Basement membranes.
Basement membranes are thin, specialized extracellular matrices surrounding most tissues in all metazoans. The compositions and functions of basement membranes have generally been well conserved throughout the subkingdom. Genetic analyses of basement membrane components in C. elegans have provided insights into their assembly and functions during development. Immuno- or GFP-tagged localization studies have shown that basement membranes on different tissues, or even sub-regions of tissues, contain different sets of proteins or alternatively spliced isoforms of them. Several components, including laminin, perlecan, type IV collagen and possibly osteonectin/SPARC, are essential for completion of embryogenesis, being necessary for tissue organization and structural integrity. In contrast, type XVIII collagen and nidogen are not required for viability but primarily influence organization of the nervous system. All of these proteins, with the exception of nidogen and the addition of fibulin, have roles of varying degree in morphogenesis of the gonad. A major family of cellular receptors for basement membrane proteins, the integrins, have also been characterized in C. elegans. As one might expect, integrins have been shown to function in many of the same processes as their potential ligands, the basement membrane components. While much remains to be explored, studies of basement membranes in C. elegans have been highly informative and hold great promise for improving our understanding of how these structures are assembled and how they function in development.
Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, IL 60611, USA. jkramer@northwestern.edu
James M
JM
Kramer
D000818:Animals; D001485:Basement Membrane / Q000502:physiology*; D017173:Caenorhabditis elegans / Q000502:physiology*; D029742:Caenorhabditis elegans Proteins / Q000502:physiology; D002135:Calcium-Binding Proteins / Q000502:physiology; D003094:Collagen / Q000502:physiology; D019812:Heparan Sulfate Proteoglycans / Q000502:physiology; D006801:Humans; D016023:Integrins / Q000502:physiology; D007797:Laminin / Q000502:physiology; D008562:Membrane Glycoproteins / Q000502:physiology; D008565:Membrane Proteins / Q000502:physiology; D015676:Osteonectin / Q000502:physiology; D017474:Receptors, Laminin / Q000502:physiology
D029742:Caenorhabditis elegans Proteins; D002135:Calcium-Binding Proteins; D019812:Heparan Sulfate Proteoglycans; D016023:Integrins; D007797:Laminin; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D015676:Osteonectin; D017474:Receptors, Laminin; C060820:fibulin; C424064:him-4 protein, C elegans; C029967:nidogen; C071927:perlecan; D003094:Collagen