Overview of Extracellular Matrix

Robert P. Mecham1

1 Washington University School of Medicine, St. Louis, Missouri
Publication Name:  Current Protocols in Cell Biology
Unit Number:  Unit 10.1
DOI:  10.1002/0471143030.cb1001s57
Online Posting Date:  December, 2012
GO TO THE FULL TEXT: PDF or HTML at Wiley Online Library

Abstract

The extracellular matrix provides an environment for cells. It is produced, assembled, and modified by cells and in turn, it modifies the functions and behavior of the cells it encounters. The molecules that make up the matrix are diverse in both structure and function. This well‐illustrated unit provides an introduction to the structure and function of the major components of the extracellular matrix and serves as a background for the other units in the chapter, which include protocols for isolation and analysis of individual components. Curr. Protoc. Cell Biol. 57:10.1.1‐10.1.16. © 2012 by John Wiley & Sons, Inc.

Keywords: cell biology; extracellular matrix; adhesion

     
 
GO TO THE FULL PROTOCOL:
PDF or HTML at Wiley Online Library

Table of Contents

  • Introduction
  • Collagens
  • Elastin and Microfibrillar Proteins
  • Adhesive Glycoproteins
  • Matricellular Proteins
  • Proteoglycans
  • Conclusions
  • Literature Cited
  • Figures
     
