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Cloning and Functional Characterization of PACAP‐Specific Receptors in Zebrafish
Author(s) -
WEI Y.,
MARTIN S. C.,
HEINRICH G.,
MOJSOV S.
Publication year - 1998
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1998.tb11161.x
Subject(s) - zebrafish , receptor , biology , microbiology and biotechnology , peptide sequence , biochemistry , gene
A bstract : Two PACAP receptors were isolated from total zebrafish cDNA library prepared from 6‐day old fish by a homology‐based cloning strategy. The two zebrafish PACAP receptors have the same topology as the one found in other members of this class of seven membrane‐spanning G‐protein‐coupled receptors. Each of the two zebrafish PACAP receptors shares about 70% sequence identity at the amino acid level with the human PACAP‐type 1 receptor, and about 50% amino acid identity with PACAP/VIP R‐1 and PACAP/VIP R‐2 receptors. One of these zebrafish receptors contains the hop2 configuration found in the human and rat PACAP‐type 1 receptors. On the basis of these structural characteristics the zebrafish PACAP receptors were classified as PACAP‐type 1 and PACAP‐type 2 receptors. In competitive binding experiments zebrafish PACAP‐type 1 and PACAP‐type 2 receptors showed similar binding specificity for zebrafish and human PACAP‐38 and PACAP‐27. Furthermore, the specificity of PACAP‐type 1 and PACAP‐type 2 receptors for zebrafish and human PACAPs is about 1,000‐fold higher than for human VIP. These results demonstrate that zebrafish PACAP‐type 1 receptor is a structural and pharmacological homolog of the mammalian PACAP‐type 1 receptor. Additional pharmacological characterization is needed in order to classify the zebrafish PACAP‐type 2 receptor.