NDLI: Molecular cloning and expression of human leukotriene-C4 synthase.

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Molecular cloning and expression of human leukotriene-C4 synthase.

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Molecular cloning and expression of human leukotriene-C4 synthase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hauser, S. D. Mathis, K. J. Krivi, G. G. Welsch, D. J. Creely, D. P. Isakson, P. C.
Description	Author Affiliation: Welsch DJ ( Searle Research and Development, Monsanto Company, St. Louis, MO 63198.);
Abstract	Leukotriene-C4 synthase (LTC4S; EC 2.5.1.37) catalyzes the committed step in the biosynthesis of the peptidoleukotrienes, which are important in the pathogenesis of asthma. Antibodies were generated to a synthetic peptide based on the partial amino acid sequence previously reported for human LTC4S [Nicholson, D.W., Ali, A., Vaillancourt, J.P., Calaycay, J.R., Mumford, R.A., Zamboni, R.J. & Ford-Hutchinson, A. W. (1993) Proc. Natl. Acad. Sci. USA 90, 2015-2019] and specifically bound detergent-solubilized LTC4S obtained from THP-1 cells, confirming that the published sequence is associated with enzyme activity. Inosine-containing oligonucleotides based on the partial protein sequence were used to isolate a 679-bp cDNA for LTC4S from THP-1 cells. The cDNA contains an open reading frame that encodes a 150-amino acid protein (M(r) = 16,568) that has a calculated pI value of 11.1. The deduced protein sequence is composed predominantly of hydrophobic amino acids; hydropathy analysis predicts three transmembrane domains connected by two hydrophilic loops. Analysis of the deduced sequence identified two potential protein kinase C phosphorylation sites and a potential N-linked glycosylation site. The amino acid sequence for human LTC4S is unique and shows no homology to other glutathione S-transferases. LTC4S was found to be most similar to 5-lipoxygenase activating protein (31% identity, 53% similarity), another protein involved in leukotriene biosynthesis. Active enzyme was expressed in bacterial, insect, and mammalian cells as shown by the biosynthesis of LTC4 in incubation mixtures containing LTA4 and reduced glutathione. The cloning and expression of human LTC4S provide the basis for a better understanding of this key enzyme in peptidoleukotriene biosynthesis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Glutathione Transferase Biosynthesis Amino Acid Sequence Animals Cell Line Cell Membrane Enzymology Ultrastructure Cloning, Molecular DNA Primers DNA, Complementary Isolation & Purification Gene Expression Chemistry Insects Models, Structural Molecular Sequence Data Polymerase Chain Reaction Protein Conformation Recombinant Proteins Restriction Mapping Sequence Homology, Amino Acid Comparative Study Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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