Current and Emerging Biomarkers of Cell Death in Human Disease

Table 1

Cell death biomarkers in human diseases.

Official symbol	Official full name	Clinical relevance	Function	Pathway	References
CASP3	Caspase-3, apoptosis-related cysteine peptidase	A potential new biomarker for myocardial injury and cardiovascular disease	Caspase-3 is responsible for chromatin condensation and DNA fragmentation	Apoptosis	[96]
TP53	Tumor protein p53	Implications for the regulation and execution of apoptosis in colorectal cancer and other cancers.	TP53 activation is capable of inducing apoptosis by intrinsic pathway.	Apoptosis	[97]
KRT18	Keratin 18	A biomarker of liver damage and apoptosis in chronic hepatitis C	CK18-Gly(−) involves the inactivation of Akt1 and protein kinase Cθ	Apoptosis	[98–100]
FAS	Fas cell surface death receptor	Granulomatous disease	Fas can increase the antigen-specific CD8(+) T-cell responses during viral infection	Apoptosis	[101, 102]
TRAIL	Tumor necrosis factor (ligand) superfamily, member 10	Inducing the autoimmune inflammation in SLE	TRAIL directly induces apoptosis through an extrinsic pathway, which involes the activation of caspases.	Apoptosis	[103]
MAP1LC3A	Microtubule-associated protein 1 light chain 3 alpha	Neurodegenerative and neuromuscular diseases, tumorigenesis, and bacterial and viral infections	LC3-II functions in phagophore expansion and also in cargo recognition	Autophagy	[104, 105]
BECN1	Beclin 1, autophagy related	Human breast cancers and ovarian cancers	BECN1 is part of a Class III PI3K complex that participates in autophagosome formation, mediating the localization of other autophagy proteins.	Autophagy	[106]
RIPK1	Receptor (TNFRSF)-interacting serine-threonine kinase 1	Involving retinal disorders including retinitis pigmentosa and retinal detachment	RIPK1 and RIPK3 association forms a necrosis-inducing complex, initiates cell-death signals (programmed necrosis).	Necrosis	[107–109]
RIPK3	Receptor-interacting serine-threonine kinase 3	Atherosclerotic lesions and the pathogenesis of inflammatory bowel	RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex, then triggering necrosis.	Necrosis	[110–112]