AbstractSystemic scleroderma (SSc) is a complex connective tissue disorder of unknown etiology. In early stages of the disease, libroblasts are activated to produce large amounts of collagen with subsequent fibrosis. Collagen metabolism of fibroblasts is modulated by their contact with the extracellular matrix (ECM), which involves distinct receptors on the cell surface, mainly belonging to the integrins. We investigated the expression of collagen receptor α2β1, in SSc and normal fibroblasts, since this receptor has been shown to be utilized by fibroblasts for adhesion to and reorganization of collagen I. 9 strains of scleroderma fibroblasts grown as monolayer cultures were first analyzed with respect to their collagen I expression. 6 of these strains were similar to controls (“low” producers) and 3 strains showed up to 2–3 × higher levels of collagen I mRNA expression (“high” producers). Northern hybridization using a cDNA probe specific for the α2integrin subunit revealed a decrease of the corresponding mRNA in SSc fibroblasts as compared to controls (75% versus 100%). “High” collagen producing cell strains displayed the lowest values for α2integrin mRNA. The decrease of α2integrin subunit expression at the mRNA level in selected fibroblasts was further substantiated by radioimmunoprecipitation using specific mAbs directed against α2integrin subunit. No significant changes in β1integrin expression could be observed‐neither at mRNA nor at the protein level. Our data indicate a correlation between excessive synthesis of collagen and low levels of α2integrin subunit expression in SSc fibroblasts. Further experiments should clarify whether this observation is a phenomenon specific for scleroderma or whether it reflects an “activ