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Urokinase-type plasminogen activator in human eccrine sweat
1Marshall Dermatology Research Laboratories, Department of Dermatology, University of Iowa College of Medicine, Iowa City.
The British Journal of Dermatology
|February 1, 1993
Summary
Urokinase-type plasminogen activator (uPA) was detected in human eccrine sweat for the first time. This enzyme likely originates from sweat glands, but its physiological role requires further investigation.
Area of Science:
- Biochemistry
- Dermatology
- Enzymology
Background:
- The presence and type of plasminogen activators (PAs) in human eccrine sweat have not been previously characterized.
- Understanding sweat composition is crucial for various physiological and diagnostic applications.
Purpose of the Study:
- To investigate the presence and nature of plasminogen activator (PA) activity in human eccrine sweat.
- To identify the specific type of PA present in sweat.
Main Methods:
- Collection of clean eccrine sweat from human subjects, followed by concentration via ultrafiltration.
- Assay of PA activity using a two-step method with S-2251 substrate.
- Characterization of PA using Sephacryl S-200 gel chromatography and gelatin-polyacrylamide enzymography.
- Inhibition studies using specific antibodies (anti-uPA IgG, anti-tPA IgG) and epidermal PA inhibitor.
Main Results:
- PA activity was detected in 53% (9 of 17) of sweat samples.
- Gel chromatography revealed a major PA peak at approximately 55,000 M(r).
- Enzymography identified a major band at 55,000 M(r) and a minor band at 33,000 M(r).
- Sweat PA activity was significantly inhibited by anti-uPA IgG and epidermal PA inhibitor, but not by anti-tPA IgG.
Conclusions:
- The PA activity detected in human eccrine sweat is primarily derived from the sweat gland.
- The enzyme is most likely urokinase-type plasminogen activator (uPA).
- The physiological significance of uPA in sweat remains to be elucidated.