Matrix Metalloproteinases of Epithelial Origin in Facial Sebum of Patients with Acne and their Regulation by Isotretinoin Eleni Papakonstantinou, Alexios.

Slides:

Advertisements

Similar presentations

G. J. Fisher, H. -C. Choi, Z. Bata-Csorgo, Yuan Shao, Subhash Datta, Z

Advertisements

Lipodermatosclerosis is Characterized by Elevated Expression and Activation of Matrix Metalloproteinases: Implications for Venous Ulcer Formation Yared.

Volume 57, Issue 1, Pages (January 2000)

Evidence for an exclusive association of matrix metalloproteinase-9 with dysfunctional high-density lipoprotein: A novel finding S. Sini, D. Deepa, S.

SiRNA Knockdown of Tissue Inhibitor of Metalloproteinase-1 in Keloid Fibroblasts Leads to Degradation of Collagen Type I Masayo Aoki, Koichi Miyake,

Treatment of Dermal Fibroblasts with GPI-Anchored Human TIMP-1 Protein Moderates Processes Linked to Scar Formation Roghieh Djafarzadeh, Susan Notohamiprodjo,

Expression of Human Macrophage Metalloelastase (MMP-12) by Tumor Cells in Skin Cancer Erja Kerkelä, Risto Ala-aho, Leila Jeskanen, Oona Rechardt, Reidar.

Volume 57, Issue 1, Pages (January 2000)

Volume 66, Issue 4, Pages (October 2004)

Peroxidated Squalene Induces the Production of Inflammatory Mediators in HaCaT Keratinocytes: A Possible Role in Acne Vulgaris Monica Ottaviani, Theodosis.

Volume 51, Issue 2, Pages (February 2007)

Matrix Metalloproteinase 9 Expression is Coordinately Modulated by the KRE-M9 and 12-O-Tetradecanoyl-Phorbol-13-Acetate Responsive Elements Takashi Kobayashi,

Topical Application of 17β-Estradiol Increases Extracellular Matrix Protein Synthesis by Stimulating TGF-β Signaling in Aged Human Skin In Vivo Eui Dong.

Expression of Protease-Activated Receptor-2 in SZ95 Sebocytes and its Role in Sebaceous Lipogenesis, Inflammation, and Innate Immunity Sang E. Lee, Ji-Min.

Human Skin is a Steroidogenic Tissue: Steroidogenic Enzymes and Cofactors Are Expressed in Epidermis, Normal Sebocytes, and an Immortalized Sebocyte Cell.

Cross-Talk Between RhoGTPases and Stress Activated Kinases for Matrix Metalloproteinase-9 Induction in Response to Keratinocytes Injury Isabelle Bourget,

Expression of Type XVI Collagen in Human Skin Fibroblasts: Enhanced Expression in Fibrotic Skin Diseases Atsushi Akagi, Shingo Tajima, Yutaka Nagai

Interleukin-17 and Interferon-γ Synergize in the Enhancement of Proinflammatory Cytokine Production by Human Keratinocytes Marcel B.M. Teunissen, Jan.

Matrix Metalloproteinase-19 Expression in Dermal Wounds and by Fibroblasts in Culture Niina Hieta, Ulla Impola, Carlos López-Otín, Ulpu Saarialho-Kere,

Coexpression of Integrin αvβ3 and Matrix Metalloproteinase-2 (MMP-2) Coincides with MMP-2 Activation: Correlation with Melanoma Progression Uta B. Hofmann,

Volume 63, Issue 5, Pages (May 2003)

Histamine Contributes to Tissue Remodeling via Periostin Expression

Elastin-Derived Peptides Upregulate Matrix Metalloproteinase-2-ediated Melanoma Cell Invasion Through Elastin-Binding Protein Carole Ntayi, Anne-Laure.

EGF Upregulates, Whereas TGF-β Downregulates, the Hyaluronan Synthases Has2 and Has3 in Organotypic Keratinocyte Cultures: Correlations with Epidermal.

Membrane Type 1 Matrix Metalloproteinase Regulates Cellular Invasiveness and Survival in Cutaneous Epidermal Cells Usha Nagavarapu, Kenneth Relloma,

IGF-II-Mediated COX-2 Gene Expression in Human Keratinocytes Through Extracellular Signal-Regulated Kinase Pathway Hye Jung Kim, Tae-Yoon Kim Journal.

