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Angiotensin-converting enzyme: characteristics in human skin fibroblasts
Metabolism: Clinical and Experimental
|October 1, 1986
Summary
This study found that cultured human skin fibroblasts contain angiotensin-converting enzyme (ACE). However, common hormones like glucocorticoids and thyroid hormone did not significantly alter fibroblast ACE activity.
Area of Science:
- Biochemistry
- Cell Biology
- Enzymology
Background:
- Angiotensin-converting enzyme (ACE) is found in various tissues beyond vascular endothelium.
- Hormonal regulation of ACE activity by glucocorticoids and thyroid hormone has been suggested.
- The presence and regulation of ACE in human skin fibroblasts remain to be fully elucidated.
Purpose of the Study:
- To investigate the presence and characterize the activity of angiotensin-converting enzyme (ACE) in cultured human skin fibroblasts.
- To determine the effect of specific hormones on fibroblast ACE activity.
Main Methods:
- Cultured human skin fibroblasts were used to measure ACE activity via a radiometric assay.
- Enzyme kinetics, including optimal pH, temperature, and substrate concentration (Km), were determined.
- The effects of various inhibitors and competitive substrates were assessed.
- Fibroblasts were incubated with hormones (T3, 1,25(OH)2D3, dexamethasone, R1881) to evaluate changes in ACE activity.
Main Results:
- Angiotensin-converting enzyme (ACE) was identified in all tested human skin fibroblast strains.
- Optimal conditions for fibroblast ACE activity were determined (pH 6.9-7.6, 37°C).
- Captopril was identified as a potent inhibitor, and angiotensin-I, substance P, and bradykinin acted as competitive substrates.
- Incubation with tested hormones did not significantly alter cellular ACE activity.
Conclusions:
- Human skin fibroblasts possess measurable angiotensin-converting enzyme (ACE) activity.
- The activity of ACE in these fibroblasts is not significantly modulated by the tested hormonal agents.
- These findings contribute to understanding the tissue-specific roles and regulation of ACE.