca fascicularis kidney by in vitro autoradiography revealed distinct patterns of binding for each peptide. 125I-rat amylin bound primarily to the cortex, being associated with the distal tubule, including apparent binding to the juxtaglomerular apparatus. 125I-salmon calcitonin displayed high-density binding in the cortex with low-density binding to the medulla. Emulsion autoradiography indicated that binding was associated with both distal tubule and thick ascending limb of the loop of Henle. Intense binding was also found often over juxtaglomerular apparatus. 125I-rat CGRP-α exhibited low- to moderate density binding to the inner medulla/papilla with high-density binding over small-, medium-, and large- caliber arteries. Weak binding to the glomerulus was also seen, but no binding was associated with cortical tubules. Competition binding studies, performed with each of the radioligands, revealed peptide specificity profiles for CGRP and calcitonin receptors that were similar to those described in rat. However, the monkey amylin receptors differed from those in rat, exhibiting relatively higher affinity for calcitonin peptides but reduced affinity for CGRP peptides. These studies suggest potential roles for amylin, calcitonin, and CGRP in primate renal function.

AB - Analysis of receptor distributions for 125I-labeled amylin, 125I- labeled calcitonin, and 125I-labeled calcitonin gene-related peptide (CGRP) in Macaca fascicularis kidney by in vitro autoradiography revealed distinct patterns of binding for each peptide. 125I-rat amylin bound primarily to the cortex, being associated with the distal tubule, including apparent binding to the juxtaglomerular apparatus. 125I-salmon calcitonin displayed high-density binding in the cortex with low-density binding to the medulla. Emulsion autoradiography indicated that binding was associated with both distal tubule and thick ascending limb of the loop of Henle. Intense binding was also found often over juxtaglomerular apparatus. 125I-rat CGRP-α exhibited low- to moderate density binding to the inner medulla/papilla with high-density binding over small-, medium-, and large- caliber arteries. Weak binding to the glomerulus was also seen, but no binding was associated with cortical tubules. Competition binding studies, performed with each of the radioligands, revealed peptide specificity profiles for CGRP and calcitonin receptors that were similar to those described in rat. However, the monkey amylin receptors differed from those in rat, exhibiting relatively higher affinity for calcitonin peptides but reduced affinity for CGRP peptides. These studies suggest potential roles for amylin, calcitonin, and CGRP in primate renal function.

KW - Autoradiography

KW - Calcitonin gene-related peptide

KW - G protein-coupled receptor

UR - http://www.scopus.com/inward/record.url?scp=0003950195&partnerID=8YFLogxK

M3 - Article

C2 - 9458823

AN - SCOPUS:0003950195

VL - 274

SP - F51-F62

JO - American Journal of Physiology - Renal Physiology

JF - American Journal of Physiology - Renal Physiology

SN - 1522-1466

IS - 1 43-1

ER -