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NCUEIR > College of Science > biotech > Periodical Articles > Item 987654321/8994

Please use this identifier to cite or link to this item: http://ir.ncue.edu.tw/ir/handle/987654321/8994

Title:	Molecular Cloning of a Putative Membrane form Guanylyl Cyclase from the Crayfish Procambarus clarkii
Authors:	Liu, H. F.;C. Y. Lai;R. D. Watson;C. Y. Lee
Contributors:	生物系
Date:	2004-06
Issue Date:	2011-05-16T07:39:45Z
Publisher:	Wiley-Blackwell
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.
Relation:	Journal of Experimental Zoology Part A: Comparative Experimental Biology, 301(6):512-520
Appears in Collections:	[biotech] Periodical Articles

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