title: Type XIX collagen: A new partner in the interactions between tumor cells and their microenvironment.
abstract: Type XIX collagen is a minor collagen that is associated with the basement membrane zone that belongs to the FACIT family (Fibril-Associated Collagens with Interrupted Triple helices). The FACIT family is composed of type IX, XII, XIV, XVI, XX, XXI, XXII and XIX collagens, which share many highly conserved structural motifs: a short NC1 domain, a thrombospondin-like N-terminal domain (TSPN), and numerous cysteine residues. The main role of FACITs is to ensure the integrity and stability of the extracellular matrix and its fibrillar collagen network by regulating the formation and size of the collagen fibrils. Type XIX collagen was discovered in a human rhabdomyosarcoma cell line. The collagen α1(XIX) chain is composed of 5 triple-helical domains (COL) interrupted by 6 non-triple-helical (NC) domains with a short, C-terminal, 19 amino acid non-collagenous domain (NC1). This collagen is involved in the differentiation of muscle cells, central nervous system development, and formation of the esophagus. Type XIX collagen is associated with the basement membrane zone, like type XVIII and XV collagens. Its short NC1(XIX) C-terminal domain inhibits the migration and invasion of melanoma cells. It also exerts a strong anti-angiogenic effect by inhibiting MMP-14 and VEGF expression. NC1(XIX) binding to αvβ3 integrin decreases the phosphorylation of proteins involved in the FAK (Focal Adhesion Kinase)/PI3K (PhosphoInositide 3-Kinase)/Akt (protein kinase B)/mTOR (Mammalian Target Of Rapamycin) pathway. On the other hand, NC1(XIX) induces an increase in GSK3β activity by decreasing its level of phosphorylation. The inhibition of this pathway could explain the anti-tumor properties of the NC1(XIX) domain.
authors.affiliation: Université de Reims Champagne-Ardenne, CNRS UMR 7369 (Matrice Extracellulaire et Dynamique Cellulaire, MEDyC), 51095 Reims, France; CHU de Reims, Laboratoire Central de Biochimie, 51092 Reims, France.
authors.forename: Jean-Baptiste
authors.initials: JB
authors.lastname: Oudart
authors.affiliation: Université de Reims Champagne-Ardenne, CNRS UMR 7369 (Matrice Extracellulaire et Dynamique Cellulaire, MEDyC), 51095 Reims, France; CHU de Reims, Laboratoire Central de Biochimie, 51092 Reims, France.
authors.forename: Jean-Claude
authors.initials: JC
authors.lastname: Monboisse
authors.affiliation: Université de Reims Champagne-Ardenne, CNRS UMR 7369 (Matrice Extracellulaire et Dynamique Cellulaire, MEDyC), 51095 Reims, France; CHU de Reims, Laboratoire Central de Biochimie, 51092 Reims, France.
authors.forename: François-Xavier
authors.initials: FX
authors.lastname: Maquart
authors.affiliation: Université de Reims Champagne-Ardenne, CNRS UMR 7369 (Matrice Extracellulaire et Dynamique Cellulaire, MEDyC), 51095 Reims, France.
authors.forename: Bertrand
authors.initials: B
authors.lastname: Brassart
authors.affiliation: Université de Reims Champagne-Ardenne, CNRS UMR 7369 (Matrice Extracellulaire et Dynamique Cellulaire, MEDyC), 51095 Reims, France.
authors.forename: Sylvie
authors.initials: S
authors.lastname: Brassart-Pasco
authors.affiliation: Université de Reims Champagne-Ardenne, CNRS UMR 7369 (Matrice Extracellulaire et Dynamique Cellulaire, MEDyC), 51095 Reims, France; CHU de Reims, Laboratoire Central de Biochimie, 51092 Reims, France. Electronic address: lramont@chu-reims.fr.
authors.forename: Laurent
authors.initials: L
authors.lastname: Ramont
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000378:metabolism* / Q000473:pathology; D045744:Cell Line, Tumor; D003094:Collagen / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D051417:Focal Adhesion Kinase 1 / Q000235:genetics / Q000378:metabolism; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D039482:Integrin alpha5 / Q000235:genetics / Q000378:metabolism; D053511:Matrix Metalloproteinase 14 / Q000235:genetics / Q000378:metabolism; D019869:Phosphatidylinositol 3-Kinases / Q000235:genetics / Q000378:metabolism; D000072417:Protein Domains; D017433:Protein Structure, Secondary; D051057:Proto-Oncogene Proteins c-akt / Q000235:genetics / Q000378:metabolism; D012208:Rhabdomyosarcoma / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D015398:Signal Transduction; D012983:Soft Tissue Neoplasms / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D058570:TOR Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism; D059016:Tumor Microenvironment / Q000235:genetics*; D042461:Vascular Endothelial Growth Factor A / Q000235:genetics / Q000378:metabolism
chemical_list: D003094:Collagen; D051417:Focal Adhesion Kinase 1; D039482:Integrin alpha5; D053511:Matrix Metalloproteinase 14; D019869:Phosphatidylinositol 3-Kinases; D051057:Proto-Oncogene Proteins c-akt; D058570:TOR Serine-Threonine Kinases; D042461:Vascular Endothelial Growth Factor A; C467484:VEGFA protein, human; C000612264:collagen XIX protein, human; C546842:MTOR protein, human; C496050:PTK2 protein, human
keywords: FACIT; Integrin; Matrikine; NC1 domain; Signal transduction; Tumor invasion; Type XIX collagen