Table 1.

The activation mechanisms of TF.

Category	Responsible factor	Action mechanism	Examined cell (tissue) type [reference]
Typical decryption	PS in the plasma membrane	Externalisation of PS in plasma membrane	Human leukaemia (THP-1) cells [16, 39]
	SM in the plasma membrane	Ceramide generation by A-SMase	• Human monocyte-derived macrophages (MDMs) [46, 47] • Human endothelial cells (HUVECs) [47] • Murine peripheral blood mononuclear cells [47]
	PDI	Disulfide bond (Cys186–Cys209) formation of TF	• HUVECs [52, 55] • Human keratinocytes (HaCaTs) [52] • THP-1 and lymphoma (U937) cells [16, 53]
	TF de-palmitoylation	Detachment from lipid raft, followed by a conformational change of the transmembrane domain of TF	• Human endothelial cells [58] • Breast cancer (MDA-MB-231 and MCF-7) cells [58]
	Complements	• Externalisation of PS in plasma membrane • Enhancement of PDI-mediated disulfide bond formation of TF	• MDA-MB-231 cells [59] • THP-1 cells [59] • Human and murine monocytes [60] • Human myeloma (MM1) cells [60]
	SARS-CoV-2	Ceramide formation via A-SMase	Human MDMs [63]
Other mechanisms	Decoupling of Integrins-arf6 association	• Increase cell-surface availability of TF • Conformational change of TF favourable to bind fVIIa	• Murine macrophage and smooth muscle cells (SMCs) [77] • Murine breast cancer cells [77] • HaCaT cells [78] • Human melanoma (A7) cells [78]
	TF glycosylation	Potential facilitation of substrate recognition	Placenta tissue [73]
	Pin1	Maintenance of the active state of TF via its phosphor-Ser258 residue	• Multiple human endothelial lines and SMCs [74, 75] • MDA-MB-231 cells [75]
	CD248	Direct allosteric conformational change of TF–fVIIa complex	• Human and murine vascular SMCs [80] • Human monocytic leukaemia (MM6) and A7 cells [80]