Scanning electron microscopy of fibrin networks in rheumatoid arthritis: a qualitative analysis

E Pretorius, HM Oberholzer, WJ van der Spuy… - Rheumatology …, 2012 - Springer
E Pretorius, HM Oberholzer, WJ van der Spuy, AC Swanepoel, P Soma
Rheumatology international, 2012Springer
Rheumatoid arthritis is a chronic inflammatory condition that affects mainly synovial joints
and has an impact on approximately 1% of the Western population. The coagulation process
is altered in this condition, and this is frequently complicated by thrombocytosis. Changes in
fibrin morphology have been linked with inflammation, and this, in turn, plays an important
role in thrombosis. Changes in the fibrin fiber formation cause the alterations observed in
thrombus morphology. In the current study, the ultrastructure of platelets and fibrin networks …
Abstract
Rheumatoid arthritis is a chronic inflammatory condition that affects mainly synovial joints and has an impact on approximately 1% of the Western population. The coagulation process is altered in this condition, and this is frequently complicated by thrombocytosis. Changes in fibrin morphology have been linked with inflammation, and this, in turn, plays an important role in thrombosis. Changes in the fibrin fiber formation cause the alterations observed in thrombus morphology. In the current study, the ultrastructure of platelets and fibrin networks was investigated to determine whether any morphological changes are present in these structures in patients suffering from rheumatoid arthritis. Six patients diagnosed with rheumatoid arthritis took part in this study, and their clot morphology was compared to that of control subjects. Citrated blood with and without the addition of thrombin was used. Results indicated that the fibrin networks in the arthritis patients formed thick, matted layers. This matted appearance is due to a changed ultrastructure of the minor, thin fibers. Also, in these patients, spontaneous networks were created without the addition of thrombin, which indicates an abnormal hemostatic protein functioning, and the latter is expressed as visible changes in ultrastructure.
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