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Characterization of a membrane glycoprotein having pharmacological and biochemical-properties of an at2 angiotensin-ii receptor from human myometrium

Academic Article
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Overview

authors

  • Lazard, D.
  • Villageois, P.
  • Briendsutren, M. M.
  • Cavaille, F.
  • Bottari, S.
  • Strosberg, Donny
  • Nahmias, C.

publication date

  • March 1994

journal

  • European Journal of Biochemistry  Journal

abstract

  • The angiotensin II receptors of human myometrial tissue were characterized using ligand binding, cross-linking with radioactive label, detergent solubilization and partial purification by lectin-affinity chromatography. Human myometrial membrane preparations contained variable amount (5-650 fmol/mg protein) of high affinity (Kd = 44-65 pM) binding sites for 125I-CGP42112, a ligand specific for the AT2 subtype of angiotensin II receptors. Competition studies with AT1-specific and AT2-specific compounds indicated that angiotensin II receptors on these membranes were exclusively of the AT2 subtype. The binding sites for 125I-CGP42112 were efficiently solubilized by the detergent Chaps, albeit with a marked decrease in affinity (Kd = 1.2 nM). The proteins in the myometrial membrane preparation were cross-linked to 125I-[Sar1, Ile8]angiotensin II (Sarile) with disuccinimidyl suberate. When low concentrations of cross-linker were used, a single radiolabelled band of about 66-70 kDa was revealed on SDS/PAGE. At higher concentrations additional bands of about 105-120 kDa and 200 kDa were labelled. The 66-70-kDa and 105-120-kDa bands were separated by electroelution of SDS/PAGE gel slices and submitted to trypsin cleavage. The tryptic-peptide maps were identical for both products, suggesting that the additional bands are homodimers and trimers of the labelled polypeptide. The Chaps-solubilized receptor was retained on wheat-germ-agglutinin-Sepharose and specifically eluted by the competing sugar triacetylchitotriose, leading to a fivefold purification factor. Treatment of the 125I-Sarile-labelled protein with N-glycanase caused a shift in its apparent molecular mass on SDS/PAGE from 66-70 kDa to 33 kDa.

subject areas

  • 1-Sarcosine-8-Isoleucine Angiotensin II
  • Cell Membrane
  • Cross-Linking Reagents
  • Female
  • Humans
  • Membrane Glycoproteins
  • Molecular Weight
  • Myometrium
  • Oligopeptides
  • Receptors, Angiotensin
  • Solubility
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Identity

International Standard Serial Number (ISSN)

  • 0014-2956

Digital Object Identifier (DOI)

  • 10.1111/j.1432-1033.1994.tb18695.x

PubMed ID

  • 8143746
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Additional Document Info

start page

  • 919

end page

  • 926

volume

  • 220

issue

  • 3

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