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The low molecular weight sulfhydryl protease inhibitor in rat skin is epidermal


, : The low molecular weight sulfhydryl protease inhibitor in rat skin is epidermal. Journal of Investigative Dermatology 71(2): 119-121

The epidermis and dermis of rat skin were separated, and the presence of the high-MW SH-protease inhibitor I1 and the low-MW inhibitor I2 in both was studied. Gel filtrations of the extracts revealed that 97% of the epidermal inhibitor activity was due to I2 and 89% of the dermal activity to I1. The presence of I2 mainly in the epidermis extract was confirmed by immunodiffusion of specific rabbit anti-I2 serum against purified I2, epidermis and dermis extracts and rat serum. Most of the immunoreactive protein was seen in the epidermis extract, traces in the dermis extract and none in the rat serum. I2 was localized in rat skin by indirect immunofluorescence using rabbit anti-I2 serum and fluorescein isothiocyanate conjugate of goat antirabbit immunoglobulins. Intense fluorescence, much brighter than in the controls treated with rabbit nonimmune serum, was seen in the epidermis, being most pronounced in the cytoplasms of cells in the granular layer. The weak fluorescence of the hair follicles, sebaceous glands, connective tissue cells and fibers was unspecific and was also seen in the controls. In view of its epidermal location, the name epidermal SH-protease inhibitor was suggested for I2.

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Related references

Järvinen, M.; Räsänen, O.; Rinne, A., 1978: The low-molecular-weight SH-protease inhibitor in rat skin is epidermal. The epidermis and dermis of rat skin were separated and the presence of the high-molecular-weight SH-protease inhibitor I1 and the low-molecular-weight inhibitor I2 in both was studied. Gel filtrations of the extracts revealed that 97% of the epid...

Anonymous, 1960: Studies on the role of sulfhydryl groups in the biochemical mechanisms of allergic inflammation HI Behavior of isolated inhibitor on skin sulfhydryl protease

Wakimoto, A.; Sagawa, Y.; Higuchi, D.; Takiuchi, I., 1983: Purification and some characteristics of human epidermal low-molecular-weight protease inhibitor of extracellular keratinase. The low-molecular-weight protease inhibitor of the extracellular keratinase from Microsporum canis was separated from human epidermis extracts by means of homogenisation, ultrafiltration, ion-exchange-chromatography and gel-filtration. By these pr...

Rinne A.; Jarvinen M.; Dammert K.; Larmi T.K.I.; Rasanen O., 1982: Epidermal sulfhydryl protease inhibitor a new marker of squamous epithelia. Pathology Research & Practice 176(1): 50

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Rinne A., 1980: Epidermal sulfhydryl protease inhibitor in human neoplasms and their metastases. The presence of the human epidermal SH(sulfhydryl)-protease inhibitor in human tumors of different types was examined using double radial immunodiffusion against specific antisera to the inhibitor. The immunoreactive protein was present in all the...

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Rinne, A.; Jarvinen, M.; Rasanen, O., 1978: A protein reminiscent of the epidermal sulfhydryl protease inhibitor occurs in squamous epithelia of man and rat. The occurrence of the human and rat epidermal SH-protease inhibitors in various human and rat tissues was studied by double radioimmunodiffusion against specific antisera. An immunoreactive protein was found in the extracts prepared from human and...

Jaervinen, M.; Rinne, A.; Rasanen, O., 1978: A protein reminiscent of epidermal sulfhydryl protease inhibitor occurs in squamous carcinoma of the lung. An immunoreactive protein resembling the human epidermal SH-protease inhibitor is demonstratable in squamous epithelial (epidermoid) carcinoma of the bronchus, but not in pulmonary adenocarcinoma or small-cell anaplastic carcinoma of the bronchus...