Literature DB >> 3888399

Immunological detection of a cysteine protease in the skin and other tissues.

K Fukuyama, Y Ito, K Yabe, W L Epstein.   

Abstract

Monospecific antibody directed to cysteine protease of 2-day-old rat epidermis recently characterized as being different from the proteases previously reported was produced in rabbits. By immunofluorescence microscopy and immunoperoxidase staining with an avidin-biotin-peroxidase method the protease was found to be present in the epidermis of rodents of different ages as well as that of humans, but not in the dermis. The staining in germinative cells was more intense than in cells in the superficial layers. It appeared as irregular patches in the nuclei and stained more diffusely in the cytoplasm where small granular components, strongly stained, were identified. The staining patterns in granular cells showed accumulation of the antigen in a granular form. The morphology and distribution of granules resembled those of keratohyalin-like granules in the nucleus and dense homogeneous deposits in the cytoplasm. In cornified cells the reaction product was localized by the plasma membrane where concentration of the dense homogeneous deposits occurred, suggesting that the cysteine protease is one component of the unique and characteristic structure of differentiated keratinocytes. In addition, the cysteine protease antigen having the same molecular weight as the epidermal enzyme was detected in liver, kidney and lung indicating a wider tissue distribution of the protease. The significance of the protease in regulation of cellular functions remains to be investigated.

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Year:  1985        PMID: 3888399     DOI: 10.1007/bf00222354

Source DB:  PubMed          Journal:  Cell Tissue Res        ISSN: 0302-766X            Impact factor:   5.249


  32 in total

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Authors:  O OUCHTERLONY
Journal:  Prog Allergy       Date:  1962

2.  alpha-N-benzoylarginine-2-naphthylamide hydrolase (cathepsin B1 ?) from rat skin. II. Purification of the enzyme and demonstration of two inhibitors in the skin.

Authors:  M Järvinen; V K Hopsu-Havu
Journal:  Acta Chem Scand B       Date:  1975

3.  Dense homogeneous deposits of keratohyalin granules in newborn rat epidermis.

Authors:  K Fukuyama; K A Wier; W L Epstein
Journal:  J Ultrastruct Res       Date:  1972-01

4.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

5.  Purification and properties of brain cathepsin B. Evidence for cleavage of pituitary lipotropins.

Authors:  A Suhar; N Marks
Journal:  Eur J Biochem       Date:  1979-11-01

6.  The low-molecular-weight SH-protease inhibitor in rat skin is epidermal.

Authors:  M Järvinen; O Räsänen; A Rinne
Journal:  J Invest Dermatol       Date:  1978-08       Impact factor: 8.551

7.  alpha-N-benzoylarginine-beta-naphthylamide hydrolase, an aminoendopeptidase from rabbit lung.

Authors:  H Singh; G Kalnitsky
Journal:  J Biol Chem       Date:  1980-01-25       Impact factor: 5.157

8.  Cathepsin B from human renal cortex.

Authors:  A D Gounaris; E E Slater
Journal:  Biochem J       Date:  1982-08-01       Impact factor: 3.857

9.  Chemical characterization, synthesis and distribution of proteinase inhibitor in newborn rat epidermis.

Authors:  T Hibino; K Fukuyama; W L Epstein
Journal:  Biochim Biophys Acta       Date:  1980-10-01

10.  Sulphure in epidermal keratohyalin granules: a quantitative assay by x-ray microanalysis.

Authors:  H Jessen; P D Peters; T A Hall
Journal:  J Cell Sci       Date:  1976-10       Impact factor: 5.285

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