Collagen XVII in hemidesmosomes is involved in keratinocyte-collagen IV adhesion and p38-MAPK-dependent cell migration and signaling

McMillan, J. R., Qiao, H., Shibaki, A., Long, H.A., Wang, G., Li, Q., Nishie, W., Abe, R., Akiyama, M. and Shimizu, H. (2009). Collagen XVII in hemidesmosomes is involved in keratinocyte-collagen IV adhesion and p38-MAPK-dependent cell migration and signaling. In: Journal of Investigative Dermatology: Proceedings of the 39th Annual European Society for Dermatological Research Meeting. 39th Annual European Society for Dermatological Research Meeting, Budapest, Hungary, (S80-S80). 9-12 September, 2009. doi:10.1038/jid.2009.232


Author McMillan, J. R.
Qiao, H.
Shibaki, A.
Long, H.A.
Wang, G.
Li, Q.
Nishie, W.
Abe, R.
Akiyama, M.
Shimizu, H.
Title of paper Collagen XVII in hemidesmosomes is involved in keratinocyte-collagen IV adhesion and p38-MAPK-dependent cell migration and signaling
Formatted title
Collagen XVII in hemidesmosomes is involved in keratinocyte-collagen IV adhesion and p38-MAPK-dependent cell migration and signaling
Conference name 39th Annual European Society for Dermatological Research Meeting
Conference location Budapest, Hungary
Conference dates 9-12 September, 2009
Proceedings title Journal of Investigative Dermatology: Proceedings of the 39th Annual European Society for Dermatological Research Meeting   Check publisher's open access policy
Place of Publication Baltimore, MD
Publisher Nature Publishing
Publication Year 2009
DOI 10.1038/jid.2009.232
ISSN 0022-202X
1523-1747
Volume 129
Issue Supplement 2
Start page S80
End page S80
Total pages 1
Language eng
Abstract/Summary Collagen XVII (COL17), a transmembrane collagen, is thought to be involved in keratinocyte adhesion and possibly migration, as COL17 defects disrupt keratinocytebasal lamina adhesion and underlie the disease non-Herlitz junctional epidermolysis bullosa (n-HJEB). COL17 is involved in keratinocyte adhesion and migration. Using siRNA to knockdown COL17 expression in HaCaT cells, we assessed cell characteristics including adhesion, migration and signaling. Control and siRNA transfected keratinocytes showed no difference in adhesion on plastic dishes after incubation for 8 hours in serum-free keratinocyte-growth medium, however when grown on collagen IV alone or BD matrigel (containing collagen IV and laminin isoforms) COL17 defi cient cells showed signifi cantly reduced adhesion compared to controls (P<0.01), and MEK1/2 and MAPK demonstrated reduced phosphorylation in COL17 depleted cells. Furthermore, COL17 defi cient HaCaT cells plated on plastic exhibited reduced motility that was p38MAP kinase dependent (after addition of the p38MAPK inhibitor SB203580). Conversely, keratinocyte adhesion was independent of p38MAPK signaling. Taken together, these results suggest COL17 has signifi cantly wider signaling roles than were previously thought, including the involvement of COL17 in keratinocyte adhesion to collagen IV, in p38MAP kinase-dependent cell migration, and multiple cell signaling events pertaining to MEK1/2 phosphorylation.
Formatted Abstract/Summary
Abstract: Collagen XVII (COL17) participates in keratinocyte adhesion and possibly migration, as COL17 defects disrupt keratinocyte-basal lamina adhesion and underlie the disease non-Herlitz junctional epidermolysis bullosa. Using small interference RNA (siRNA) to knock down COL17 expression in HaCaT cells, we assessed cell characteristics, including adhesion, migration, and signaling. Control and siRNA-transfected keratinocytes showed no difference in adhesion on plastic dishes after incubation for 8 hours in serum-free keratinocyte-growth medium; however, when grown on collagen IV alone or BD matrigel (containing collagen IV and laminin isoforms), COL17-deficient cells showed significantly reduced adhesion compared with controls (P < 0.01), and mitogen-activated protein kinase (MAPK)/ERK kinase (MEK)1/2 and MAPK showed reduced phosphorylation. Furthermore, COL17-deficient HaCaT cells plated on plastic exhibited reduced motility that was p38MAPK-dependent (after addition of the p38MAPK inhibitor SB203580). Together, these results suggest that COL17 has significantly wider signaling roles than were previously thought, including the involvement of COL17 in keratinocyte adhesion to collagen IV, in p38MAPK-dependent cell migration, and multiple cell signaling events pertaining to MEK1/2 phosphorylation.
Subjects 110304 Dermatology
Keyword JUNCTIONAL EPIDERMOLYSIS-BULLOSA
HEMIDESMOSOMES
PHOSPHORYLATION
GROWTH
ECTODOMAIN
EXPRESSION
INTEGRIN
ACTIVATION
MAP KINASES
HAIR-FOLLICLES
Q-Index Code EX
Q-Index Status Provisional Code
Institutional Status Unknown

 
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Created: Mon, 30 Nov 2009, 12:28:18 EST by Michael Affleck on behalf of Faculty Of Health Sciences