作者: Fran�oise Gangnon , Jean-Michel Danger , Sylvie Jegou , Didier Vieau , Nabil G. Seidah
DOI: 10.1002/(SICI)1096-9861(19990308)405:2<160::AID-CNE2>3.0.CO;2-Y
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摘要: Prohormone convertases (PCs) are calcium-dependent serine endoproteases of the subtilisin/kexin family that play a key role in posttranslational processing precursors for biologically active peptides. In this study, we have characterized cDNA encoding PC1 European green frog Rana ridibunda. A brain library was screened by using heterologous probe at low stringency, and 2.3-kb clone isolated. This encodes 736-residue protein with 26-amino-acid signal peptide. Comparative structural analysis revealed exhibits high degree amino acid identity its mammalian counterparts, particular subtilisin-like catalytic domain. Northern blot resolved two major transcripts 3.0 kb 5.0 were expressed differentially pituitary. situ hybridization studies showed that, brain, highest densities mRNA present amygdala, hypothalamus, anterior preoptic area. High concentrations also found pars distalis intermedia pituitary, whereas nervosa devoid signal. The wide distribution pituitary suggests frog, is involved number hormone neuropeptide precursors. J. Comp. Neurol. 405:160–172, 1999. © 1999 Wiley-Liss, Inc.