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 language | English |
|---|---|
| Pages (from-to) | 512-520 |
| Number of pages | 9 |
| Journal | Journal of Experimental Zoology Part A: Comparative Experimental Biology |
| Volume | 301 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2004 Jun 1 |
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All Science Journal Classification (ASJC) codes
- Animal Science and Zoology
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Molecular cloning of a putative membrane form guanylyl cyclase from the crayfish Procambarus clarkii. / Liu, Hui Fen; Lai, Chi Yung; Watson, R. Douglas; Lee, Chi Ying.
In: Journal of Experimental Zoology Part A: Comparative Experimental Biology, Vol. 301, No. 6, 01.06.2004, p. 512-520.Research output: Contribution to journal › Article
TY - JOUR
T1 - Molecular cloning of a putative membrane form guanylyl cyclase from the crayfish Procambarus clarkii
AU - Liu, Hui Fen
AU - Lai, Chi Yung
AU - Watson, R. Douglas
AU - Lee, Chi Ying
PY - 2004/6/1
Y1 - 2004/6/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=3042768002&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=3042768002&partnerID=8YFLogxK
U2 - 10.1002/jez.a.75
DO - 10.1002/jez.a.75
M3 - Article
C2 - 15181645
AN - SCOPUS:3042768002
VL - 301
SP - 512
EP - 520
JO - Journal of Experimental Zoology Part A: Comparative Experimental Biology
JF - Journal of Experimental Zoology Part A: Comparative Experimental Biology
SN - 0022-104X
IS - 6
ER -