Fibroblasts that migrate into a wound during the early stages of repair use cell surface integrins to interact with extracellular molecules as they move away from the interstitial matrix of normal tissue and into the provisional matrix of the wound. Therefore, to understand a critical phase of wound healing, it is necessary to understand the details of integrin involvement. Normal adult human dermal fibroblasts in culture express many receptors for the provisional matrix proteins fibronectin, vitronectin, and fibrinogen, including the integrins α3β1,α4β1, α5β1,αvβ1,αvβ3, and αvβ5. We used quantitative flow cytometry to estimate the relative numbers of these receptors and immunoprecipitation to confirm the expression of αvβ1. Adult human dermal fibroblasts primarily use β1 integrins, α4β1, α5β1, and possibly αvβ1, for attachment to fibronectin. αvβ3 and perhaps other integrins containing the αv subunit serve fibroblasts as secondary or auxiliary receptors for fibronectin. In contrast, these cells use αv integrins but probably not β1 integrins for attachment to vitronectin. αvβ3 and αvβ5 apparently act in concert to mediate attachment to vitronectin, and these two integrins may perform different functions during wound repair. Fibroblast adhesion to certain preparations of fibrinogen occurs, at least partially, through the small amount of fibronectin present in the preparations. Fibroblast attachment to fibrinogen purified free of fibronectin also occurs, and that was demonstrated with a sensitive new assay called electrical cell-substrate impedance sensing. Fibroblast attachment to pure fibrinogen can be inhibited by RGD peptide, suggesting that integrins are involved.