Advertisement

Structure of Hemidesmosomes and the Epidermal Basement Membrane Zone

  • Iana TurcanEmail author
  • Marcel F. Jonkman
Chapter

Abstract

Hemidesmosomes are complex, multiprotein structures that mediate the attachment of epithelial cells to the underlying basement membrane. While providing mechanical attachment, these adhesion units are extremely dynamic. They play a significant role in signaling pathways involved in the various important cell functions, such as differentiation, wound healing, and survival. Structurally, hemidesmosomes contain the following molecules: plectin (over 500 kDa protein), BP230 (230 kDa antigen, also known as BPAG1), integrin α6β4, and BP180 (180 kDa protein, also known as BPAG2 or type XVII collagen, and CD151 (protein of tetraspan superfamily). The epidermal basement membrane zone can be viewed as a thin sheet of matrix underlying the basal epithelial cells. It consists of lamina lucida and lamina densa, mainly containing laminin and type IV collagen networks. Type VII collagen which enters into the composition of semicircular anchoring fibrils provide the attachment to the papillary dermis underneath the lamina densa of the basement membrane. When molecules in hemidesmosomes or in the basement membrane zone become target of autoantibodies, a particular acquired subepidermal autoimmune bullous disease (sAIBD) will develop.

Keywords

Hemidesmosome Dermal-epidermal junction Basement membrane zone Autoimmune disease Pemphigoid 

References

  1. 1.
    Koster J, van Wilpe S, Kuikman I, Litjens SH, Sonnenberg A. Role of binding of plectin to the integrin beta4 subunit in the assembly of hemidesmosomes. Mol Biol Cell. 2004;15:1211–23.CrossRefPubMedPubMedCentralGoogle Scholar
  2. 2.
    Buijsrogge JJ, de Jong MC, Kloosterhuis GJ, Vermeer MH, Koster J, Sonnenberg A, Jonkman MF, Pas HH. Antiplectin autoantibodies in subepidermal blistering diseases. Br J Dermatol. 2009;161:762–71.CrossRefPubMedGoogle Scholar
  3. 3.
    Koster J, Geerts D, Favre B, Borradori L, Sonnenberg A. Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly. J Cell Sci. 2003;116:387–99.CrossRefPubMedGoogle Scholar
  4. 4.
    Leung CL, Zheng M, Prater SM, Liem RK. The BPAG1 locus: alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles. J Cell Biol. 2001;154:691–7.CrossRefPubMedPubMedCentralGoogle Scholar
  5. 5.
    Hashmi S, Marinkovich MP. Molecular organization of the basement membrane zone. Clin Dermatol. 2011;29:398–411.CrossRefPubMedGoogle Scholar
  6. 6.
    Borradori L, Sonnenberg A. Structure and function of hemidesmosomes: more than simple adhesion complexes. J Invest Dermatol. 1999;112:411–8.CrossRefPubMedGoogle Scholar
  7. 7.
    Turcan I, Jonkman MF. Blistering disease: insight from the hemidesmosome and other components of the dermal-epidermal junction. Cell Tissue Res. 2015;360:545–69.Google Scholar
  8. 8.
    Pierce RA, Griffin GL, Mudd MS, Moxley MA, Longmore WJ, Sanes JR, Miner JH, Senior RM. Expression of laminin alpha3, alpha4, and alpha5 chains by alveolar epithelial cells and fibroblasts. Am J Respir Cell Mol Biol. 1998;19:237–44.CrossRefPubMedGoogle Scholar
  9. 9.
    Rousselle P, Beck K. Laminin 332 processing impacts cellular behavior. Cell Adh Migr. 2013;7:122–34.CrossRefPubMedPubMedCentralGoogle Scholar
  10. 10.
    Uitto J, Pulkkinen L, Christiano AM. Molecular basis of the dystrophic and junctional forms of epidermolysis bullosa: mutations in the type VII collagen and kalinin (laminin 5) genes. J Invest Dermatol. 1994;103:39S–46.CrossRefPubMedGoogle Scholar

Additional Reading

  1. Walko G, Castanon MJ, Wiche G. Molecular architecture and function of the hemidesmosome. Cell Tissue Res. 2014;360(3):529–44.CrossRefGoogle Scholar

Copyright information

© Springer International Publishing Switzerland 2016

Authors and Affiliations

  1. 1.Department of DermatologyCenter for Blistering Diseases, University Medical Center Groningen, University of GroningenGroningenthe Netherlands

Personalised recommendations