DDR1b forms covalent dimers. A, 293 cells were transiently
transfected with DDR1b or an empty plasmid (control) and stimulated
with type I collagen (col) for 90 min. Using an antibody specific for
the C terminus of DDR1, Western blot analysis of gels run under reducing
conditions (left panel) detected DDR1b as a monomeric protein
(arrow), whereas under nonreducing conditions (right panel),
DDR1b was present as both a monomer (arrow) and a dimer
(chevron). B, T-47D cells that endogenously express DDR1b
were stimulated with collagen for 18 h and lysates analyzed by Western
blotting under reducing (left panel) and nonreducing conditions
(right panel). The experiments were performed three times, and
representative data are shown.