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Mol Cell Endocrinol

Title:		Cleavage-secretion of angiotensin I-converting enzyme in yeast
Author(s):		Williams TA; Gouttaya M; Tougard C; Michaud A; Chauvet MT; Corvol P;
Address:		"INSERM unite 36, College de France, Paris. williams@infobiogen.fr"
Journal Title:		Mol Cell Endocrinol
Year:		1997
Volume:		128
Issue:		1-Feb
Page Number:		39 - 45
DOI:		10.1016/s0303-7207(97)04022-7
ISSN/ISBN:		0303-7207 (Print) 0303-7207 (Linking)
Abstract:		"Angiotensin I-converting enzyme (ACE) is a type I transmembrane protein composed of two domains (N and C domains) which undergoes a post-translational proteolytic cleavage in mammalian cells to release the soluble ectodomain. The protease involved in ACE cleavage-secretion (ACE-secretase) is not well characterised and eludes isolation: the presence of a yeast homologue, thus more amenable to genetic manipulation, would facilitate its identification. We have expressed a secreted form of the ACE C domain, lacking the C-terminal membrane anchor (C domain(deltaCOOH)), and the membrane-anchored C domain (C domain) in the yeast Pichia pastoris by fusion to prepro-alpha-factor. Immunofluorescent labelling localises the ACE C domain to the periphery of yeast cells but not C domain(deltaCOOH), however, expression of both C domain and C domain(deltaCOOH) produced soluble enzymes in the culture medium. Immunocharacterisation of the two soluble forms of the C domain indicates a proteolytic cleavage of the membrane-bound C domain to produce the soluble counterpart. Thus ACE undergoes a proteolytic cleavage in yeast"
Keywords:		"Amino Acid Sequence Cloning, Molecular Endopeptidases/*metabolism Humans Kinetics Mating Factor Molecular Sequence Data Mutagenesis, Site-Directed Peptide Biosynthesis *Peptides Peptidyl-Dipeptidase A/biosynthesis/chemistry/*metabolism Pichia Protease Inh;"
Notes:		"MedlineWilliams, T A Gouttaya, M Tougard, C Michaud, A Chauvet, M T Corvol, P eng Research Support, Non-U.S. Gov't Ireland 1997/04/04 Mol Cell Endocrinol. 1997 Apr 4; 128(1-2):39-45. doi: 10.1016/s0303-7207(97)04022-7"