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Fibrin clots are equilibrium polymers that can be remodeled without proteolytic digestion.

Abstract：

:Fibrin polymerization is a necessary part of hemostasis but clots can obstruct blood vessels and cause heart attacks and strokes. The polymerization reactions are specific and controlled, involving strong knob-into-hole interactions to convert soluble fibrinogen into insoluble fibrin. It has long been assumed that clots and thrombi are stable structures until proteolytic digestion. On the contrary, using the technique of fluorescence recovery after photobleaching, we demonstrate here that there is turnover of fibrin in an uncrosslinked clot. A peptide representing the knobs involved in fibrin polymerization can compete for the holes and dissolve a preformed fibrin clot, or increase the fraction of soluble oligomers, with striking rearrangements in clot structure. These results imply that in vivo clots or thrombi are more dynamic structures than previously believed that may be remodeled as a result of local environmental conditions, may account for some embolization, and suggest a target for therapeutic intervention.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Chernysh IN,Nagaswami C,Purohit PK,Weisel JW

doi

10.1038/srep00879

subject

Has Abstract

pub_date

2012-01-01 00:00:00

pages

879

issn

2045-2322

journal_volume

2

pub_type

杂志文章

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