title: [Dermis collagens: beyond their structural properties].
abstract: The extracellular matrix is a complex network composed of macromolecules such as collagens, proteoglycans and elastin that strongly interact with each other and with cells to maintain the structural integrity of many tissues. These interactions also sustain important cell programs such as migration, proliferation, differentiation and apoptosis. The skin, and more specifically the dermis, contains an extreme diversity of macromolecules that reflects the importance of the composition and organization of the matrix components in providing physical properties and function of the tissues. The most abundant matrix components are the collagens that form a super-family of 27 different members which are divided into different subgroups. The fibrillar collagens, types I, III and V, the FACIT collagens, types XII, XIV and XVI, and collagen VI are all expressed in the collagen-rich dermis. Although the structural features of these collagens are now well characterized, their functions remain elusive. Mutations in human collagen genes give rise to numerous connective tissue diseases including dermis disorders. For example, clinical manifestations in the classical Elhers-Danlos syndrome caused by collagen V gene mutations occur predominantly in the dermis. However, the genotype-phenotype relationship is not clearly established as well as the relation between the distribution and the function of the collagens in dermis. There is no doubt that the ongoing and future work using in vivo approaches will provide new cues regarding the function of collagens in dermis.
authors.affiliation: Institut de Biologie et Chimie des Protéines, UMR CNRS 5086, IFR 128 BioSciences Lyon-Gerland, 7, passage du Vercors, 69367 Lyon cedex 07.
authors.forename: Florence
authors.initials: F
authors.lastname: Ruggiero
authors.forename: Muriel
authors.initials: M
authors.lastname: Roulet
authors.forename: Christelle
authors.initials: C
authors.lastname: Bonod-Bidaud
mesh_terms: D051722:ADAM Proteins / Q000172:deficiency / Q000378:metabolism; D000071121:ADAMTS4 Protein; D000818:Animals; D003094:Collagen / Q000737:chemistry / Q000145:classification / Q000502:physiology*; D003095:Collagen Diseases / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D020405:Dermis / Q000737:chemistry*; D004195:Disease Models, Animal; D004535:Ehlers-Danlos Syndrome / Q000378:metabolism / Q000473:pathology; D005109:Extracellular Matrix / Q000737:chemistry / Q000502:physiology; D005838:Genotype; D006801:Humans; D051379:Mice; D018345:Mice, Knockout; D010013:Osteogenesis Imperfecta / Q000235:genetics / Q000378:metabolism; D010641:Phenotype; D010748:Phosphopeptides / Q000378:metabolism; D011347:Procollagen / Q000378:metabolism; D011348:Procollagen N-Endopeptidase / Q000172:deficiency / Q000378:metabolism; D020033:Protein Isoforms / Q000737:chemistry / Q000502:physiology; D013329:Structure-Activity Relationship
chemical_list: C062121:N-propeptide type I collagen; D010748:Phosphopeptides; D011347:Procollagen; D020033:Protein Isoforms; D003094:Collagen; D051722:ADAM Proteins; D011348:Procollagen N-Endopeptidase; D000071121:ADAMTS4 Protein