Matrilysin-2 (Matrix Metalloproteinase-26) Is Upregulated in Keratinocytes During Wound Repair and Early Skin Carcinogenesis Katja Ahokas, Tiina Skoog,

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Matrilysin-2 (Matrix Metalloproteinase-26) Is Upregulated in Keratinocytes During Wound Repair and Early Skin Carcinogenesis Katja Ahokas, Tiina Skoog, Sari Suomela, Leila Jeskanen, Ulla Impola, Keiichi Isaka, Ulpu Saarialho-Kere Journal of Investigative Dermatology Volume 124, Issue 4, Pages 849-856 (April 2005) DOI: 10.1111/j.0022-202X.2005.23640.x Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 1 Matrix metalloproteinase (MMP)-26 is expressed in keratinocyte (KC) during wound repair. (A) Immunostaining for MMP-26 in a normally healing 2 d wound. (B) Immunostaining for laminin-5 in a serial section. (C) Immunostaining for MMP-9 does not co-localize with MMP-26. Also MMP-9-positive neutrophils are seen. Arrows depict positive KC and U the location of the wound. (D) Immunostaining for MMP-26 in a chronic wound. (E) MMP-26 is positive in KC on top of rete ridges in psoriasis. (F) Immunostaining for MMP-26 in a sample of lichen planus. (G) Occasional expression for MMP-26 protein in seborrhoeic keratosis. (H) MMP-26 is expressed in anagen hair follicles, but not in normal skin. Scale bars: 25 μm (A–C); 125 μm (D and H); 50 μm (E–G). Journal of Investigative Dermatology 2005 124, 849-856DOI: (10.1111/j.0022-202X.2005.23640.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 2 Matrix metalloproteinase (MMP)-26 and p16 co-localize in wounds but not in dedifferentiated cancers. (A) Staining for MMP-26. (B) p16 in an acute wound. (C) Staining for MMP-26. (D) p16 in Bowen's disease. (E) Staining for MMP-26. (F) p16 in a microinvasive squamous cell cancer (SCC). (G) Staining for MMP-26. (H) p16 in serial sections of a grade II SCC. Arrows depict corresponding spots. Scale bars: 25 μm (A, B); 50 μm (C–F); 125 μm (G, H). Journal of Investigative Dermatology 2005 124, 849-856DOI: (10.1111/j.0022-202X.2005.23640.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 3 Matrix metalloproteinase (MMP)-26 is expressed in actinic keratosis, but does not co-localize with the proliferation marker Ki-67. (A) MMP-26 is expressed in keratinocytes with atypia in actinic keratosis. (B) Immunostaining for MMP-26 in a basal cell cancer. (C) Serial section stained with E-cadherin. (D) The proliferation marker Ki-67. Arrows depict corresponding spots. Scale bars: 50 μm (A); 25 μm (B–D). Journal of Investigative Dermatology 2005 124, 849-856DOI: (10.1111/j.0022-202X.2005.23640.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 4 Matrix metalloproteinase (MMP)-26 expression disappears along with cancer dedifferentiation. (A) MMP-26 staining in a microinvasive squamous cell cancer (SCC). (B) Serial section stained for elastin. (C) MMP-26 staining in a grade I SCC. (D) Serial section stained with laminin-5 (LN-5). (E) Higher magnification of MMP-26. (F) LN-5-positive cells in a grade II SCC. (G) Grade III SCC showing absence of MMP-26 from dedifferentiated tumor cell islands. (H, I) Serial sections of a grade II SCC stained for MMP-26 and MMP-9. Arrows depict corresponding regions. Scale bars: 125 μm (A–D, G); 50 μm (E, F); 25 μm (H, I). Journal of Investigative Dermatology 2005 124, 849-856DOI: (10.1111/j.0022-202X.2005.23640.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 5 Matrix metalloproteinase (MMP)-26 protein is expressed by cultured keratinocyte (KC). (A) HaCaT cells cultured on type I collagen. (B) Negative control with pre-immune serum. (C) Positive A-431 squamous cancer cells. (D) Primary KC grown on fibronectin. (E) KC cultured in DMEM. Cells were cultured on LabTek chamber slides, aminoethylcarbazole was used as chromogenic substrate and counterstaining was performed with hematoxylin. Scale bars: 25 μm (A, B); 12.5 μm (C); 50 μm (D, E). Journal of Investigative Dermatology 2005 124, 849-856DOI: (10.1111/j.0022-202X.2005.23640.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 6 Matrix metalloproteinase (MMP)-26 mRNA expression in cultured keratinocytes, placenta, and testis. (A) MMP-26 mRNA expression is low in unstimulated primary keratinocyte (KC) and HaCaT cells. Primary keratinocytes were cultured and supplemented as described in Materials and Methods. Total RNA was extracted, reverse transcribed, and analyzed by real-time quantitative RT-PCR (Applied Biosystems) using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as endogenous control. Results are shown relative to mRNA levels from control primary KC, assigned the value 1. (B) Expression of MMP-26 (upper lane) and GAPDH (lower lane) in transformed (HaCaT) and primary KC by RT-PCR. HaCaT cells and normal keratinocytes were cultured as described above. Total RNA was reverse transcribed to cDNA and reverse transcriptase PCR was performed. Journal of Investigative Dermatology 2005 124, 849-856DOI: (10.1111/j.0022-202X.2005.23640.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions