caa a22 4500 477038301 CHVBK 20180405111310.0 cr unu---uuuuu 170330e19960401xx s 000 0 eng 10.1007/BF02740648 doi (NATIONALLICENCE)springer-10.1007/BF02740648 Role of laminin and integrin interactions in growth cone guidance [Elektronische Daten] [Lisa McKerracher, Muriel Chamoux, Carlos Arregui] Laminin is well known to promote neuronal adhesion and axonal growth, but recent experiments suggest laminin has a wider role in guiding axons, both in development and regeneration. In vitro experiments demonstrate that laminin can alter the rate and direction of axonal growth, even when growth cone contact with laminin is transient. Investigations focused on a single neuronal type, such as retinal ganglion cells (RGCs), strongly implicate laminin as an important guidance molecule in development and suggest the involvement of integrins. Integrins are receptors for laminin, and neurons express multiple types of integrins that bind laminin. Morphologically, integrins cluster in point contacts, specialized regions of the growth cone that may coordinately regulate adhesion and motility. Recent evidence suggests that the structure and regulation of point contacts may differ from that of their nonneuronal counterparts, focal contacts. In part, this may be because the interaction of the cytoplasmic domain of integrin with the cytoskeleton is different in point contacts and focal contacts. Mutational studies where the cytoplasmic domain is truncated or altered are leading to a better understanding of the role of the α and β subunit in regulating integrin clustering and binding to the cytoskeleton. In addition, whereas integrins may regulate motility through direct physical linkages to the growth cone cytoskeleton, an equally important role is their ability to elicit signaling, both through protein tyrosine phosphorylation and modulating calcium levels. Through such mechanisms integrins likely regulate the dynamic attachment and detachment of the growth cone as it moves on laminin substrates. Humana Press Inc, 1996 Neuronal integrins nationallicence point contacts nationallicence adhesion nationallicence laminin nationallicence McKerracher Lisa Department de Pathologie, Université de Montréal, CP 6128 Centre-ville, H3C 3J7, Montreal, Quebec, Canada aut Chamoux Muriel Department de Pathologie, Université de Montréal, CP 6128 Centre-ville, H3C 3J7, Montreal, Quebec, Canada aut Arregui Carlos Dpto. de Quimica Biologica, Facultad de Ciencias Quimicas, Universidad Nacionalde Cordoba, Ciudad Universitaria CC. 61, Cordoba, Argentina aut Molecular Neurobiology Humana Press 12/2(1996-04-01), 95-116 0893-7648 12:2<95 1996 12 12035 https://doi.org/10.1007/BF02740648 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF02740648 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- McKerracher Lisa Department de Pathologie, Université de Montréal, CP 6128 Centre-ville, H3C 3J7, Montreal, Quebec, Canada aut NATIONALLICENCE 700 1- Chamoux Muriel Department de Pathologie, Université de Montréal, CP 6128 Centre-ville, H3C 3J7, Montreal, Quebec, Canada aut NATIONALLICENCE 700 1- Arregui Carlos Dpto. de Quimica Biologica, Facultad de Ciencias Quimicas, Universidad Nacionalde Cordoba, Ciudad Universitaria CC. 61, Cordoba, Argentina aut NATIONALLICENCE 773 0- Molecular Neurobiology Humana Press 12/2(1996-04-01), 95-116 0893-7648 12:2<95 1996 12 12035 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer