Molecular cloning of a putative membrane form guanylyl cyclase from the crayfish Procambarus clarkii

Hui Fen Liu, Chi Yung Lai, R. Douglas Watson, Chi Ying Lee

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19 Citations (Scopus)


Available data indicate that crustacean hyperglycemic hormone (CHH) stimulates membrane-bound guanylyl cyclase (GC), producing cyclic guanosine 3′,5′-monophosphate, which in turn mediates the effect of CHH on carbohydrate metabolism. In the present study, we report the cloning of a cDNA (PcGC-M2) encoding a putative membrane form GC from the muscle of the crayfish, Procambarus clarkii. Analysis of the deduced amino acid sequence shows that PcGC-M2 contains the signature domains characteristic of membrane form GCs, including an extracellular ligand-binding domain, a single transmembrane, and intracellular kinase-like and cyclase catalytic domains. In addition, a C-terminal domain of 247 residues is present following the cyclase catalytic domain. PcGC-M2 is most closely related (33% identity) to a Drosophila membrane form GC (DrGC-1), and an Anopheles gambiae membrane form GC (AgaGC); the three GCs also share a similar distribution pattern of conserved cysteine residues in the extracellular domain. The PcGC-M2 transcript is expressed in several CHH target tissues, including muscle, hepatopancreas, heart, ovary, testis, and gill, suggesting that PcGC-M2 may participate in the signaling cascade activated by CHH.

Original languageEnglish
Pages (from-to)512-520
Number of pages9
JournalJournal of Experimental Zoology Part A: Comparative Experimental Biology
Issue number6
Publication statusPublished - 2004 Jun 1

All Science Journal Classification (ASJC) codes

  • Animal Science and Zoology

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