 
GO TO THE FULL PROTOCOL:
PDF or HTML at Wiley Online Library

Materials

GO TO THE FULL PROTOCOL:
PDF or HTML at Wiley Online Library

Figures

Videos

Literature Cited

Literature Cited
   Adams, J.C. and Lawler, J. 2011. The thrombospondins. Cold Spring Harbor Perspect. Biol. 3:a009712.
   Aumailley, M., Bruckner‐Tuderman, L., Carter, W.G., Deutzmann, R., Edgar, D., Ekblom, P., Engel, J., Engvall, E., Hohenester, E., Jones, J.C., Kleinman, H.K., Marinkovich, M.P., Martin, G.R., Mayer, U., Meneguzzi, G., Miner, J.H., Miyazaki, K., Patarroyo, M., Paulsson, M., Quaranta, V., Sanes, J.R., Sasaki, T., Sekiguchi, K., Sorokin, L.M., Talts, J.F., Tryggvason, K., Uitto, J., Virtanen, I., von der Mark, K., Wewer, U.M., Yamada, Y., and Yurchenco, P.D. 2005. A simplified laminin nomenclature. Matrix Biol. 24:326‐332.
   Aumailley, M., Gimond, C., and Rousselle, P. 1996. Integrin‐mediated cellular interactions with laminins. In The Laminins (P. Ekblom and R. Timpl, eds.) pp. 127‐158. Harwood Academic Publishers, New York.
   Baldock, C., Sherratt, M.J., Shuttleworth, C.A., and Kielty, C.M. 2003. The supramolecular organization of collagen VI microfibrils. J. Mol. Biol. 330:297‐307.
   Beck, K., Hunter, I., and Engel, J. 1990. Structure and function of laminin: Anatomy of a multidomain glycoprotein. FASEB J. 4:148‐160.
   Beecher, N., Roseman, A.M., Jowitt, T.A., Berry, R., Troilo, H., Kammerer, R.A., Shuttleworth, C.A., Kielty, C.M., and Baldock, C. 2011. Collagen VI, conformation of A‐domain arrays and microfibril architecture. J. Biol. Chem. 286:40266‐40275.
   Belkin, A.M. and Stepp, M.A. 2000. Integrins as receptors for laminins. Microsc. Res. Tech. 51:280‐301.
   Birk, D.E. and Bruckner, P. 2011. Collagens, suprastructures, and collagen fibril assembly. In Extracellular Matrix: An Overview (R.P. Mecham, ed.) pp. 77‐115. Springer‐Verlag, Berlin.
   Bornstein, P. and Sage, E.H. 2002. Matricellular proteins: Extracellular modulators of cell function. Curr. Opin. Cell Biol. 14:608‐616.
   Brodsky, B. and Ramshaw, J.A. 1997. The collagen triple‐helix structure. Matrix Biol. 15:545‐554.
   Burgeson, R.E. 1993. Type VII collagen, anchoring fibrils, and epidermolysis bullosa. J. Invest. Dermatol. 101:252‐255.
   Chautard, E., Fatoux‐Ardore, M., Ballut, L., Thierry‐Mieg, N., and Ricard‐Blum, S. 2011. MatrixDB, the extracellular matrix interaction database. Nucleic Acids Res. 39:D235‐D240.
   Chiquet‐Ehrismann, R. and Tucker, R.P. 2011. Tenascins and the importance of adhesion modulation. Cold Spring Harbor Perspect. Biol. 3:a004960.
   Choi, Y., Chung, H., Jung, H., Couchman, J.R., and Oh, E.S. 2011. Syndecans as cell surface receptors: Unique structure equates with functional diversity. Matrix Biol. 30:93‐99.
   Ekblom, P. and Timpl, R. 1996. The Laminins. Harwood Academic Publishers, New York.
   Engel, J. and Chiquet, M. 2011. An overview of extracellular matrix structure and function. In The Extracellular Matrix: An Overview (R.P. Mecham, ed.) pp. 1‐39. Springer‐Verlag, Berlin.
   Erickson, H.P. 1993. Tenascin‐C, tenasin‐R, tenascin‐X: A family of talented proteins in search of functions. Curr. Opin. Cell Biol. 5:869‐876.
   Esposito, C. and Caputo, I. 2005. Mammalian transglutaminases. Identification of substrates as a key to physiological function and physiopathological relevance. FEBS J. 272:615‐631.
   Eyre, D.R., Weis, M.A., and Wu, J.J. 2008. Advances in collagen cross‐link analysis. Methods 45:65‐74.
   Filmus, J., Capurro, M., and Rast, J. 2008. Glypicans. Genome Biol. 9:224.
   Franzke, C.W., Tasanen, K., Schumann, H., and Bruckner‐Tuderman, L. 2003. Collagenous transmembrane proteins: Collagen XVII as a prototype. Matrix Biol. 22:299‐309.
   Franzke, C.W., Bruckner, P., and Bruckner‐Tuderman, L. 2005. Collagenous transmembrane proteins: Recent insights into biology and pathology. J. Biol. Chem. 280:4005‐4008.
   Gorres, K.L. and Raines, R.T. 2010. Prolyl 4‐hydroxylase. Crit. Rev. Biochem. Mol. Biol. 45:106‐124.
   Hassell, J.R., Blochberger, T.C., Rada, J.A., Chakravarti, S., and Noonan, D. 1993. Proteoglycan gene families. In Extracellular Matrix (H.K. Kleinman, ed.) pp. 69‐113. JAI Press, New York.
   Hubmacher, D. and Reinhardt, D.P. 2011. Microfibrils and fibrillin. In The Extracellular Matrix: an Overview (R.P. Mecham, ed.) pp. 233‐265. Springer, Berlin.
   Hynes, R.O. and Yamada, K.M. 2012. Extracellular Matrix Biology. Cold Spring Harbor Laboratory Press, New York.
