title: Molecular composition and function of integrin-based collagen glues-introducing COLINBRIs.
abstract: BACKGROUND
  Despite detailed knowledge about the structure and signaling properties of individual collagen receptors, much remains to be learned about how these receptors participate in linking cells to fibrillar collagen matrices in tissues. In addition to collagen-binding integrins, a group of proteins with affinity both for fibrillar collagens and integrins link these two protein families together. We have introduced the name COLINBRI (COLlagen INtegrin BRIdging) for this set of molecules. Whereas collagens are the major building blocks in tissues and defects in these structural proteins have severe consequences for tissue integrity, the mild phenotypes of the integrin type of collagen receptors have raised questions about their importance in tissue biology and pathology.
  
  
  METHODS
  We will discuss the two types of cell linkages to fibrillar collagen (direct- versus indirect COLINBRI-mediated) and discuss how the parallel existence of direct and indirect linkages to collagens may ensure tissue integrity.
  
  
  CONCLUSIONS
  The observed mild phenotypes of mice deficient in collagen-binding integrins and the relatively restricted availability of integrin-binding sequences in mature fibrillar collagen matrices support the existence of indirect collagen-binding mechanisms in parallel with direct collagen binding in vivo.
  
  
  CONCLUSIONS
  A continued focus on understanding the molecular details of cell adhesion mechanisms to collagens will be important and will benefit our understanding of diseases like tissue- and tumor fibrosis where collagen dynamics are disturbed. This article is part of a Special Issue entitled Matrix-mediated cell behaviour and properties.
authors.affiliation: Department of Biomedicine and Centre for Cancer Biomarkers, Norwegian Centre of Excellence, University of Bergen, Jonas Lies vei 91, N-5009 Bergen, Norway.
authors.forename: Cédric
authors.initials: C
authors.lastname: Zeltz
authors.affiliation: Departments of Biology, Physics and Biomedical Engineering, Pritzker Institute of Biomedical Science and Engineering, Illinois Institute of Technology, 3440 S. Dearborn Ave, Chicago, IL 60616, USA.
authors.forename: Joseph
authors.initials: J
authors.lastname: Orgel
authors.affiliation: Department of Biomedicine and Centre for Cancer Biomarkers, Norwegian Centre of Excellence, University of Bergen, Jonas Lies vei 91, N-5009 Bergen, Norway. Electronic address: donald.gullberg@biomed.uib.no.
authors.forename: Donald
authors.initials: D
authors.lastname: Gullberg
mesh_terms: D000269:Adhesives / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D002448:Cell Adhesion; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D016023:Integrins / Q000737:chemistry* / Q000378:metabolism*; D010641:Phenotype; D011485:Protein Binding
chemical_list: D000269:Adhesives; D016023:Integrins; D003094:Collagen
keywords: COLINBRI; Collagen integrin bridging molecule; Collagen-binding integrin; Fibrillar collagen