Natriuretic peptide receptors are expressed during cerebral growth in the fetal rat.

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  • Author(s): Brown J;Brown J; Zuo Z
  • Source:
    The American journal of physiology [Am J Physiol] 1995 Aug; Vol. 269 (2 Pt 2), pp. R261-73.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: American Physiological Society Country of Publication: United States NLM ID: 0370511 Publication Model: Print Cited Medium: Print ISSN: 0002-9513 (Print) Linking ISSN: 00029513 NLM ISO Abbreviation: Am J Physiol Subsets: MEDLINE
    • Publication Information:
      Publication: Bethesda, MD : American Physiological Society
      Original Publication: Washington [etc.] American Physiological Society.
    • Subject Terms:
      Brain/*embryology ; Fetus/*physiology ; Guanylate Cyclase/*metabolism ; Receptors, Atrial Natriuretic Factor/*metabolism; Animals ; Autoradiography ; Chromatography, Gel ; Electrophoresis, Polyacrylamide Gel ; Embryonic and Fetal Development ; Nerve Tissue Proteins/metabolism ; Rats/embryology ; Rats, Wistar ; Telencephalon/embryology
    • Abstract:
      Autoradiography of frozen sections of fetal rat brain shows that receptor-like binding sites for atrial and C-type natriuretic peptides (ANP and CNP) occur in the generative juxtaventricular zone of the telencephalon after the 12th embryonic day (E12). These sites avidly bind both ANP and CNP. They thus resemble the cloned NPR-C type of natriuretic peptide receptor. Covalent cross-linking of 3-[125I]iodo-O-tyrosyl CNP-(1-22) and 3-[125I]iodo-28-tyrosyl rat ANP-(1-28) to membrane proteins from E16 telencephala labels a single protein band on reducing sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. The protein has high affinities for ANP and CNP and a molecular mass of 60-70 kDa under reducing conditions, consistent with reduced NPR-C. However, because the telencephalic protein has unusual physicochemical properties in SDS under nonreducing conditions it was not possible to assess whether this protein can form disulfide-bridged dimers like NPR-C. CNP-(1-22) was a full agonist and ANP-(1-28) was a partial agonist of guanosine 3',5'-cyclic monophosphate (cGMP) production by E16 telencephalon. C-ANP, a synthetic ligand of NPR-C, antagonized CNP-(1-22)-mediated cGMP production. The results imply that either the NPR-C-like telencephalic receptor modulates the level of cGMP or a guanylate cyclase-coupled receptor, such as the 120-kDa B-type NPR, for which CNP-(1-22) is a full agonist, is present at levels insufficient to be detected by autoradiography or protein labeling.(ABSTRACT TRUNCATED AT 250 WORDS)
    • Accession Number:
      0 (Nerve Tissue Proteins)
      EC 4.6.1.2 (Guanylate Cyclase)
      EC 4.6.1.2 (Receptors, Atrial Natriuretic Factor)
      EC 4.6.1.2 (atrial natriuretic factor receptor C)
    • Publication Date:
      Date Created: 19950801 Date Completed: 19950922 Latest Revision: 20171213
    • Publication Date:
      20231215
    • Accession Number:
      10.1152/ajpregu.1995.269.2.R261
    • Accession Number:
      7653646