Separation and Identification of Cathepsins in Newborn Rat Epidermis

Harvima, Rauno J.; Yabe, Kazuo; Fräki, Jorma E.; Fukuyama, Kimie; Epstein, William L.

doi:10.1111/1523-1747.ep12469719

Cited by 10 publications

(8 citation statements)

References 24 publications

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“…1991). Cathepsin L‐like proteinase has been purified from rat epidermis (Harvima et al . 1987), and inactive precursors of cathepsin L have been identified in normal human epidermis.…”

Section: Discussionmentioning

confidence: 99%

“…It has been postulated that cathepsin L may partly regulate both protein breakdown and intracellular protein metabolism during the course of cell differentiation, and terminal differentiation, in cultured rat keratinocytes (Tanabe et al 1991). Cathepsin L-like proteinase has been purified from rat epidermis (Harvima et al 1987), and inactive precursors of cathepsin L have been identified in normal human epidermis. Activated cathepsin L has been linked to the pathology of psoriasis (Kawada et al 1978).…”

Section: Discussionmentioning

confidence: 99%

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Cathepsin L‐deficient mice exhibit abnormal skin and bone development and show increased resistance to osteoporosis following ovariectomy

Potts

Bowyer

Jones

et al. 2004

Int J Experimental Path

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The role of cathepsin L in normal physiological processes was assessed using cathepsin L homozygous knockout mice (B6;129-Ctsl(tm1Alpk)). These mice were generated using gene targeting in embryonic stem cells. Null mice fail to express mRNA and protein to cathepsin L. They developed normally and were fertile. The distinct phenotypic change exhibited was a progressive hair loss, culminating in extensive alopecia by 9 months of age. Histological analysis of the skin from homozygous mice revealed diffuse epithelial hyperplasia, hypotrichosis, hair shaft fragmentation and utricle formation. These findings provide evidence that cathepsin L is involved in the regulation of epithelial cell proliferation and differentiation in the skin. In addition, the role of cathepsin L in bone remodelling was evaluated. Using bone histomorphometric measurements, trabecular, but not cortical, bone volume was found to be significantly decreased in the cathepsin L heterozygote and homozygote mice compared to the wild-type mice. Following ovariectomy, it was observed that loss of trabecular bone, the most metabolically active component of bone, occurred to a lesser extent in homozygote, and heterozygote mice, than was seen in wild-type mice. These observations suggest that cathepsin L is likely to have a role in controlling bone turnover during normal development and in pathological states.

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“…1991). Cathepsin L‐like proteinase has been purified from rat epidermis (Harvima et al . 1987), and inactive precursors of cathepsin L have been identified in normal human epidermis.…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Cathepsin L‐deficient mice exhibit abnormal skin and bone development and show increased resistance to osteoporosis following ovariectomy

Potts

Bowyer

Jones

et al. 2004

Int J Experimental Path

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“…We therefore think that CB-like enzyme activity and CPI activity are derived mainly from melanocytes/melanoma cells [1,3,5,6,9]. Therefore, the possibility cannot be excluded that the homogenates of the tissues we used contained less CB-like enzyme activity and/or CPI activity derived from fibroblasts, keratinocytes and leucocytes.…”

Section: Discussionmentioning

confidence: 99%

Clinical relevance of cathepsin B-like enzyme activity and cysteine proteinase inhibitor in melanocytic tumours

et al. 1995

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We studied the relationship between cathepsin B (CB)-like enzyme activities and cysteine proteinase inhibitor (CPI) activities in lesions of human pigmented naevi (PN), primary melanomas (PM) and metastases/metastatic melanomas (MM). The CB-like enzyme activities in PM and MM were 2.5 and 6.8 times higher than in PN, respectively. The CB-like/CPI ratios in PM and MM were 1.9 and 11.6 times higher than in PN, respectively. CPI had the highest activity in PM and the lowest activity in MM. The disease-free interval of patients with a high CB-like enzyme activity (> or = 80 U/mg protein) and/or a high CB-like/CPI ratio (> or = 7) was shorter than that of patients with a low CB-like enzyme activity (< 80 U/mg protein) and/or a low CB-like/CPI ratio (< 7). Analysis of CB-like enzyme activity and/or the CB-like/CPI ratio may be useful in predicting the prognosis of human malignant melanoma.

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“…Separation of epidermis and extraction of epidermal proteins were done as described previously [27].…”

Section: Extraction and Fractionation Of Epidermal Proteinasesmentioning

confidence: 99%

“…of 20 mM-sodium acetate buffer, pH 5.0, containing I mM-EDTA and 1 mM-DTT, and centrifuged at 8000 g for 30 min. The proteins in the supernatant were further fractionated on a CM-cellulose CM-52 column [27]. U.v.…”

Section: Extraction and Fractionation Of Epidermal Proteinasesmentioning

confidence: 99%

Hydrolysis of histones by proteinases

Harvima

Yabe

Fräki

et al. 1988

Biochemical Journal

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Hydrolysis of histones by proteinases from rat liver, skin and other sources was studied by using a rat thymus histone preparation as the substrate and polyacrylamide-gel electrophoresis and densitometric analysis as the methods to detect histone subtypes and their hydrolysis. The rat mast-cell proteinase I effectively hydrolysed histones except type H4. Thrombin hydrolysed effectively histones H1 and H2A, whereas plasmin hydrolysed all types of histones. Cathepsin D hydrolysed especially histone H2A. Cathepsins B and L hydrolysed all histones more slowly, and cathepsin H hydrolysed them extremely slowly. Epidermal aminoendopeptidase did not hydrolyse histones. Trypsin and chymotrypsin were used as reference enzymes, which hydrolysed all types of histones in very low concentrations. This study suggests that a variety of proteinases could play a role in histone hydrolysis. Hydrolysis of a specific subtype of histones, such as histone H2A at pH 6 by cathepsin D, may be directly involved in regulation of epidermal-cell differentiation.

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Separation and Identification of Cathepsins in Newborn Rat Epidermis

Cited by 10 publications

References 24 publications

Cathepsin L‐deficient mice exhibit abnormal skin and bone development and show increased resistance to osteoporosis following ovariectomy

Cathepsin L‐deficient mice exhibit abnormal skin and bone development and show increased resistance to osteoporosis following ovariectomy

Clinical relevance of cathepsin B-like enzyme activity and cysteine proteinase inhibitor in melanocytic tumours

Hydrolysis of histones by proteinases

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