Interactions between the discoidin domain receptor 1 and β1 integrin regulate attachment to collagen.

ABSTRACT: Collagen degradation by phagocytosis is essential for physiological collagen turnover and connective tissue homeostasis. The rate limiting step of phagocytosis is the binding of specific adhesion receptors, which include the integrins and discoidin domain receptors (DDR), to fibrillar collagen. While previous data suggest that these two receptors interact, the functional nature of these interactions is not defined. In mouse and human fibroblasts we examined the effects of DDR1 knockdown and over-expression on β1 integrin subunit function. DDR1 expression levels were positively associated with enhanced contraction of floating and attached collagen gels, increased collagen binding and increased collagen remodeling. In DDR1 over-expressing cells compared with control cells, there were increas

SUBMITTER: Staudinger LA 

PROVIDER: S-EPMC3828761 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature