Collagen Fibril Formation
نویسندگان
چکیده
Soluble rat tail tendon collagen with intact nonhelical ends and largely free of aggregates was used to study fibril formation in vitro. The process was initiated by raising the pH and warming a cold solution of collagen. Fibril formation was monitored by turbidity and the product was examined by electron microscopy. Optimal conditions that will form fibrils similar to those observed in vivo are: a solvent containing 30 mM phosphate, 30 mu i’V-[tris(hydroxymethyl)methyl-2-amino]ethanesulfonic acid (Tes), and NaCl to give an ionic strength of 0.225 at pH 7.3; temperatures between 20 and 30°C; and collagen concentrations between 0.02 and 0.5 mg/ml. Phosphate is required to obtain well ordered fibrils. Under other conditions polymorphic aggregates may form, including nonbanded filamentous forms and two types of D-periodic symmetricbanded fibrils, one of which has not been previously described. Turbidity shows a lag period followed by a growth phase. The overall process is strongly temperature-dependent with an activation energy of 58 kcal/mol. The rate of fibril formation as measured by turbidity halftimes is directly proportional to collagen concentration. The apparent critical concentration is <7 pg/ml and could be zero. We conclude that turbidity is a measure of growth by accretion rather than nucleationpolymerization. Based on the microfibril model of the collagen fibril, it is possible that this growth process is dominated by lateral association of microfibrils. Assembly of monomer to microfibril would then occur during the lag period and involve intermediates too small to be seen by turbidity.
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تاریخ انتشار 2002