The Extracellular Matrix: An Overview
The extracellular matrix encompasses the very large number of constituent macromolecules that are synthesized and secreted by cells into the space surrounding them, followed in most cases by further assembly, cross-linking, and/or polymerization of the secreted proteins to form an organized structure. The extracellular matrix has a number of critical roles in tissue and organ development, function, and repair after injury. In addition, there are numerous serious and debilitating genetic diseases whose bases lie in mutations in genes encoding extracellular matrix proteins. There are also acquired diseases, such as scurvy, chronic obstructive pulmonary disease, and cancer, that can be caused by damage to or are influenced by changes in the organization or integrity of the extracellular matrix. The goal of this chapter is to provide an overview of the extracellular matrix by discussing the different classes of extracellular matrix molecules and presenting a subset of individual extracellular matrix proteins from each class in greater detail in order to demonstrate their importance.
KeywordsBasement membrane collagen laminin proteoglycan elastic fiber bone fibrosis
This work was supported by R01DK078314 and R01GM060432 (both to JHM).
- Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, Engel J, Engvall E, Hohenester E, Jones JC, Kleinman HK, Marinkovich MP, Martin GR, Mayer U, Meneguzzi G, Miner JH, Miyazaki K, Patarroyo M, Paulsson M, Quaranta V, Sanes JR, Sasaki T, Sekiguchi K, Sorokin LM, Talts JF, Tryggvason K, Uitto J, Virtanen I, von der Mark K, Wewer UM, Yamada Y, Yurchenco PD (2005) A simplified laminin nomenclature. Matrix Biol 24:326–332CrossRefPubMedGoogle Scholar
- Hynes R (1999) Fibronectins. In: Kreis T, Vale R (eds) Guidebook to the extracellular matrix, anchor, and adhesion proteins. Oxford University Press, New York, pp 422–425Google Scholar
- Kobayashi N, Kostka G, Garbe JH, Keene DR, Bachinger HP, Hanisch FG, Markova D, Tsuda T, Timpl R, Chu ML, Sasaki T (2007) A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization. J Biol Chem 282:11805–11816CrossRefPubMedGoogle Scholar
- Le Goff C, Somerville RP, Kesteloot F, Powell K, Birk DE, Colige AC, Apte SS (2006) Regulation of procollagen amino-propeptide processing during mouse embryogenesis by specialization of homologous ADAMTS proteases: insights on collagen biosynthesis and dermatosparaxis. Development 133:1587–1596CrossRefPubMedGoogle Scholar
- Mecham R (1999) Elastin. In: Kreis T, Vale R (eds) Guidebook to the extracellular matrix, anchor, and adhesion proteins. Oxford University Press, New York, pp 414–417Google Scholar
- Metcalfe K, Rucka AK, Smoot L, Hofstadler G, Tuzler G, McKeown P, Siu V, Rauch A, Dean J, Dennis N, Ellis I, Reardon W, Cytrynbaum C, Osborne L, Yates JR, Read AP, Donnai D, Tassabehji M (2000) Elastin: mutational spectrum in supravalvular aortic stenosis. Eur J Hum Genet 8:955–963CrossRefPubMedGoogle Scholar
- Ninomiya Y, Kagawa M, Iyama K, Naito I, Kishiro Y, Seyer JM, Sugimoto M, Oohashi T, Sado Y (1995) Differential expression of two basement membrane collagen genes, COL4A6 and COL4A5, demonstrated by immunofluorescence staining using peptide-specific monoclonal antibodies. J Cell Biol 130:1219–1229CrossRefPubMedGoogle Scholar
- Olsen BR, Ninomiya Y (1999a) Collagens: overview of the family. In: Kreis T, Vale R (eds) Guidebook to the extracellular matrix, anchor, and adhesion proteins. Oxford University Press, New York, pp 380–383Google Scholar
- Olsen BR, Ninomiya Y (1999b) Fibrillar collagens. In: Kreis T, Vale R (eds) Guidebook to the extracellular matrix, anchor, and adhesion proteins. Oxford University Press, New York, pp 383–387Google Scholar
- Plaisier E, Gribouval O, Alamowitch S, Mougenot B, Prost C, Verpont MC, Marro B, Desmettre T, Cohen SY, Roullet E, Dracon M, Fardeau M, Van Agtmael T, Kerjaschki D, Antignac C, Ronco P (2007) COL4A1 mutations and hereditary angiopathy, nephropathy, aneurysms, and muscle cramps. N Engl J Med 357:2687–2695CrossRefPubMedGoogle Scholar
- Ricard-Blum S, Ruggiero F (2005) The collagen superfamily: from the extracellular matrix to the cell membrane. Pathol Biol (Paris) 53:430–442Google Scholar
- Sakai T, Johnson KJ, Murozono M, Sakai K, Magnuson MA, Wieloch T, Cronberg T, Isshiki A, Erickson HP, Fassler R (2001) Plasma fibronectin supports neuronal survival and reduces brain injury following transient focal cerebral ischemia but is not essential for skin-wound healing and hemostasis. Nat Med 7:324–330CrossRefPubMedGoogle Scholar