Type II Collagen Accumulation in Overlying Dermo-Epidermal Junction of Pilomatricoma Is Mediated by Bone Morphogenetic Protein 2 and 4 Hideki Mieno,

Analysis of Proteins with Caseinolytic Activity in a Human Stratum Corneum Extract Revealed a Yet Unidentified Cysteine Protease and Identified the So-Called.

Human Keratinocytes Constitutively Express Interleukin-18 and Secrete Biologically Active Interleukin-18 After Treatment with Pro-Inflammatory Mediators.

Stimulation of Purinergic Receptors Modulates Chemokine Expression in Human Keratinocytes Saveria Pastore, Francesca Mascia, Sara Gulinelli, Sylvia Forchap,

Characterization of Group X Phospholipase A2 as the Major Enzyme Secreted by Human Keratinocytes and its Regulation by the Phorbol Ester TPA Gérard Lambeau,

Anti-Inflammatory Activity of Sertaconazole Nitrate Is Mediated via Activation of a p38– COX-2–PGE2 Pathway Runa Sur, Jeffrey M. Babad, Michelle Garay,

Min Qin, Aslan Pirouz, Myung-Hwa Kim, Stephan R. Krutzik, Hermes J

Antibodies Elicited by Inactivated Propionibacterium acnes-Based Vaccines Exert Protective Immunity and Attenuate the IL-8 Production in Human Sebocytes:

Heat Modulation of Tropoelastin, Fibrillin-1, and Matrix Metalloproteinase-12 in Human Skin In Vivo Zhou Chen, Jin Young Seo, Yeon Kyung Kim, Se Rah.

Induction of Adipose Differentiation Related Protein and Neutral Lipid Droplet Accumulation in Keratinocytes by Skin Irritants Emmanuela Corsini, PhD,

Cloning and Characterization of the Expression Pattern of a Novel Splice Product MIA (Splice) of Malignant Melanoma-derived Growth-inhibiting Activity.

Min Qin, Aslan Pirouz, Myung-Hwa Kim, Stephan R. Krutzik, Hermes J

Elastin Peptides Induce Migration and Terminal Differentiation of Cultured Keratinocytes Via 67 kDa Elastin Receptor in Vitro: 67 kDa Elastin Receptor.

Noritaka Oyama, Keiji Iwatsuki, Yoshimi Homma, Fumio Kaneko

Respective Contribution of Neutrophil Elastase and Matrix Metalloproteinase 9 in the Degradation of BP180 (Type XVII Collagen) in Human Bullous Pemphigoid

Takashi Kobayashi, Hiroshi Shinkai

Role of Matrix Metalloproteinases in HaCaT Keratinocytes Apoptosis Induced by Loxosceles Venom Sphingomyelinase D Danielle Paixão-Cavalcante, Carmen.

All-Trans-Retinoic Acid Induces Interleukin-8 via the Nuclear Factor-κB and p38 Mitogen-Activated Protein Kinase Pathways in Normal Human Keratinocytes

Rosiglitazone Inhibits Proliferation, Motility, and Matrix Metalloproteinase Production in Keratinocytes Narasimharao Bhagavathula, Kamalakar C. Nerusu,

Plasmin Triggers Rapid Contraction and Degradation of Fibroblast-Populated Collagen Lattices George D. Pins, Maura E. Collins-Pavao, Livingston Van De.

The Melanocortin 5 Receptor is Expressed in Human Sebaceous Glands and Rat Preputial Cells Diane Thiboutot, Aruntha Sivarajah, Kathryn Gilliland, Zhaoyuan.

Protease-Activated Receptor 2, a Receptor Involved in Melanosome Transfer, is Upregulated in Human Skin by Ultraviolet Irradiation Glynis Scott, Cristina.

Characterization of Keratinocyte Differentiation Induced by Ascorbic Acid: Protein Kinase C Involvement and Vitamin C Homeostasis1 Isabella Savini, Antonello.

Differential Gene Induction of Human β-Defensins (hBD-1, -2, -3, and -4) in Keratinocytes Is Inhibited by Retinoic Acid Jürgen Harder, Ulf Meyer-Hoffert,

Hongli Lin, Xiangmei Chen, Jianzhong Wang, Zhiheng Yu

G. J. Fisher, H. -C. Choi, Z. Bata-Csorgo, Yuan Shao, Subhash Datta, Z

Heat Shock-Induced Matrix Metalloproteinase (MMP)-1 and MMP-3 Are Mediated through ERK and JNK Activation and via an Autocrine Interleukin-6 Loop Chi-Hyun.

