Molecular cloning of a putative receptor guanylyl cyclase from Y-organs of the blue crab, Callinectes sapidus.
Gen Comp Endocrinol
; 146(3): 329-36, 2006 May 01.
Article
em En
| MEDLINE
| ID: mdl-16426608
ABSTRACT
Crustacean molt-inhibiting hormone (MIH), a polypeptide produced by neurosecretory cells in eyestalk ganglia, suppresses the synthesis of ecdysteroid molting hormones by paired Y-organs. Data from several sources indicate the effects of MIH are mediated, at least in part, by a cGMP second messenger. Based on these and related findings, our working hypothesis is that the MIH receptor is a receptor guanylyl cyclase (rGC). In studies reported here, we used a PCR-based cloning strategy (RT-PCR followed by 5'- and 3'-RACE) to clone from blue crab (Callinectes sapidus) Y-organs a cDNA (CsGC-YO1) encoding a putative rGC. DNA sequence analysis revealed a 3807 base pair open reading frame encoding a 56 residue signal peptide and a 1213 residue rGC. Analysis of the deduced amino acid sequence showed that CsGC-YO1 contains the signature domains characteristic of rGCs, including an extracellular ligand-binding domain, a single transmembrane domain, a kinase-like domain, a dimerization domain, and a cyclase catalytic domain. CsGC-YO1 is most closely related to an rGC from the crayfish, Procambarus claikii (PcGC-M2, 58.4% identity), and rGCs from three insect species (33.1-37.5% identity). Conserved cysteine residues are similarly distributed in the extracellular domains of CsGC-YO1, PcGC-M2, and the three insect rGCs. RT-PCR revealed the CsGC-YO1 transcript is expressed in Y-organs and several other tissues. While other interpretations of the data are possible, our working hypothesis is that the cloned cDNA encodes an MIH receptor.
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Base de dados:
MEDLINE
Assunto principal:
Braquiúros
/
Glândulas Endócrinas
/
Guanilato Ciclase
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article