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Dystroglycan in skin and cutaneous cells: beta-subunit is shed from the cell surface

Herzog, C; Has, C; Franzke, CW; Echtermeyer, FG; Schlotzer-Schrehardt, U; Kroger, S; Gustafsson, Erika LU ; Fassler, R and Bruckner-Tuderman, L (2004) In Journal of Investigative Dermatology 122(6). p.1372-1380
Abstract
In skin, hemidesmosomal protein complexes attach the epidermis to the dermis and are critical for stable connection of the basal epithelial cell cytoskeleton with the basement membrane (BM). In muscle, a similar supramolecular aggregate, the dystrophin glycoprotein complex links the inside of muscle cells with the BM. A component of the muscle complex, dystroglycan (DG), also occurs in epithelia. In this study, we characterized the expression and biochemical properties of authentic and recombinant DG in human skin and cutaneous cells in vitro. We show that DG is present at the epidermal BM zone, and it is produced by both keratinocytes and fibroblasts in vitro. The biosynthetic precursor is efficiently processed to the alpha- and beta-DG... (More)
In skin, hemidesmosomal protein complexes attach the epidermis to the dermis and are critical for stable connection of the basal epithelial cell cytoskeleton with the basement membrane (BM). In muscle, a similar supramolecular aggregate, the dystrophin glycoprotein complex links the inside of muscle cells with the BM. A component of the muscle complex, dystroglycan (DG), also occurs in epithelia. In this study, we characterized the expression and biochemical properties of authentic and recombinant DG in human skin and cutaneous cells in vitro. We show that DG is present at the epidermal BM zone, and it is produced by both keratinocytes and fibroblasts in vitro. The biosynthetic precursor is efficiently processed to the alpha- and beta-DG subunits; and, in addition, a distinct extracellular segment of the transmembranous beta-subunit is shed from the cell surface by metalloproteinases. Shedding of the beta-subunit releases the alpha-subunit from the DG complex on the cell surface into the extracellular space. The shedding is enhanced by IL-1beta and phorbol esters, and inhibited by metalloproteinase inhibitors. Deficiency of perlecan, a major ligand of alpha-DG, enhanced shedding suggesting that lack of a binding partner destabilizes the epithelial DG complex and makes it accessible to proteolytic processing. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
secretase, glycoprotein, adhesion, BM, shedding
in
Journal of Investigative Dermatology
volume
122
issue
6
pages
1372 - 1380
publisher
Nature Publishing Group
external identifiers
  • pmid:15175026
  • wos:000221693500008
  • scopus:2942568034
ISSN
1523-1747
DOI
10.1111/j.0022-202X.2004.22605.x
language
English
LU publication?
yes
id
5a0d4b24-3857-427c-a5a3-662e5da71e64 (old id 276888)
date added to LUP
2007-10-30 12:03:25
date last changed
2017-10-22 03:46:37
@article{5a0d4b24-3857-427c-a5a3-662e5da71e64,
  abstract     = {In skin, hemidesmosomal protein complexes attach the epidermis to the dermis and are critical for stable connection of the basal epithelial cell cytoskeleton with the basement membrane (BM). In muscle, a similar supramolecular aggregate, the dystrophin glycoprotein complex links the inside of muscle cells with the BM. A component of the muscle complex, dystroglycan (DG), also occurs in epithelia. In this study, we characterized the expression and biochemical properties of authentic and recombinant DG in human skin and cutaneous cells in vitro. We show that DG is present at the epidermal BM zone, and it is produced by both keratinocytes and fibroblasts in vitro. The biosynthetic precursor is efficiently processed to the alpha- and beta-DG subunits; and, in addition, a distinct extracellular segment of the transmembranous beta-subunit is shed from the cell surface by metalloproteinases. Shedding of the beta-subunit releases the alpha-subunit from the DG complex on the cell surface into the extracellular space. The shedding is enhanced by IL-1beta and phorbol esters, and inhibited by metalloproteinase inhibitors. Deficiency of perlecan, a major ligand of alpha-DG, enhanced shedding suggesting that lack of a binding partner destabilizes the epithelial DG complex and makes it accessible to proteolytic processing.},
  author       = {Herzog, C and Has, C and Franzke, CW and Echtermeyer, FG and Schlotzer-Schrehardt, U and Kroger, S and Gustafsson, Erika and Fassler, R and Bruckner-Tuderman, L},
  issn         = {1523-1747},
  keyword      = {secretase,glycoprotein,adhesion,BM,shedding},
  language     = {eng},
  number       = {6},
  pages        = {1372--1380},
  publisher    = {Nature Publishing Group},
  series       = {Journal of Investigative Dermatology},
  title        = {Dystroglycan in skin and cutaneous cells: beta-subunit is shed from the cell surface},
  url          = {http://dx.doi.org/10.1111/j.0022-202X.2004.22605.x},
  volume       = {122},
  year         = {2004},
}