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

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

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
Volume301
Issue number6
DOIs
Publication statusPublished - 2004 Jun 1

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guanylate cyclase
Procambarus clarkii
crayfish
molecular cloning
Crustacea
hormones
active sites
cyclic GMP
Anopheles gambiae
hepatopancreas
carbohydrate metabolism
muscle tissues
cysteine
Drosophila
testes
gills
phosphotransferases (kinases)
amino acid sequences
heart
muscles

All Science Journal Classification (ASJC) codes

  • Animal Science and Zoology

Cite this

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title = "Molecular cloning of a putative membrane form guanylyl cyclase from the crayfish Procambarus clarkii",
abstract = "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.",
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AU - Lee, Chi Ying

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