   Hynes, R.O. and Naba, A. 2012. Overview of the matrisome—An inventory of extracellular matrix constituents and functions. Cold Spring Harbor Perspect. Biol. 4:a004903.
   Iozzo, R.V., and Sanderson, R.D. 2011. Proteoglycans in cancer biology, tumour microenvironment and angiogenesis. J. Cell. Mol. Med. 15:1013‐1031.
   Iozzo, R.V., Cohen, I.R., Grässel, S., and Murdoch, A.D. 1994. The biology of perlecan: The multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices. Biochem. J. 302:625‐639.
   Iozzo, R.V., Zoeller, J.J., and Nystrom, A. 2009. Basement membrane proteoglycans: Modulators par excellence of cancer growth and angiogenesis. Mol. Cells 27:503‐513.
   Iozzo, R.V., Goldoni, S., Berendsen, A.D., and Young, M.F. 2011. Small leucine‐rich proteoglycans. In The Extracellular Matrix: An Overview (R. P. Mecham, ed.) pp. 197‐231. Springer, Berlin.
   Kadler, K. 1994. Extracellular matrix 1: Fibril‐forming collagens. Protein Profile 1:519‐638.
   Kessler, E., Takahara, K., Biniaminov, L., Brusel, M., and Greenspan, D.S. 1996. Bone morphogenetic protein‐1: The type I procollagen C‐proteinase. Science 271:360‐362.
   Khoshnoodi, J., Pedchenko, V., and Hudson, B.G. 2008. Mammalian collagen IV. Microsc. Res. Tech. 71:357‐370.
   Kielty, C.M., Sherratt, M.J., and Shuttleworth, C.A. 2002. Elastic fibres. J. Cell Sci. 115:2817‐2828.
   Kivirikko, K.I. and Myllyharju, J. 1998. Prolyl 4‐hydroxylases and their protein disulfide isomerase subunit. Matrix Biol. 16:357‐368.
   Koivu, J., Myllylä, R., Helaakoski, T., Pihlajaniemi, T., Tasanen, K., and Kivirikko, K.I. 1987. A single polypeptide acts both as the β subunit of prolyl 4‐hydroxylase and as a protein disulfide‐isomerase. J. Biol. Chem. 262:6447‐6449.
   Kozel, B.A., Mecham, R.P., and Rosenbloom, J. 2011. Elastin. In The Extracellular Matrix: An Overview (R.P. Mecham, ed.) pp. 267‐301. Springer, Berlin.
   Kühn, K. 1987. The classical collagens: Types I, II, and III. In Structure and Function of Collagen Types (R. Mayne and R.E. Burgeson, eds.) pp. 1‐42. Academic Press, San Diego.
   Kwan, A.P., Cummings, C.E., Chapman, J.A., and Grant, M.E. 1991. Macromolecular organization of chicken type X collagen in vitro. J. Cell Biol. 114:597‐604.
   Li, D., Clark, C.C., and Myers, J.C. 2000. Basement membrane zone type XV collagen is a disulfide‐bonded chondroitin sulfate proteoglycan in human tissues and cultured cells. J. Biol. Chem. 275:22339‐22347.
   Maurer, P. and Engel, J. 1996. Structure of laminins and their chain assembly. In The Laminins (P. Ekblom and R. Timpl, eds.) pp. 27‐49. Harwood Academic Publishers, New York.
   Mayer, U. and Timpl, R. 1994. Nidogen: A versatile binding protein of basement membranes. In Extracellular Matrix Assembly and Structure (P.D. Yurchenco, D.E. Birk, and R.P. Mecham, eds.) pp. 318‐416. Academic Press, San Diego.
   Mayne, R. and Brewton, R.G. 1993. New members of the collagen superfamily. Curr. Opin. Struct. Biol. 5:883‐890.
   McLaughlin, P.J., Chen, Q., Horiguchi, M., Starcher, B.C., Stanton, J.B., Broekelmann, T.J., Marmorstein, A.D., McKay, B., Mecham, R., Nakamura, T., and Marmorstein, L.Y. 2006. Targeted disruption of fibulin‐4 abolishes elastogenesis and causes perinatal lethality in mice. Mol. Cell Biol. 26:1700‐1709.
   Mecham, R.P. 2011. The Extracellular Matrix: An Overview. Springer‐Verlag, Berlin.
   Mecham, R.P. and Hinek, A. 1996. Non‐integrin laminin receptors. In The Laminins (P. Ekblom and R. Timpl, eds.) pp. 159‐183. Harwood Academic Publishers, New York.
   Miner, J.H. 2011. Basement membranes. In The Extracellular Matrix: An Overview (R.P. Mecham, ed.) pp. 117‐145. Springer, Berlin.
   Myllyla, R., Wang, C., Heikkinen, J., Juffer, A., Lampela, O., Risteli, M., Ruotsalainen, H., Salo, A., and Sipila, L. 2007. Expanding the lysyl hydroxylase toolbox: New insights into the localization and activities of lysyl hydroxylase 3 (LH3). J. Cell Physiol. 212:323‐329.
   Naba, A., Clauser, K.R., Hoersch, S., Liu, H., Carr, S.A., and Hynes, R.O. 2012. The matrisome: In silico definition and in vivo characterization by proteomics of normal and tumor extracellular matrices. Mol. Cell Proteomics 11:M111.014647.
   Nakamura, T., Lozano, P.R., Ikeda, Y., Iwanaga, Y., Hinek, A., Minamisawa, S., Cheng, C.F., Kobuke, K., Dalton, N., Takada, Y., Tashiro, K., Ross, J. Jr., Honjo, T., and Chien, K.R. 2002. Fibulin‐5/DANCE is essential for elastogenesis in vivo. Nature 415:171‐175.
   Olsen, B.R., Winterhalter, K.H., and Gordon, M.K. 1995. FACIT collagens and their biological roles. Trends Glycos. Glycotech. 7:115‐127.
