THE RECOGNITION SITES OF THE INTEGRINS ALPHA(1)BETA(1) AND ALPHA(2)BETA(1) WITHIN COLLAGEN-IV ARE PROTECTED AGAINST GELATINASE-A ATTACK IN THE NATIVE PROTEIN

The susceptibility of three different solubilized forms of type IV col lagen to gelatinase A cleavage and the concomitant effects on cell and integrin binding have been assessed, Dithiothreitol-solubilized Engel breth-Holm Swarm (EHS) type TV collagen with disrupted intramolecular disulfide bonds in the CE3[N] region was cleaved N-terminally to the C B3[IV] region into the two characteristic 100-300-nm fragments at 30 d egrees C and was totally degraded at 37 degrees C. This was reflected in the partial or total loss of the alpha(1) beta(1) and alpha(2) beta (1) integrin binding sites within this region, The ability of gelatina se A to cleave EHS type TV collagen preparations with intact interchai n disulfide bonds in CB3[IV] only occurred at higher temperatures. Fur thermore, no effect on binding of cells or isolated integrins to the g elatinase-treated collagen could be detected after treatment at 37 deg rees C, Dimeric collagen TV of human placenta with intact disulfide bo nds in the CB3[IV] region was not degraded at all by gelatinase A at 3 7 degrees C.