Tyrosine phosphorylation induced by integrin-mediated adhesion of retinal neurons to laminin

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Abstract

Integrin α6β1 is a laminin receptor involved in adhesion and neurite extension of retinal neurons on laminin. The present study was carried out to understand some of the intracellular mechanisms which allow integrin-mediated neurite extension on laminin in primary neuronal cultures. Both integrin-mediated adhesion to laminin and antibody-induced integrin clustering resulted in the increased tyrosine phosphorylation of a 120 kDa polypeptide which was identified as the focal adhesion kinase. The kinetics of phosphorylation and dephosphorylation of this kinase were dramatically different in neurons plated on laminin, than in neurons in which the receptors were clustered with anti-integrin antibodies. To look at possible interactions of the focal adhesion kinase with integrins, we made use of sucrose velocity gradients, which have allowed the identification of a large complex containing the α6β1 laminin receptor. Analysis of the gradients showed that the focal adhesion kinase was not associated with the integrin receptors under these experimental conditions, while about 26% of the c-Src kinase codistributed with the integrin receptor complex, and showed a molecular size and a distribution similar to that of a 59 kDa phosphoprotein co-migrating with the α6β1 receptor. Our results suggest that integrin-induced tyrosine phosphorylation is an early intracellular event during neuronal adhesion, and that the integrin-mediated increase in tyrosine phosphorylation of the focal adhesion kinase is not sufficient per se for the induction of neurite outgrowth. Furthermore, our data indicate that Src kinase may be involved in integrin-mediated neuronal interactions with laminin.

Original languageEnglish
Pages (from-to)269-281
Number of pages13
JournalInternational Journal of Developmental Neuroscience
Volume14
Issue number3
DOIs
Publication statusPublished - 1996

Fingerprint

Retinal Neurons
Laminin
Integrins
Tyrosine
Phosphorylation
Focal Adhesion Protein-Tyrosine Kinases
Laminin Receptors
Neurites
Neurons
src-Family Kinases
Phosphoproteins
Cluster Analysis
Sucrose
Anti-Idiotypic Antibodies
Phosphotransferases

Keywords

  • Adhesion
  • Integrin
  • Laminin
  • Neurons
  • Retina
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Developmental Biology
  • Developmental Neuroscience

Cite this

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title = "Tyrosine phosphorylation induced by integrin-mediated adhesion of retinal neurons to laminin",
abstract = "Integrin α6β1 is a laminin receptor involved in adhesion and neurite extension of retinal neurons on laminin. The present study was carried out to understand some of the intracellular mechanisms which allow integrin-mediated neurite extension on laminin in primary neuronal cultures. Both integrin-mediated adhesion to laminin and antibody-induced integrin clustering resulted in the increased tyrosine phosphorylation of a 120 kDa polypeptide which was identified as the focal adhesion kinase. The kinetics of phosphorylation and dephosphorylation of this kinase were dramatically different in neurons plated on laminin, than in neurons in which the receptors were clustered with anti-integrin antibodies. To look at possible interactions of the focal adhesion kinase with integrins, we made use of sucrose velocity gradients, which have allowed the identification of a large complex containing the α6β1 laminin receptor. Analysis of the gradients showed that the focal adhesion kinase was not associated with the integrin receptors under these experimental conditions, while about 26{\%} of the c-Src kinase codistributed with the integrin receptor complex, and showed a molecular size and a distribution similar to that of a 59 kDa phosphoprotein co-migrating with the α6β1 receptor. Our results suggest that integrin-induced tyrosine phosphorylation is an early intracellular event during neuronal adhesion, and that the integrin-mediated increase in tyrosine phosphorylation of the focal adhesion kinase is not sufficient per se for the induction of neurite outgrowth. Furthermore, our data indicate that Src kinase may be involved in integrin-mediated neuronal interactions with laminin.",
keywords = "Adhesion, Integrin, Laminin, Neurons, Retina, Tyrosine phosphorylation",
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AU - Malosio, Maria Luisa

AU - Curtis, Ivan De

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N2 - Integrin α6β1 is a laminin receptor involved in adhesion and neurite extension of retinal neurons on laminin. The present study was carried out to understand some of the intracellular mechanisms which allow integrin-mediated neurite extension on laminin in primary neuronal cultures. Both integrin-mediated adhesion to laminin and antibody-induced integrin clustering resulted in the increased tyrosine phosphorylation of a 120 kDa polypeptide which was identified as the focal adhesion kinase. The kinetics of phosphorylation and dephosphorylation of this kinase were dramatically different in neurons plated on laminin, than in neurons in which the receptors were clustered with anti-integrin antibodies. To look at possible interactions of the focal adhesion kinase with integrins, we made use of sucrose velocity gradients, which have allowed the identification of a large complex containing the α6β1 laminin receptor. Analysis of the gradients showed that the focal adhesion kinase was not associated with the integrin receptors under these experimental conditions, while about 26% of the c-Src kinase codistributed with the integrin receptor complex, and showed a molecular size and a distribution similar to that of a 59 kDa phosphoprotein co-migrating with the α6β1 receptor. Our results suggest that integrin-induced tyrosine phosphorylation is an early intracellular event during neuronal adhesion, and that the integrin-mediated increase in tyrosine phosphorylation of the focal adhesion kinase is not sufficient per se for the induction of neurite outgrowth. Furthermore, our data indicate that Src kinase may be involved in integrin-mediated neuronal interactions with laminin.

AB - Integrin α6β1 is a laminin receptor involved in adhesion and neurite extension of retinal neurons on laminin. The present study was carried out to understand some of the intracellular mechanisms which allow integrin-mediated neurite extension on laminin in primary neuronal cultures. Both integrin-mediated adhesion to laminin and antibody-induced integrin clustering resulted in the increased tyrosine phosphorylation of a 120 kDa polypeptide which was identified as the focal adhesion kinase. The kinetics of phosphorylation and dephosphorylation of this kinase were dramatically different in neurons plated on laminin, than in neurons in which the receptors were clustered with anti-integrin antibodies. To look at possible interactions of the focal adhesion kinase with integrins, we made use of sucrose velocity gradients, which have allowed the identification of a large complex containing the α6β1 laminin receptor. Analysis of the gradients showed that the focal adhesion kinase was not associated with the integrin receptors under these experimental conditions, while about 26% of the c-Src kinase codistributed with the integrin receptor complex, and showed a molecular size and a distribution similar to that of a 59 kDa phosphoprotein co-migrating with the α6β1 receptor. Our results suggest that integrin-induced tyrosine phosphorylation is an early intracellular event during neuronal adhesion, and that the integrin-mediated increase in tyrosine phosphorylation of the focal adhesion kinase is not sufficient per se for the induction of neurite outgrowth. Furthermore, our data indicate that Src kinase may be involved in integrin-mediated neuronal interactions with laminin.

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