The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation

Becker-Pauly, Christoph; Höwel, Markus; Walker, Tatjana; Vlad, Annica; Aufenvenne, Karin; Oji, Vinzenz; Lottaz, Daniel; Sterchi, Erwin E; Debela, Mekdes; Magdolen, Viktor; Traupe, Heiko; Stöcker, Walter (2007). The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation. Journal of Investigative Dermatology, 127(5), pp. 1115-25. New York, N.Y.: Nature Publishing 10.1038/sj.jid.5700675

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The zinc endopeptidase meprin (EC 3.4.24.18) is expressed in brush border membranes of intestine and kidney tubules, intestinal leukocytes, and certain cancer cells, suggesting a role in epithelial differentiation and cell migration. Here we show by RT-PCR and immunoblotting that meprin is also expressed in human skin. As visualized by immunohistochemistry, the two meprin subunits are localized in separate cell layers of the human epidermis. Meprin alpha is expressed in the stratum basale, whereas meprin beta is found in cells of the stratum granulosum just beneath the stratum corneum. In hyperproliferative epidermis such as in psoriasis vulgaris, meprin alpha showed a marked shift of expression from the basal to the uppermost layers of the epidermis. The expression patterns suggest distinct functions for the two subunits in skin. This assumption is supported by diverse effects of recombinant meprin alpha and beta on human adult low-calcium high-temperature keratinocytes. Here, beta induced a dramatic change in cell morphology and reduced the cell number, indicating a function in terminal differentiation, whereas meprin alpha did not affect cell viability, and may play a role in basal keratinocyte proliferation.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Sterchi, Erwin-Ernst

ISSN:

0022-202X

ISBN:

17195012

Publisher:

Nature Publishing

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:53

Last Modified:

04 May 2014 23:15

Publisher DOI:

10.1038/sj.jid.5700675

PubMed ID:

17195012

Web of Science ID:

000245889900017

URI:

https://boris.unibe.ch/id/eprint/22699 (FactScience: 36073)

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