Felis Catus
Senior Member (Voting Rights)
Thank you. I'll have another look sometime and post it here if I find it.
Surface cues shape procoagulant properties of amyloidogenic microclots, 2025, Pretorius, Kell et al
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Jonathan Edwards
Senior Member (Voting Rights)
I doubt it would have been flagged as a letter. It was a comment sent to a journal in response to Kell and Pretorius, likely listed under letters but that would depend on the journal.
Connors and Ariens say what needs to be said.
There was this one by authors including Garner and Carson, which obviously has issues of its own. https://www.s4me.info/threads/chall...n-2024-carson-davey-smith-garner-et-al.39004/
Thank you
Jonathan Edwards
Senior Member (Voting Rights)
But it also makes some cogent points about the weakness of the theory. Even wrong people can be right some times. Beverley Hunt is head of thrombosis at Guy's and Thomas' Hospitals. It would be hard to get a more hard core thrombosis expert in the UK.
Frits Rosendaal has done work on microclots in Long-Covid (unpublished) and seemed rather critical of the whole story as well. I think it could be useful to hear his thoughts on the whole saga (but obviously people that publish a study every week might be happy to just put their name onto everything possible), even though I think everything that can be said has already been said, even if that won't stop people from writing nonsensical reviews even if their predications have turned out the wrong already.
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Surface cues shape procoagulant properties of amyloidogenic microclots
Hypercoagulability, immunothrombosis, and protein misfolding are deeply interconnected processes that converge on cell membranes as central orchestrators of thrombo-inflammation. In health, membrane lipid asymmetry, intact glycocalyx, and regulated receptor activity maintain vascular homeostasis. During inflammation or cell death, however, phosphatidylserine (PS) externalization, protein unfolding, and damage to glycosaminoglycans expose negatively charged, amyloidogenic surfaces that attract coagulation factors, inflammatory mediators, and adhesion proteins. These events generate catalytic sites for prothrombinase assembly.
We review how cellular debris, microparticles, immune complexes such as neutrophil extracellular traps, and amyloidogenic plasma proteins, including serum amyloid A, interact with fibrinogen to form circulating (heterogeneous) procoagulant complexes, we term fibrinaloid microclot complexes (FMCs). Distinct from canonical fibrin clots, these FMCs display β-sheet–rich features, ThT-binding, and resistance to fibrinolysis, implicating them as key drivers of vascular pathology in inflammatory (and post-viral) syndromes.
Recognizing different FMC phenotypes, mechanisms, and biochemical composition of these circulating complexes provides new insights into the pathogenesis of systemic inflammatory diseases and clarifies how membrane damage, protein misfolding, and coagulation converge to drive thrombo-inflammation. These insights position FMCs as a conceptual framework for understanding pathological clotting across inflammatory and post-infectious vascular syndromes.
Web | DOI | PDF | Cell Death & Disease | Open Access
Surface cues shape procoagulant properties of amyloidogenic microclots
Pretorius, Etheresia; Venter, Chantelle; Nunes, Massimo; Thierry, Alain R; Kell, Douglas B
Hypercoagulability, immunothrombosis, and protein misfolding are deeply interconnected processes that converge on cell membranes as central orchestrators of thrombo-inflammation. In health, membrane lipid asymmetry, intact glycocalyx, and regulated receptor activity maintain vascular homeostasis. During inflammation or cell death, however, phosphatidylserine (PS) externalization, protein unfolding, and damage to glycosaminoglycans expose negatively charged, amyloidogenic surfaces that attract coagulation factors, inflammatory mediators, and adhesion proteins. These events generate catalytic sites for prothrombinase assembly.
We review how cellular debris, microparticles, immune complexes such as neutrophil extracellular traps, and amyloidogenic plasma proteins, including serum amyloid A, interact with fibrinogen to form circulating (heterogeneous) procoagulant complexes, we term fibrinaloid microclot complexes (FMCs). Distinct from canonical fibrin clots, these FMCs display β-sheet–rich features, ThT-binding, and resistance to fibrinolysis, implicating them as key drivers of vascular pathology in inflammatory (and post-viral) syndromes.
Recognizing different FMC phenotypes, mechanisms, and biochemical composition of these circulating complexes provides new insights into the pathogenesis of systemic inflammatory diseases and clarifies how membrane damage, protein misfolding, and coagulation converge to drive thrombo-inflammation. These insights position FMCs as a conceptual framework for understanding pathological clotting across inflammatory and post-infectious vascular syndromes.
Web | DOI | PDF | Cell Death & Disease | Open Access