Structural and Functional Plasticity of Collagen Fibrils.

Collagen is a major component of the subendothelial matrix and participates in bleeding arrest by activating and aggregating platelets at the site of vascular injury. The most common type I collagen exists in both soluble and fibrillar forms, but structural exchangeability between the two forms is currently unknown. Using atomic force microscopy, we show that type I collagen switches between soluble and fibrillar forms in a pH-dependent and ion-independent manner. Fibrillar collagen is rope like with characteristic "D-bands." The collagen fibrils can be disrupted with 0.1 M acetic acid and will reform when the pH is adjusted to 7.4. This structural plasticity leads to drastically different activities, with fibrillar collagen being significantly more active for platelets under static and flow conditions. More important, by probing with noncontact hopping probe ion-conductance microscopy, we find that platelets adherent to fibrillar collagen present primarily as high-density bubble shapes that have undergone rapid microvesiculation.