Collagen receptors mediate early events in the attachment of epithelial (MDCK) cells.

Madin-Darby canine kidney (MDCK) cells kept in suspension culture for 12-15 hr displayed high-affinity binding sites for 125I-lathyritic (soluble) collagen (120,000/cell, KD = 30 nM) and preferred collagens types I and IV over laminin or fibronectin as substrates during the first hour of attachment. On the other hand, after 4 hr, attachment to all four substrates was equally efficient. Upon challenge with a collagen substrate, the high-affinity sites were rapidly recruited on it (T1/2 = 6 min). Their occupancy by soluble collagen triggered the exocytosis of a second large population of low-affinity collagen binding sites that included laminin and seems to be involved in a second cell-attachment mechanism. These results are compatible with a two-step model of MDCK cell attachment to the substrate: first, via high-affinity collagen binding sites, and second, via laminin of cellular origin.