Expression and Activation of Matrix Metalloproteinases in Wounds: Modulation by the Tripeptide–Copper Complex Glycyl-L-Histidyl-L-Lysine-Cu2+ Alain Siméon,

Loxosceles Sphingomyelinase Induces Complement-Dependent Dermonecrosis, Neutrophil Infiltration, and Endogenous Gelatinase Expression Denise V. Tambourgi,

Bikunin, a Serine Protease Inhibitor, is Present on the Cell Boundary of Epidermis Cui Chang-Yi, Yoshinori Aragane, Akira Maeda, Piao Yu-Lan, Masae Takahashi,

Collagen Synthesis Is Suppressed in Dermal Fibroblasts by the Human Antimicrobial Peptide LL-37 Hyun Jeong Park, Dae Ho Cho, Hee Jung Kim, Jun Young.

Tiziana De Angelis, Adele Noè, Mitali Chatterjee, Joy Mulholland

Corticotropin-Releasing Hormone (CRH) Downregulates Interleukin-18 Expression in Human HaCaT Keratinocytes by Activation of p38 Mitogen-Activated Protein.

Volume 56, Issue 5, Pages (November 1999)

Expression of Opsin Molecule in Cultured Murine Melanocyte

Myeloid Differentiation Factor 88 Regulates Basal and UV-Induced Expressions of IL-6 and MMP-1 in Human Epidermal Keratinocytes Youngae Lee, Hyunjung.

Distinct Strains of Propionibacterium acnes Induce Selective Human β-Defensin-2 and Interleukin-8 Expression in Human Keratinocytes Through Toll-Like.

PADMA 28: A Multi-Component Herbal Preparation with Retinoid-Like Dermal Activity but Without Epidermal Effects Muhammad Nadeem Aslam, Helene Fligiel,

Expression of Matrix Metalloproteinase-13 Is Controlled by IL-13 via PI3K/Akt3 and PKC-δ in Normal Human Dermal Fibroblasts Chikako Moriya, Masatoshi.

Relationship Between Cell-Associated Matrix Metalloproteinase 9 and Psoriatic Keratinocyte Growth Nathalie Buisson-Legendre, Hervé Emonard, Philippe.

Effects of Hepatocyte Growth Factor on the Expression of Type I Collagen and Matrix Metalloproteinase-1 in Normal and Scleroderma Dermal Fibroblasts

Increased Migration of Murine Keratinocytes Under Hypoxia Is Mediated by Induction of Urokinase Plasminogen Activator Richard J. Daniel, Richard W. Groves,

Doxycycline Indirectly Inhibits Proteolytic Activation of Tryptic Kallikrein-Related Peptidases and Activation of Cathelicidin Kimberly N. Kanada, Teruaki.

Matrix Metalloproteinase Inhibitor BB-3103 Unlike the Serine Proteinase Inhibitor Aprotinin Abrogates Epidermal Healing of Human Skin Wounds Ex Vivo1

Presentation transcript:

