Molecular cloning of a putative membrane form guanylyl cyclase from the crayfish Procambarus clarkii.
J Exp Zool A Comp Exp Biol
; 301(6): 512-20, 2004 Jun 01.
Article
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| MEDLINE
| ID: mdl-15181645
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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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
ARN Mensajero
/
Astacoidea
/
Guanilato Ciclasa
/
Proteínas de la Membrana
Límite:
Animals
Idioma:
En
Revista:
J Exp Zool A Comp Exp Biol
Año:
2004
Tipo del documento:
Article
País de afiliación:
China