In Vivo Evidence for a Bridging Role of a Collagen V Subtype at the Epidermis–Dermis Interface Christelle Bonod-Bidaud, Muriel Roulet, Uwe Hansen, Ahmed.

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In Vivo Evidence for a Bridging Role of a Collagen V Subtype at the Epidermis–Dermis Interface Christelle Bonod-Bidaud, Muriel Roulet, Uwe Hansen, Ahmed Elsheikh, Marilyne Malbouyres, Sylvie Ricard-Blum, Clément Faye, Elisabeth Vaganay, Patricia Rousselle, Florence Ruggiero Journal of Investigative Dermatology Volume 132, Issue 7, Pages 1841-1849 (July 2012) DOI: 10.1038/jid.2012.56 Copyright © 2012 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 1 Transgene expression. (a, b) Skin was dissected from 17.5d.p.c. (days post coitum) and 5-day-old mice, both wild-type (WT) and transgenic (Tg). (a) The epidermis (Ep) was separated from the dermis (D). Reverse-transcriptase (RT)-PCR was performed with specific primers on (a) the dermis and epidermis or (b) total skin. (c) Immunoblot analysis of human proα1(V) and mouse proα2(V) expression in 17.5d.p.c. skin embryos. Membranes were probed with (left) 13F6 antibody or with (right) polyclonal antibodies that recognize the murine proα2(V) chain. (d) Crude extracts (lanes 2 and 4) and isolated suprastructural fragments (lanes 1 and 3) from mouse skin. bp, bead pellet; ce, crude extract. Journal of Investigative Dermatology 2012 132, 1841-1849DOI: (10.1038/jid.2012.56) Copyright © 2012 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 2 Analysis of skin structure and ultrastructure. (a) Immunolocalization of the transgene using the monoclonal 18G5 antibody in (left panel) 5-day-old wild-type (WT) and (right panel) transgenic mice (K14-COL5A1). (b, upper panel) Masson's trichrome staining of skin cross-sections of 5-day-old WT and transgenic mice. (b, lower panel) Light microscope micrographs of depilated 5-day-old epidermis and histogram of hair follicle counting. **P<0.01. (c, d) Ultrastructural analysis of 17.5d.p.c. (days post coitum) (left) and 5-day-old (right) transgenic and WT mouse skin. (c) Asterisks indicate lacunae in the basal layer of the transgenic epidermis; arrows show the accumulation of dense unstriated fibrillar material underneath the basement membrane in transgenic skin compared with WT. (d) Arrows indicate hemidesmosomes. Histogram of hemidesmosome (HD) counting, ***P<0.001. Fb, fibroblast; Ke, keratinocyte. Journal of Investigative Dermatology 2012 132, 1841-1849DOI: (10.1038/jid.2012.56) Copyright © 2012 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 3 Analysis of skin by immunogold electron microscopy. Ultrastructural analysis of the skin from (a) wild-type and (b–d) transgenic mice and hair follicles of (e, f) transgenic mice by using an antibody against human proα1(V) chain. Arrowheads indicate representative gold particles. BM, basement membrane; fib, dermal collagen fibrils; hs, hair shaft. Bar=200nm. Journal of Investigative Dermatology 2012 132, 1841-1849DOI: (10.1038/jid.2012.56) Copyright © 2012 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 4 Analysis of biomechanical properties of 1-month-old mouse skin. (a) Stress/strain behavior of mouse skin. (b) Splitting tests results. Journal of Investigative Dermatology 2012 132, 1841-1849DOI: (10.1038/jid.2012.56) Copyright © 2012 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 5 Binding partners of collagen V. (a) Transmission electron microscope (TEM) analysis of suprastructures isolated with superparamagnetic immunobeads. (A, B) Double labeling with antibodies against collagen VI (large gold particles, black arrowheads) and the human proα1(V) chain (small gold particles, white arrowheads). (C) Double labeling with antibodies against laminin-γ-1 chain (black arrowheads) and the human proα1(V) chain (white arrowheads). (D, E) Double labeling with antibodies against collagen IV (large gold particles, black arrowheads) and the human proα1(V) chain (small gold particles, white arrowheads). (F) Double labeling with antibodies against tenascin-X (large gold particles, black arrowheads) and the human proα1(V) chain (small gold particles, white arrowheads). Bp, superparamagnetic immunobeads. Bar=100nm. (b) Surface plasmon resonance (SPR) assays. Top: Injection of soluble pepsinized collagens IV and VI over spotted recombinant collagen V homotrimer. Bottom: Interactions between immobilized recombinant domains of collagen V and collagens IV and VI. (c) Solid-phase binding assays. Soluble lanimin-111 binding to immobilized recombinant collagen V homotrimer (pN[α1(V)]3 and N-propeptide (Nα1(V)). OD, optical density. (d) Diagram showing the organization and location of collagen V subtypes (homotrimer vs. heterotrimer) expressed in skin. Journal of Investigative Dermatology 2012 132, 1841-1849DOI: (10.1038/jid.2012.56) Copyright © 2012 The Society for Investigative Dermatology, Inc Terms and Conditions