Laminin: multiple forms, multiple receptors

https://doi.org/10.1016/0955-0674(90)90082-PGet rights and content

First page preview

First page preview
Click to open first page preview

References (25)

  • M.M. Lotz et al.

    Human colon carcinoma cells use multiple receptors to adhere to laminin: involvement of α6β4 an α2β1 integrins

    Cell Regulation

    (1990)
  • K.R. Gehlsen et al.

    Subunit structure of a laminin binding integrin and localization of its binding site on laminin

    J Biol Chem

    (1989)
  • Cited by (77)

    • Shootin1b Mediates a Mechanical Clutch to Produce Force for Neuronal Migration

      2018, Cell Reports
      Citation Excerpt :

      In addition, shootin1b accumulates to high levels at the growth cones, and shootin1 KO led to the reduction of the traction forces and concurrent inhibition of leading process extension and cell migration. Neuronal environments in the brain include laminin located on the extracellular matrix and L1-CAM presented on the neighboring cells (Mercurio, 1990; Kamiguchi et al., 1998). In this study, neurons were cultured on laminin-coated or L1-CAM-coated coverslips.

    • Regulated Splicing of the α6 Integrin Cytoplasmic Domain Determines the Fate of Breast Cancer Stem Cells

      2014, Cell Reports
      Citation Excerpt :

      A frequent observation is that high expression of the α6 integrin subunit (CD49f) is a biomarker for breast and other CSCs (Goel et al., 2013; Meyer et al., 2010; Vieira et al., 2012). This subunit heterodimerizes with either the β1 or β4 subunits to generate the α6β1 and α6β4 integrins, which function primarily as laminin receptors (Mercurio, 1990). Interestingly, however, the β4 subunit appears to be expressed at very low levels, if at all, in CSCs compared to non-CSCs, indicating that α6β1 is the dominant α6 integrin expressed by CSCs (Goel et al., 2013; Lathia et al., 2010).

    • Interaction of Schwann cells with laminin encapsulated PLCL core-shell nanofibers for nerve tissue engineering

      2014, European Polymer Journal
      Citation Excerpt :

      Laminin is a major glycoprotein of the basement membrane of nerve tissue with molecular weight of 850 kDa and it consists of multidomain “cross-like” shaped structure made up of three disulfide-linked polypeptides [17,18]. The main function of laminin in the nervous system is to stimulate neurite outgrowth [19] and it is also associated with axonal guidance [5]. This glycoprotein promotes neurite function in tissue culture along with stimulation of cell mitosis [20], and influence the proliferation and migration of Schwann cells (SCs) [21], that form myelin around axons, which is also critical for the appropriate function of the peripheral nerves [22].

    View all citing articles on Scopus
    View full text