Adhesion of cells to the extracellular matrix is mediated by structural glycoproteins such as fibronectin and laminin, and also elastonectin, whose role is to ensure binding of elastin fibers to cells. Interactions between elastin fibers and human skin fibroblasts cultured in a Rose chamber were investigated by using cinemicrography to observe elastin fiber attachment, detachment, and displacement over a five-day period. Elastin fiber displacement over the cell layer resulted in aggregation, which was measured using morphometry. The total number of isolated elastin fibers or aggregates decreased between 1 h and 8 h and remained stable thereafter. During the same time interval, significant decreases occurred in the numbers of isolated fibers and small aggregates (perimeter < 0.268 mm; surface area < 894 microns 2), whereas larger aggregates were formed. After 15 hours of interaction, none of the aggregates had a perimeter greater than 0.536 mm, consistent with an increase in aggregate compacting. These data demonstrate that elastin-cell interactions do not occur at random. These interactions may play a pivotal role in morphogenesis and in maintaining the integrity of elastic tissues such as the arterial wall, lungs, and skin.