The integrin α6β1 is a prominent laminin receptor used by many cell types. In the present work, we isolate clones and determine the primary sequence of the chick integrin α6 subunit. We show that α6β1 is a prominent integrin expressed by cells in the developing chick retina. Between embryonic days 6 and 12, both retinal ganglion cells and other retinal neurons lose selected integrin functions, including the ability to attach and extend neuntes on Iaminin. In retinal ganglion cells, we show that this is correlated with a dramatic decrease in α6 mRNA and protein, suggesting that changes in gene expression account for the developmental regulation of the interactions of these neurons with laminin. In other retinal neurons the expression of α6 mRNA and protein remains high while function is lost, suggesting that the function of the α6β1 heterodimer in these cells is regulated by posttranslational mechanisms.
|Number of pages||12|
|Journal||Journal of Cell Biology|
|Publication status||Published - Apr 1991|
ASJC Scopus subject areas
- Cell Biology