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Your search keyword '"Seidah, N.G."' showing total 228 results
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228 results on '"Seidah, N.G."'

6. cDNA structure, tissue distribution, and chromosomal localization of rat PC7, a novel mammalian proprotein convertase closest to yeast kexin-like proteinases

Author

Seidah, N.G., Hamelin, J., Mamarbachi M., Dong, W., Tadros, T., Mbikay, M., Chretien, M., and Day, R.

Subjects
In situ hybridization -- Research, Rats -- Genetic aspects, Aspartic proteinases -- Research, Science and technology
Abstract

By using reverse transcription-coupled PCR on rat anterior pituitary RNA, we isolated a 285-bp cDNA coding for a novel subtilisin/kexin-like protein convertase (PC), called rat (r) PC7. By screening rat spleen and PC12 cell Agtll cDNA libraries, we obtained a composite 3.5-kb full-length cDNA sequence of rPC7. The open reading frame codes for a prepro-PC with a 36-amino acid signal peptide, a 104-amino acid prosegment ending with a cleavable RAKR sequence, and a 747-amino acid type I membrane-bound glycoprotein, representing the mature form of this serine proteinase. Phylogenetic analysis suggests that PC7 represents the most divergent enzyme of the mammalian convertase family and that it is the closest member to the yeast convertases krp and kexin. Northern blot analyses demonstrated a widespread expression with the richest source of rPC7 mRNA being the colon and lymphoid-associated tissues. In situ hybridization revealed a distinctive tissue distribution that sometimes overlaps with that of furin, suggesting that PC7 has widespread proteolytic functions. The gene for PC7 (Pcsk7) was mapped to mouse chromosome 9 by linkage analysis of an interspecific backcross DNA panel.

Published
1996

7. cDNA structure of the mouse and rat subtilisin/kexin-like PC5: a candidate proprotein convertase expressed in endocrine and nonendocrine cells

Author

Lusson, J., Vieau, D., Hamelin, J., Day, R., Chretien, M., and Seidah, N.G.

Subjects
Drosophila -- Analysis, Science and technology
Abstract

PC5, a subtilisn/kexin-like protein convertase (PC) in mouse and rat tissues, was discovered by studying the reverse transcription/PCR products together with the sequence from a clone isolated from a cDNA library developed from corticotropin-stimulated mouse adrenocortical Y/cells. Corticotropin-activated adrenocortical Y/cells revealed an enhanced expression of PC5 mRNA, indicating an upregulation by cAMP.

Published
1993

8. Ontogeny of the prohormone convertases PC1 and PC2 in the mouse hypophysis and their colocalization with corticotropin and alpha-melanotropin

Author

Marcinkiewicz, M., Day, R., Seidah, N.G., and Chretien, M.

Subjects
Ontogeny -- Analysis, Pituitary gland -- Physiological aspects, Science and technology
Abstract

Researchers studied how the expression pattern of prohormone convertases PC1 and PC2 mRNA transcripts correlates with that of corticotropin (ACTH) and alpha-melanotropin (alphaMSH)-like immunoreactivity in an ontogeny analysis. Their results prove the hypothesis that PC2 is the significant convertase in the processing of proopiomelanocortin (POMC) into alpha MSH.

Published
1993

20. Isolation, structure, and synthesis of a human seminal plasma peptide with inhibin-like activity

Author

Ramasharma, K., Sairam, M.R., Seidah, N.G., Chretien, M., Manjunath, P., Schiller, P.W., and Yamashiro, D.

Subjects
Hormone research -- Research, Science and technology, Research
Abstract

A substance called 'inhibin,' believed to be present in aqueous extracts of testis, was imputed (1) to have an important if not exclusive role in the secretion of pituitary follicle-stimulating [...]

Published
1984

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