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Gene Review

lam-1  -  Protein LAM-1

Caenorhabditis elegans

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Disease relevance of laminin


High impact information on laminin

  • UNC-6 netrin, a laminin-related protein secreted from neuroglia and neurons along the ventral midline, orients migrating cells and pioneering growth cones on the nematode epidermis [2].
  • Basement membrane assembly is a cooperative process in which laminins polymerize through their LN domains and anchor to the cell surface through their G domains; this leads to cell signaling through integrins and dystroglycan (and possibly other receptors) recruited to the adherent laminin [3].
  • Recent observations suggest that specific laminin and netrin members have developmental functions that are highly conserved across species [3].
  • The first domain is unique to the unc-52 polypeptide, whereas the three remaining domains contain sequences found in the LDL receptor (domain II) laminin (domain III) and N-CAM (domain IV) [4].
  • Netrins are laminin-related proteins that guide circumferential migrations on the ectoderm [5].

Biological context of laminin

  • The defects resemble those of epi-1 laminin alphaB mutants, suggesting that DGN-1 serves as a receptor for laminin. dgn-1(0)/+ animals are fertile but show gonad migration defects in addition to the defects seen in homozygotes, indicating that DGN-1 function is dosage sensitive [6].
  • This is a large complex protein with regions similar to low-density lipoprotein receptors, laminin and neural cell-adhesion molecules [7].

Anatomical context of laminin

  • The results suggest a receptor-mediated process localizes each secreted laminin to exposed cell surfaces and that laminin is crucial for organizing extracellular matrix, receptor and intracellular proteins at those surfaces [8].
  • Dystroglycan is a novel laminin receptor that links the extracellular matrix and sarcolemma in skeletal muscle [9].
  • Recombinant MTP-1 was catalytically active and digested a range of native and denatured connective tissue substrates, including gelatin, collagen, laminin, and fibronectin [10].
  • Recent advances in the characterization of genetic disruptions in humans, mice, nematodes and flies have revealed developmental roles for the different laminin subunits in diverse cell types, affecting differentiation from blastocyst formation to the post-natal period [11].


  1. The childhood muscular dystrophies: making order out of chaos. Tsao, C.Y., Mendell, J.R. Seminars in neurology. (1999) [Pubmed]
  2. UNC-40, a C. elegans homolog of DCC (Deleted in Colorectal Cancer), is required in motile cells responding to UNC-6 netrin cues. Chan, S.S., Zheng, H., Su, M.W., Wilk, R., Killeen, M.T., Hedgecock, E.M., Culotti, J.G. Cell (1996) [Pubmed]
  3. Assembly and tissue functions of early embryonic laminins and netrins. Yurchenco, P.D., Wadsworth, W.G. Curr. Opin. Cell Biol. (2004) [Pubmed]
  4. Products of the unc-52 gene in Caenorhabditis elegans are homologous to the core protein of the mammalian basement membrane heparan sulfate proteoglycan. Rogalski, T.M., Williams, B.D., Mullen, G.P., Moerman, D.G. Genes Dev. (1993) [Pubmed]
  5. Neuroglia and pioneer neurons express UNC-6 to provide global and local netrin cues for guiding migrations in C. elegans. Wadsworth, W.G., Bhatt, H., Hedgecock, E.M. Neuron (1996) [Pubmed]
  6. C. elegans dystroglycan DGN-1 functions in epithelia and neurons, but not muscle, and independently of dystrophin. Johnson, R.P., Kang, S.H., Kramer, J.M. Development (2006) [Pubmed]
  7. UNC-52/perlecan isoform diversity and function in Caenorhabditis elegans. Rogalski, T.M., Mullen, G.P., Bush, J.A., Gilchrist, E.J., Moerman, D.G. Biochem. Soc. Trans. (2001) [Pubmed]
  8. Laminin alpha subunits and their role in C. elegans development. Huang, C.C., Hall, D.H., Hedgecock, E.M., Kao, G., Karantza, V., Vogel, B.E., Hutter, H., Chisholm, A.D., Yurchenco, P.D., Wadsworth, W.G. Development (2003) [Pubmed]
  9. SH3 domain-mediated interaction of dystroglycan and Grb2. Yang, B., Jung, D., Motto, D., Meyer, J., Koretzky, G., Campbell, K.P. J. Biol. Chem. (1995) [Pubmed]
  10. Ancylostoma caninum MTP-1, an astacin-like metalloprotease secreted by infective hookworm larvae, is involved in tissue migration. Williamson, A.L., Lustigman, S., Oksov, Y., Deumic, V., Plieskatt, J., Mendez, S., Zhan, B., Bottazzi, M.E., Hotez, P.J., Loukas, A. Infect. Immun. (2006) [Pubmed]
  11. Form and function: the laminin family of heterotrimers. Colognato, H., Yurchenco, P.D. Dev. Dyn. (2000) [Pubmed]
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