Matrix Metalloproteinases of Epithelial Origin in Facial Sebum of Patients with Acne and their Regulation by Isotretinoin Eleni Papakonstantinou, Alexios J. Aletras, Evelyn Glass, Panagiotis Tsogas, Alexander Dionyssopoulos, James Adjaye, Sabine Fimmel, Panagiotis Gouvousis, Ralf Herwig, Hans Lehrach, Christos C. Zouboulis, George Karakiulakis Journal of Investigative Dermatology Volume 125, Issue 4, Pages 673-684 (October 2005) DOI: 10.1111/j.0022-202X.2005.23848.x Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 1 Gelatinase activity is reduced in sebum of facial acne lesions in a time-dependent manner during therapy with isotretinoin. (a) Representative gelatin zymography in aliquots of sebum (5 μg of protein) during systemic per os (lanes 4–6) and topical (lanes 7–9) treatment with isotretinoin. Arrows indicated pre-stained standard protein molecular weight markers (lane 1): phosphorylase b (97.4 kDa), bovine serum albumin (66.2 kDa), L-glutamic dehydrogenase (55.0 kDa), and ovalbumin (42.7 kDa). Lane 2: migration of purified promatrix metalloproteinase (proMMP)-2 (72 kDa); lane 3: proMMP-9 (92 kDa); lanes 4 and 7: 0 d samples; lanes 5 and 8: 30 d samples; lanes 6 and 9: 60 d samples. (b) Quantitative analysis of gelatinolytic activity in sebum following systemic per os (n=23) or topical (n=36) treatment of acne patients with isotretinoin using a computer-supported image analysis program. Each bar represents the mean±SD from n specimens. Statistical significance: *p<0.05; ***p<0.01 as compared with 0 d samples, which were regarded as 100% gelatinolytic activity. Journal of Investigative Dermatology 2005 125, 673-684DOI: (10.1111/j.0022-202X.2005.23848.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 2 Western blot analysis of gelatinases in sebum samples indicates the presence of matrix metalloproteinase (MMP)-9 but not of MMP-2. (a) Representative western blot analysis of sebum during systemic per os treatment with isotretinoin. Analysis was performed using human MMP-2 antiserum: lane 1: purified promatrix metalloproteinase (proMMP)-2 (72.0 kDa), lane 2, 0 d sample; lane 3, 30 d sample, and human MMP-9 antiserum: lane 4, 0 d sample; lane 5, 30 d sample. Arrow on the right indicates the reference sample of proMMP-9 (94.0 kDa), which has been previously fully characterized from human periprosthetic tissue of loose hip endoprostheses. Arrows on the left indicate molecular weight size markers (phosphorylase b, 97.4 kDa; bovine serum albumin, 66.2 kDa; L-glutamic dehydrogenase, 55.0 kDa). (b) Quantitative analysis of western blots of MMP-9 immunoreactive bands of sebum following systemic per os treatment of acne patients (n=23) with isotretinoin for 30 d, using a computer-supported image analysis program. Each bar represents the mean±SD from n specimens. Statistical significance: *p<0.05; ***p<0.01 as compared with 0 d samples. Journal of Investigative Dermatology 2005 125, 673-684DOI: (10.1111/j.0022-202X.2005.23848.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 3 Isotretinoin does not influence gelatinase in vitro. (a) Sebum samples (0 d, corresponding to 5 μg protein) were preincubated with isotretinoin (0–1 mM) for 30 min at room temperature and subjected to gelatin zymography, as described in Materials and Methods. Lane 4, 0 mM; lane 5, 0.01 mM; lane 6, 0.1 mM; lane 7, 1 mM. (b) Commercially available purified promatrix metalloproteinase (proMMP)-2 and proMMP-9 (1 ng protein) were treated as above. ProMMP-2: lane 4, 01 mM; lane 5, 1 mM. ProMMP-9: lane 6, 0.1 mM; lane 7, 1 mM, lane 7. Arrows and lane 1 indicate molecular weight markers: phosphorylase b (97.4 kDa), bovine serum albumin (66.2 kDa), L-glutamic dehydrogenase (55.0 kDa), ovalbumin (42.7 kDa), and aldolase (40.0 kDa). Lane 2: purified proMMP-2 (72 kDa) and lane 3 purified proMMP-9 (92 kDa). Journal of Investigative Dermatology 2005 125, 673-684DOI: (10.1111/j.0022-202X.2005.23848.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 4 Matrix metalloproteinase (MMP)-1 and MMP-13 are expressed in sebum of facial acne lesions, and MMP-13 expression is reduced during isotretinoin treatment. (a) Representative western blot analysis of sebum during topical treatment with isotretinoin using polyclonal antibodies for MMP-1. Lane 1 and arrows on the left: immunoreactive bands from reference samples of promatrix metalloproteinase (proMMP)-1 (52.4 kDa) and MMP-1 (45.0 and 43.5 kDa), which have been fully characterized previously from human periprosthetic tissue of loose hip endoprostheses. Lane 2: immunoreactive bands of 0 d sebum samples. Lane 3: immunoreactive bands of 30 d sebum samples following topical treatment with isotretinoin. Lane 4 and arrows on the right indicate protein molecular weight markers: bovine serum albumin (66.2 kDa), ovalbumin (42.7 kDa), and soybean trypsin ihibitor (21.5 kDa). (b) Representative western blot analysis of sebum during topical treatment with isotretinoin using polyclonal antibodies for MMP-13. Lane 1 and arrows on the left indicate protein molecular weight markers: bovine serum albumin (66.2 kDa), ovalbumin (42.7 kDa) and soybean trypsin ihibitor (21.5 kDa). Lane 2: immunoreactive bands of 0 d sebum samples. Lane 3: immunoreactive bands of 30 d sebum samples following topical treatment with isotretinoin. Lane 4 and arrows on the right: immunoreactive bands from reference samples of proMMP-13 (65.0 kDa) and MMP-13 (52.0 kDa) from human periprosthetic tissue. (c) Aliquots of sebum samples were assessed for MMP-1 and MMP-13 by ELISA, prior to and following per os (n=23) and topical (n=36) treatment of acne patients with isotretinoin, for 30 and 60 d. Each bar represents the mean±SD of triplicate determinations from n samples. Statistical significance: **p<0.02 as compared with 0 d sample. Journal of Investigative Dermatology 2005 125, 673-684DOI: (10.1111/j.0022-202X.2005.23848.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 5 Tissue inhibitor of matrix metalloproteinase (TIMP)-1 and -2 are expressed in sebum samples of facial acne lesions but are not influenced during isotretinoin treatment. TIMP were measured by ELISA in aliquots of sebum specimens (2 μg of protein) during per os treatment of 23 acne patients and topical treatment of 36 acne patients with isotretinoin for 0, 30, and 60 d. Each bar represents the mean±SD of triplicate determinations from n specimens. Journal of Investigative Dermatology 2005 125, 673-684DOI: (10.1111/j.0022-202X.2005.23848.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 6 HaCaT keratinocytes and SZ95 sebocytes secrete promatrix metalloproteinase pro(MMP)-2 and -9, which are upregulated by arachidonic acid and downregulated by isotretinoin. Representative gelatin zymographies from the cell culture medium of HaCaT keratinocytes (a) and SZ95 sebocytes (c), incubated for 24 h. Lanes 1: untreated (control), lanes 2: arachidonic acid (AA; 10-4 M), lanes 3: isotretinoin (Iso; 10-8 M), lanes 4: isotretinoin (10-7 M), lanes 5: arachidonic acid (10-4 M)+isotretinoin (10-8 M), lanes 6: AA (10-4 M)+isotretinoin (10-7 M), lanes 7: untreated (control), lanes 8: N-ethyl-maleimide (NEM, 5 mM), lanes 9: Na2EDTA (EDTA, 20 mM), and lanes 10: 1,10-phenanthroline (Phen, 4 mM). Arrows indicate proMMP-9 (92 kDa), proMMP-2 (72 kDa), and MMP-2 (64 kDa). Quantitative analysis of the gelatinolytic activity present in the culture media from cell cultures of HaCaT keratinocytes (b) and SZ95 sebocytes (d). Each bar represents the mean±SD from 4 zymograms. Statistical significance: *p<0.05; **p<0.02, ***p<0.01, as compared with control (untreated cells) (), or with AA alone []. Iso, isotretinoin; AA, (10-4 M). Journal of Investigative Dermatology 2005 125, 673-684DOI: (10.1111/j.0022-202X.2005.23848.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 7 Matrix metalloproteinase (MMP)-1 is secreted by HaCaT keratinocytes and upregulated by arachidonic acid. Aliquots of supernatants from HaCaT keratinocytes incubated for 12–48 h were assessed for MMP-1 by ELISA. Each bar represents the mean±SD of triplicate determinations from four assays. Iso, isotretinoin, AA, arachidonic acid (10-4 M). Statistical significance: *p<0.05; **p<0.02, as compared with control (untreated cells). Journal of Investigative Dermatology 2005 125, 673-684DOI: (10.1111/j.0022-202X.2005.23848.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions

