title: Collagen XII and XIV, new partners of cartilage oligomeric matrix protein in the skin extracellular matrix suprastructure.
abstract: The tensile and scaffolding properties of skin rely on the complex extracellular matrix (ECM) that surrounds cells, vasculature, nerves, and adnexus structures and supports the epidermis. In the skin, collagen I fibrils are the major structural component of the dermal ECM, decorated by proteoglycans and by fibril-associated collagens with interrupted triple helices such as collagens XII and XIV. Here we show that the cartilage oligomeric matrix protein (COMP), an abundant component of cartilage ECM, is expressed in healthy human skin. COMP expression is detected in the dermal compartment of skin and in cultured fibroblasts, whereas epidermis and HaCaT cells are negative. In addition to binding collagen I, COMP binds to collagens XII and XIV via their C-terminal collagenous domains. All three proteins codistribute in a characteristic narrow zone in the superficial papillary dermis of healthy human skin. Ultrastructural analysis by immunogold labeling confirmed colocalization and further revealed the presence of COMP along with collagens XII and XIV in anchoring plaques. On the basis of these observations, we postulate that COMP functions as an adapter protein in human skin, similar to its function in cartilage ECM, by organizing collagen I fibrils into a suprastructure, mainly in the vicinity of anchoring plaques that stabilize the cohesion between the upper dermis and the basement membrane zone.
authors.affiliation: Department of Dermatology, University of Cologne, Cologne 50937, Germany.
authors.forename: Pallavi
authors.initials: P
authors.lastname: Agarwal
authors.forename: Daniela
authors.initials: D
authors.lastname: Zwolanek
authors.forename: Douglas R
authors.initials: DR
authors.lastname: Keene
authors.forename: Jan-Niklas
authors.initials: JN
authors.lastname: Schulz
authors.forename: Katrin
authors.initials: K
authors.lastname: Blumbach
authors.forename: Dick
authors.initials: D
authors.lastname: Heinegård
authors.forename: Frank
authors.initials: F
authors.lastname: Zaucke
authors.forename: Mats
authors.initials: M
authors.lastname: Paulsson
authors.forename: Thomas
authors.initials: T
authors.lastname: Krieg
authors.forename: Manuel
authors.initials: M
authors.lastname: Koch
authors.forename: Beate
authors.initials: B
authors.lastname: Eckes
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D064236:Cartilage Oligomeric Matrix Protein; D002675:Child, Preschool; D003094:Collagen / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D024042:Collagen Type I / Q000235:genetics / Q000378:metabolism; D024082:Collagen Type XII / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020405:Dermis / Q000378:metabolism* / Q000648:ultrastructure; D005109:Extracellular Matrix / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D057809:HEK293 Cells; D006801:Humans; D007223:Infant; D015603:Keratinocytes / Q000378:metabolism; D064235:Matrilin Proteins; D051379:Mice; D016253:Microscopy, Immunoelectron; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D020349:Surface Plasmon Resonance
chemical_list: C547160:COL12A1 protein, human; C054447:COL14A1 protein, human; D064236:Cartilage Oligomeric Matrix Protein; C504563:Col14a1 protein, mouse; D024042:Collagen Type I; D024082:Collagen Type XII; D016326:Extracellular Matrix Proteins; D006023:Glycoproteins; C577540:Matn1 protein, mouse; D064235:Matrilin Proteins; D011994:Recombinant Proteins; C577553:TSP5 protein, human; D003094:Collagen