Cartilage Oligomeric Matrix Protein Increases in Photodamaged Skin
| Autor: | Keigo Kawabata, Akira Ozawa, Shingo Sakai, Ayumi Kusaka-Kikushima, Susumu Takekoshi, Masaki Kobayashi, Tomotaka Mabuchi, Muneo Miyasaka, Yoshinori Sugiyama |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
musculoskeletal diseases
0301 basic medicine Adult Male Pathology medicine.medical_specialty Ultraviolet Rays Photoaging Immunoelectron microscopy Dermatology Cartilage Oligomeric Matrix Protein Real-Time Polymerase Chain Reaction Biochemistry Severity of Illness Index 030207 dermatology & venereal diseases 03 medical and health sciences Young Adult 0302 clinical medicine Keloid Dermis Japan Reference Values Transforming Growth Factor beta medicine Ultraviolet light Humans Microscopy Immunoelectron Molecular Biology In Situ Hybridization Aged Cartilage oligomeric matrix protein Aged 80 and over integumentary system biology Chemistry Papillary dermis Biopsy Needle Cell Biology Middle Aged medicine.disease Immunohistochemistry Skin Aging 030104 developmental biology medicine.anatomical_structure biology.protein Female Reticular Dermis Biomarkers |
| Zdroj: | The Journal of investigative dermatology. 136(6) |
| ISSN: | 1523-1747 |
| Popis: | Cartilage oligomeric matrix protein (COMP) is a structural component of cartilage. Recent studies have described COMP as a pathogenic factor that promotes collagen deposition in fibrotic skin disorders such as scleroderma and keloid skin. Although collagen, a major dermis component, is thought to decrease in photoaged skin, recent reports have demonstrated the presence of tightly packed collagen fibrils with a structural resemblance to fibrosis in the papillary dermis of photoaged skin. Here we examined how photoaging damage relates to COMP expression and localization in photoaged skin. In situ hybridization revealed an increase in COMP-mRNA-positive cells with the progress of photoaging in preauricular skin (sun-exposed skin). The signal intensity of immunostaining for COMP increased with photoaging in not only the papillary dermis but also the reticular dermis affected by advancing solar elastosis. Immunoelectron microscopy detected the colocalization of COMP with both elastotic materials and collagen fibrils in photoaged skin. Ultraviolet light A irradiation of human dermal fibroblasts induced COMP expression at both the mRNA and protein levels. Ultraviolet light A-induced COMP expression was inhibited by an anti-transforming growth factor-β antibody or SB431542, an activin receptor-like kinase 5 inhibitor. These results suggest that the transforming growth factor-β-mediated upregulation of COMP expression may contribute to the modulation of dermal extracellular matrix in the photoaging process. |
| Databáze: | OpenAIRE |
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