Human Eccrine Sweat Contains Tissue Kallikrein and Kininase II
Human Eccrine Sweat Contains Tissue Kallikrein and Kininase II Toshihiko Hibino, Toshiyuki Takemura, and Kenzo Sato Marshall Dermatology Research Laboratories, Department of Dermatology, Universiry of Iowa Co llege of Medicine, Iowa Ciry, Iowa, U.S.A. We attempted to determine the level of sweat kallikrein kallikrein is the glandular type. Purified sweat and salivary (kininogenase) and to purify and characterize it using sweat kallikrein showed similar Mr and responses to inhibitors and collected over a white petrolatum barrier. Thermally induced antibodies. Using immunohistochemistry, kallikrein activity eccrine sweat obtained from 24 healthy subjects showed kal was localized in luminal ductal cells and in the peripheral rirn likrein activity of 24.4 ng kinins generated/1 mg of sweat of secretory coil segments, presumably the outer membrane protein when heated plasma was used as the substrate and of the myoepithelium. We also observed kininase activity in 16.1 ng kinin when purified low molecular weight bovine sweat at Mr 160,000, which was inhibited by ethylenedia kininogen was used as the substrate. Sweat was sequentially mine tetraacetic acid, captopril, and angiotensin converting purified by Sephacryl S-200, diethyaminoethyl Sephacel, enzyme inhibitor peptide, indicating that it is kininase II (or and fast flow liquid chromatography Mono Q chromatogra angiotensin converting enzyme). Sweat also contains abun phy. Sweat kallikrein had aMrof 40,000 and was inhibited by dant non-kallikrein hydrolases for S-2266 and S-2302. The aprotinin but not by soybean trypsin inhibitor. The peptide demonstration of glandular kallikrein, its tissue localization, generated by sweat kallikrein was identified as lys-bradykinin and the presence of kininase II in sweat provide the basis for using reverse phase high-performance liquid chromatogra future studies on the physiologic role of the kallikrein/kinin phy and by its amino acid sequence.
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