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- Title
Limited Proteolysis of High Molecular Weight Histidine-Rich Protein of Rat Epidermis by Epidermal Proteinases.
- Authors
Kashima, Masato; Fukuyama, Kimie; Kikuchi, Mamoru; Epstein, William L.
- Abstract
Epidermal proteinases, which may be involved in proteolysis of Mr> 300k histidine-rich protein in epidermis, were studied by SDS-PAGE analysis. Mr> 300k histidine-rich protein was extracted from granular cells of 2-day-old rats in citric acid-sucrose solution and separated from proteinases and smaller Mr proteins by Sephacryl S-300 column chromatography. The proteinase-free histidine-rich protein was stable in pH 3.5-9 at 37°C for 12 h. Proteinases were partially purified from rat epidermis and inhibitor spectrum determined for each enzyme. Limited hydrolysis of Mr> 300k histidine-rich protein yielded a derivative of Mr 56k with cathepsin D at pH 3.5-7.5 and a serine proteinase at pH 7-9. Further proteolysis of Mr 56k protein to Mr 44k and a doublet of Mr 45k and 47k also was detected with cathepsin D at pH 3.5 and 7.5, respectively, while the serine proteinase degraded Mr 56k protein to a number of protein bands. Cathepsins B and L degraded Mr> 300k protein but no specific predominant product was identified. We suggest that cathepsin D and the serine proteinase may play a role in in situ processing of histidine-rich protein during cornification.
- Subjects
PROTEIN metabolism; PROTEINASES; PROTEOLYSIS; EPIDERMIS; PROTEOLYTIC enzymes; LABORATORY rats
- Publication
Journal of Investigative Dermatology, 1988, Vol 90, Issue 6, p829
- ISSN
0022-202X
- Publication type
Article
- DOI
10.1111/1523-1747.ep12462067