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Research Article Free access | 10.1172/JCI118693
Department of Surgery, Maine Medical Center/Maine Medical Center Research Institute, South Portland, Maine 04106, USA.
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Department of Surgery, Maine Medical Center/Maine Medical Center Research Institute, South Portland, Maine 04106, USA.
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Department of Surgery, Maine Medical Center/Maine Medical Center Research Institute, South Portland, Maine 04106, USA.
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Department of Surgery, Maine Medical Center/Maine Medical Center Research Institute, South Portland, Maine 04106, USA.
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Department of Surgery, Maine Medical Center/Maine Medical Center Research Institute, South Portland, Maine 04106, USA.
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Department of Surgery, Maine Medical Center/Maine Medical Center Research Institute, South Portland, Maine 04106, USA.
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Department of Surgery, Maine Medical Center/Maine Medical Center Research Institute, South Portland, Maine 04106, USA.
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Published June 1, 1996 - More info
Remodeling of the extracellular matrix by activated mesenchymal cells (myofibroblasts) is a critical aspect of wound repair in all adult organs. Collagen-dependent gel contraction, a process requiring integrin function, is an established in vitro assay thought to mimic in vivo matrix remodeling. Numerous data have implicated the alpha2beta1 integrin in various cell types as the primary collagen receptor responsible for collagen gel contraction. However, evidence from the literature suggests that the major collagen binding integrin expressed on mesenchymally derived cells in situ is the alpha1beta1 integrin, not the alpha2beta1 integrin. In this report, we use a rat vascular injury model to illustrate that the alpha1beta1 integrin is the major collagen receptor expressed on vascular smooth muscle cells after injury. Using two smooth muscle cell lines, expressing either the alpha1beta1 integrin alone or both the alpha1beta1 and alpha2beta1 integrins, along with Chinese hamster ovary cells transfected with the alpha1 integrin, we demonstrate that alpha1beta1 supports not only collagen-dependent adhesion and migration, but also gel contraction. These data suggest that in vivo the alpha1beta1 integrin is a critical collagen receptor on mesenchymally derived cells potentially involved in matrix remodeling after injury.