   Partridge, S.M. 1962. Elastin. Adv. Prot. Chem. 17:227‐302.
   Partridge, S.M. 1986. Reflections on a career. In Regulation of Matrix Accumulation (R.P. Mecham, ed.) pp. 1‐28. Academic Press, New York.
   Piez, K.A. 1997. History of extracellular matrix: A personal view. Matrix Biol. 16:85‐92.
   Potts, J.R. and Campbell, I.D. 1994. Fibronectin structure and assembly. Curr. Opin. Cell Biol. 6:648‐655.
   Prockop, D.J. and Kivirikko, K.I. 1995. Collagens: Molecular biology, disease, and potential therapy. Annu. Rev. Biochem. 64:403‐434.
   Ramirez, F. and Dietz, H.C. 2009. Extracellular microfibrils in vertebrate development and disease processes. J. Biol. Chem. 284:14677‐14681.
   Rauch, U., Karthikeyan, L., Maurel, P., Margolis, R.U., and Margolis, R.K. 1992. Cloning and primary structure of neurocan, a developmentally regulated, aggregating chondroitin sulfate proteoglycan of brain. J. Biol. Chem. 267:19536‐19547.
   Rehn, M. and Pihlajaniemi, T. 1994. Alpha 1(XVIII), a collagen chain with frequent interruptions in the collagenous sequence, a distinct tissue distribution, and homology with type XV collagen. Proc. Natl. Acad. Sci. U.S.A. 91:4234‐4238.
   Ricard‐Blum, S. 2011. The collagen family. Cold Spring Harbor Perspect. Biol. 3:a004978.
   Roberts, D.D. and Lau, L.F. 2011. Matricellular proteins. In The Extracellular Matrix: An Overview (R.P. Mecham, ed.) pp. 369‐413. Springer, Berlin.
   Schaefer, L. and Iozzo, R.V. 2008. Biological functions of the small leucine‐rich proteoglycans: From genetics to signal transduction. J. Biol. Chem. 283:21305‐21309.
   Schwartz, N.B. and Domowicz, M. 2004. Proteoglycans in brain development. Glycoconj. J. 21:329‐341.
   Schwarzbauer, J.E. and DeSimone, D.W. 2011. Fibronectins, their fibrillogenesis, and in vivo functions. Cold Spring Harbor Perspect. Biol. 3:a005041.
   Shoulders, M.D. and Raines, R.T. 2009. Collagen structure and stability. Annu. Rev. Biochem. 78:929‐958.
   Starcher, B., Green, M., and Scott, M. 1995. Measurement of urinary desmosine as an indicator of acute pulmonary disease. Respiration 3:a005041.
   Stephan, S., Sherratt, M.J., Hodson, N., Shuttleworth, C.A., and Kielty, C.M. 2004. Expression and supramolecular assembly of recombinant alpha1(viii) and alpha2(viii) collagen homotrimers. J. Biol. Chem. 279:21469‐21477.
   Timpl, R. 1996. Macromolecular organization of basement membranes. Curr. Opin. Cell Biol. 8:618‐624.
   Timpl, R. and Chu, M.L. 1994. Microfibrillar collagen type VI. In Extracellular Matrix Assembly (P.D. Yurchenco, D.E. Birk, and R.P. Mecham, eds.) pp. 207‐242. Academic Press, San Diego.
   Wagenseil, J.E. and Mecham, R.P. 2009. Vascular extracellular matrix and arterial mechanics. Physiol. Rev. 89:957‐989.
   Weinbaum, J.S., Broekelmann, T.J., Pierce, R.A., Werneck, C.C., Segade, F., Craft, C.S., Knutsen, R.H., and Mecham, R.P. 2008. Deficiency in microfibril‐associated glycoprotein‐1 leads to complex phenotypes in multiple organ systems. J. Biol. Chem. 283:25533‐25543.
   Wight, T.N. 2002. Versican: A versatile extracellular matrix proteoglycan in cell biology. Curr. Opin. Cell Biol. 14:617‐623.
   Wight, T.N., Toole, B.P., and Hascall, V.C. 2011. Hyaluronana and the aggregating proteoglycans. In The Extracellular Matrix: An Overview (R.P. Mecham, ed.) pp. 147‐149. Springer, Berlin.
   Xu, J. and Mosher, D.F. 2011. Fibronectin and other adhesive glycoproteins. In The Extracellular Matrix: An Overview (R.P. Mecham, ed.) p. 41‐75. Springer, Berlin.
   Yamada, H., Watanabe, K., Shimonaka, M., and Yamaguchi, Y. 1994. Molecular cloning of brevican, a novel brain proteoglycan of the aggrecan/versican family. J. Biol. Chem. 269:10119‐10126.
   Yanagisawa, H., Davis, E.C., Starcher, B.C., Ouchi, T., Yanagisawa, M., Richardson, J.A., and Olson, E.N. 2002. Fibulin‐5 is an elastin‐binding protein essential for elastic fibre development in vivo. Nature 415:168‐171.
   Yurchenco, P.D. 2011. Basement membranes: Cell scaffoldings and signaling platforms. Cold Spring Harbor Perspect. Biol. 3:a004911.
   Zanetti, M., Braghetta, P., Sabatelli, P., Mura, I., Doliana, R., Colombatti, A., Volpin, D., Bonaldo, P., and Bressan, G.M. 2004. EMILIN‐1 deficiency induces elastogenesis and vascular cell defects. Mol. Cell Biol. 24:638‐650.
   Zimmermann, D.R. and Ruoslahti, E. 1989. Multiple domains of the large fibroblast proteoglycan, versican. EMBO J. 8:2975‐2981.
GO TO THE FULL PROTOCOL:
PDF or HTML at Wiley Online Library