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Cloning and Expression of a Second Photoreceptor-Specific Membrane Retina Guanylyl Cyclase (RetGC), RetGC-2
Journal article   Open access   Peer reviewed

Cloning and Expression of a Second Photoreceptor-Specific Membrane Retina Guanylyl Cyclase (RetGC), RetGC-2

David G. Lowe, Alexander M. Dizhoor, Kathleen Liu, Qimin Gu, Maribeth Spencer, Richard Laura, Lucy Lu and James B. Hurley
Proceedings of the National Academy of Sciences - PNAS, v 92(12), pp 5535-5539
06 Jun 1995
PMID: 7777544
url
https://europepmc.org/articles/pmc41730View
Published, Version of Record (VoR)Open Access (License Unspecified) Open

Abstract

Amino acids CDNA libraries Cell membranes Complementary DNA Globular star clusters In situ hybridization Photoreceptors Physiological regulation Retina Ungulates
One of the membrane guanylyl cyclases (GCs), RetGC, is expressed predominantly in photoreceptors. No extracellular ligand has been described for RetGC, but it is sensitive to activation by a soluble 24-kDa protein (p24) and is inhibited by Ca2+. This enzyme is, therefore, thought to play a role in resynthesizing cGMP for photoreceptor recovery or adaptation. By screening a human retinal cDNA library at low stringency with the cytoplasmic domains from four cyclases, we cloned cDNAs encoding a membrane CG that is most closely related to RetGC. We have named this GC RetGC-2, and now term the initially described RetGC RetGC-1. By in situ hybridization, mRNA encoding RetGC-2 is found only in the outer nuclear layer and inner segments of photoreceptor cells. By using synthetic peptide antiserum specific for each RetGC subtype, RetGC-2 can be distinguished from RetGC-1 as a slightly smaller protein in immunoblots of bovine rod outer segments. Membrane GC activity of recombinant RetGC-2 expressed in human embryonic kidney 293 cells is stimulated by the activator p24 and is inhibited by Ca2+with an EC50value of 50-100 nM. Our data reveal a previously unappreciated diversity of photoreceptor GCs.

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Biochemistry & Molecular Biology
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