cDNA structure and in situ localization of the Aplysia californica pro-hormone convertase PC2.
The complete cDNA structure of the Aplysia californica pro-protein and pro-hormone convertase PC2 (aPC2) was obtained from a cDNA library of the nervous system. The deduced amino acid sequence revealed that aPC2 exhibits an 85%, 61% and 62% sequence identity to the Lymnaea stagnalis, Xenopus laevis and mouse PC2 homologues, respectively. The deduced stagnalis, Xenopus laevis and mouse PC2 homologues, respectively. The deduced primary sequence suggested a protein of 653 amino acids which includes a 27- and 88-amino acid signal peptide and pro-segment. The signal peptide and the C-terminal segments are the least conserved regions. On Northern blots of nervous system we detected a transcript of 6.8 kb. The in situ hybridization histochemistry on the abdominal ganglion revealed intense labeling of the bag cells. Large peptidergic cells and clusters of sensory and motor neurons also contained high levels of aPC2 mRNA.
Ouimet
T
T
Laboratory of Neurobiology, Clinical Research Institute of Montreal, Que., Canada.
Mammarbachi
A
A
Cloutier
T
T
Seidah
N G
NG
Castellucci
V F
VF
D000595:Amino Acid Sequence; D000818:Animals; D001048:Aplysia / Q000201:enzymology*; D001483:Base Sequence; D004247:DNA / Q000235:genetics*; D017403:In Situ Hybridization; D008969:Molecular Sequence Data; D045706:Proprotein Convertase 2; D012333:RNA, Messenger / Q000378:metabolism; D013381:Subtilisins / Q000235:genetics* / Q000378:metabolism
D012333:RNA, Messenger; D004247:DNA; D013381:Subtilisins; D045706:Proprotein Convertase 2