Biochemical Journal · 1993 · 516 citations · 48 references
Life SciencesMolecular BiologyMolecular GeneticsBiochemical GeneticsGene ExpressionImmunogeneticsEnzyme RegulationPlasma ProteinsInsertion-deletion MarkersInsertion-deletion Polymorphism MarkersInsertion-deletion VariantsInsertion-deletion VariationPolymorphism Studies
The expression of angiotensin-I converting enzyme (ACE; EC 3.4.15.1) in human circulating mononuclear cells was studied. T-lymphocytes contained the highest level of enzyme, approx. 28 times more per cell than monocytes. No activity was detected in B-lymphocytes. ACE was present mainly in the microsomal fraction, where it was found to be the major membrane-bound bradykinin-inactivating enzyme. An mRNA for ACE was detected and characterized after reverse transcription and amplification by PCR in T-lymphocytes and several T-cell leukaemia cell lines. We have previously observed that the interindividual variability in the levels of ACE in plasma is, in part, genetically determined and influenced by an insertion/deletion polymorphism of the ACE gene. To investigate the mechanisms involved in the regulation of ACE biosynthesis, the ACE levels of T-lymphocytes from 35 healthy subjects having different ACE genotypes were studied. These levels varied widely between individuals but were highly reproducible and influenced by the polymorphism of the ACE gene. T-lymphocyte levels of ACE were significantly higher in subjects who were homozygote for the deletion than in the other subjects. These results show that ACE is expressed in T-lymphocytes and indicate that the level of ACE expression in cells synthesizing the enzyme is genetically determined.
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Brigitte Rigat, C. Hübert, F Alhenc‐Gelas et al. · Journal of Clinical Investigation · 1990 · 3.8K citations · Full text