Abstract
Human erythroleukemia cells transformed arachidonic acid and prostaglandin endoperoxide H2 into thromboxane A2. Stimulation of these cells with A23187 or thrombin, however, produced no thromboxane. Similarly, cells labeled with [3H]-arachidonic acid released no detectable label upon stimulation. Data suggest that human erythroleukemia cells contain the enzymatic capacity for thromboxane formation from exogenous precursors, but lack the endogenous mechanisms for arachidonate release. The presence of thromboxane synthase messenger RNA was verified using the polymerase chain reaction. Amplification and sequence analysis of a 528 bp cDNA demonstrated virtually 100% identity to a published thromboxane synthase cDNA fragment.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Arachidonic Acid / metabolism
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Base Sequence
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Calcimycin / pharmacology
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Electrophoresis, Polyacrylamide Gel
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Gene Expression
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Humans
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Leukemia, Erythroblastic, Acute / metabolism
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Molecular Sequence Data
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Polymerase Chain Reaction
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Prostaglandins H / metabolism
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RNA, Messenger / genetics
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Sequence Homology, Nucleic Acid
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Thrombin / pharmacology
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Thromboxane A2 / biosynthesis*
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Thromboxane-A Synthase / genetics
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Tumor Cells, Cultured
Substances
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Prostaglandins H
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RNA, Messenger
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Arachidonic Acid
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Calcimycin
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Thromboxane A2
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Thrombin
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Thromboxane-A Synthase
Associated data
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GENBANK/M64053
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GENBANK/M64054
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GENBANK/M64055
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GENBANK/M64056
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GENBANK/M64057
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GENBANK/M64058
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GENBANK/M64059
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GENBANK/M64060
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GENBANK/S60133
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GENBANK/S60134