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. Author manuscript; available in PMC: 2010 Oct 13.

Published in final edited form as: Sci Transl Med. 2010 Mar 17;2(23):23ra20. doi: 10.1126/scitranslmed.3000488

(A) Cell attachment (upper panel) and spreading (lower panel) of FS2 dermal fibroblasts (left panel) and VB6 keratinocytes (right panel) adherent on recombinant wild-type and mutant cbEGF22-TB4-cbEGF23 W1570C and C1564S protein constructs. Wild-type cbEGF22-TB4-cbEGF23 was used as a positive control and BSA as negative control. In contrast to FS2 cells, similar attachment and spreading profiles were observed for VB6 cells plated onto wild-type and mutant fragments. Data are expressed as mean ±S.D. (attachment, n=9; spreading, n=5), from three independent experiments. (B) Assessment of phosphorylated focal adhesion kinase protein (phosphorylation at Y397) at steady state comparing six controls and four SSS patients. Quantification shows decreased pFAK in SSS.

(A) Cell attachment (upper panel) and spreading (lower panel) of FS2 dermal fibroblasts (left panel) and VB6 keratinocytes (right panel) adherent on recombinant wild-type and mutant cbEGF22-TB4-cbEGF23 W1570C and C1564S protein constructs. Wild-type cbEGF22-TB4-cbEGF23 was used as a positive control and BSA as negative control. In contrast to FS2 cells, similar attachment and spreading profiles were observed for VB6 cells plated onto wild-type and mutant fragments. Data are expressed as mean ±S.D. (attachment, n=9; spreading, n=5), from three independent experiments. (B) Assessment of phosphorylated focal adhesion kinase protein (phosphorylation at Y397) at steady state comparing six controls and four SSS patients. Quantification shows decreased pFAK in SSS.