Figure 8 HaCaT keratinocytes express mRNA for matrix metalloproteinase (MMP) and tissue inhibitor of matrix metalloproteinase (TIMP)-1, and isotretinoin inhibits MMP-9 and MMP-13 de novo and arachidonic acid-induced mRNA. Quantitative analysis of chemiluminescence of RT-PCR analyses of HaCaT keratinocytes incubated in the absence or in the presence of isotretinoin (10-7 M, 24 h) using primers for MMP-1, MMP-9, MMP-13, and TIMP-1, as described under “Materials and Methods”. Each bar represents the mean±SD from four assays. Statistical significance: *p<0.05; AA, arachidonic acid, 10-4 M; Iso, isotretinoin, 10-7 M. Inset: Representative analysis of chemiluminescence of RT-PCR analyses of HaCaT keratinocytes incubated in the absence or in the presence of isotretinoin (10-7 M, 24 h) using primers for MMP-13. GAPDH of expected size 263 bp was used as an internal standard. The expected size of the reaction product for MMP-13 is indicated by the arrow. Lane 1, DNA ladder (100 bp); lane 2, untreated; lane 3, AA (10-4 M); lane 4, isotretinoin (10-7 M); and lane 5, AA (10-4 M) and isotretinoin (10-7 M). Journal of Investigative Dermatology 2005 125, 673-684DOI: (10.1111/j.0022-202X.2005.23848.x) Copyright © 2005 The Society for Investigative Dermatology, Inc Terms and Conditions