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Cloning of the cDNA for human 5-lipoxygenase

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
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The enzyme 5-lipoxygenase (5-LO) catalyzes the first two reactions in the pathway leading to the formation of leukotrienes from arachidonic acid. Leukotrienes are potent arachidonic acid metabolites possessing biological activities that suggest a role in the pathophysiology of allergic and inflammatory disease. To obtain structural information about 5-LO for use in developing anti-flammatory chemotherapeutic agents, the enzyme was purified from human polymorphonuclear leukocytes and the amino acid sequences were determined for several cyanogen bromide-derived peptides. A cDNA clone encoding a 674-amino acid protein containing all of the derived peptide sequences was isolated from a dimethyl sulfoxide differentiated HL60 cell cDNA library. The mRNA encoding 5-LO was detected only in differentiated HL60 cells and not in the undifferentiated cell line, indicating that the expression of 5-LO in this cell line is transcriptionally regulated. In addition, the human protein displays some amino acid sequence homology with several lipases and significant homology with the partial sequences of soybean and reticulocyte lipoxygenases. Thus, 5-LO appears to be a member of a larger family of related enzymes.

Research Organization:
Merck Sharp and Dohme Research Labs., West Point, PA (USA)
OSTI ID:
6143379
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 85:2; ISSN PNASA
Country of Publication:
United States
Language:
English

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Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
ANIMALS
ARACHIDONIC ACID
BIOLOGICAL PATHWAYS
CARBOXYLIC ACIDS
CLONING
DNA
DNA HYBRIDIZATION
DNA-CLONING
ENZYMES
GROWTH FACTORS
HYBRIDIZATION
INFLAMMATION
LYMPHOKINES
MAMMALS
MAN
MESSENGER-RNA
MITOGENS
MOLECULAR STRUCTURE
MONOCARBOXYLIC ACIDS
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
OXYGENASES
PATHOLOGICAL CHANGES
PRIMATES
PROTEINS
PURIFICATION
RECOMBINANT DNA
RNA
SYMPTOMS
VERTEBRATES