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Please use this identifier to cite or link to this item: http://ir.ncue.edu.tw/ir/handle/987654321/12232

Title: Molecular Cloning of a Putative Membrane Form Guanylyl Cyclase From the Crayfish Procambarus Clarkii
Authors: Liu, Hui-Fen;Lai, Chi-Yung;Watson, R. Douglas;Lee, Chi-Ying
Contributors: 生物學系
Date: 2004-06
Issue Date: 2012-07-03T04:02:48Z
Publisher: Wiley-Liss, Inc.
Abstract: Available data indicate that crustacean hyperglycemic hormone (CHH) stimulates
membrane-bound guanylyl cyclase (GC), producing cyclic guanosine 30,50–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. J. Exp. Zool.
Relation: Journal of Experimental Zoology, 301A(6): 512-520
Appears in Collections:[生物學系] 期刊論文

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