EGTA AM is a membrane-permeable Ca2+ chelator with slow chelating dynamics[1]. EGTA AM can be loaded into the cell by bath application and can therefore block the slow rise in Ca2+ required to trigger asynchronous release of glutamate [1]. Calcium chelation by EGTA AM inhibits the zona pellucida-induced acrosome reaction and apoptosis, and increases sperm motility [2]. EGTA AM can inhibit the fusion to form hybrid organelles by chelating calcium ions[3]. EGTA AM can effectively dissolve amyloid plaques in Alzheimer's disease brain tissue samples at low concentrations[4]. EGTA AM facilitates the detection of M1/MUC5AC mucin by altering the physicochemical properties of respiratory mucin, thereby exposing epitopes with which anti-M1 monoclonal antibodies are reactive[5]. EGTA AM can bind to harmful redox-active metal ions and can detoxify reactive oxygen and nitrogen substances, which is helpful for the development of catalytic antioxidants[6].
References:
[1] Li M J, Chang T W, Hung W C, et al. Cholinergic and glutamatergic transmission at synapses between pedunculopotine tegmental nucleus axonal terminals and A7 catecholamine cell group noradrenergic neurons in the rat[J]. Neuropharmacology, 2016, 110: 237-250.
[2] Ebrahimi B, Keshtgar S. The effects of EGTA on the quality of fresh and cryopreserved-thawed human spermatozoa[J]. Iranian Journal of Medical Sciences, 2020, 45(3): 188.
[3] Pryor P R, Mullock B M, Bright N A, et al. The role of intraorganellar Ca2+ in late endosome–lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles[J]. The Journal of cell biology, 2000, 149(5): 1053-1062.
[4] Cherny R A, Legg J T, McLean C A, et al. Aqueous dissolution of Alzheimer's disease Aβ amyloid deposits by biometal depletion[J]. Journal of Biological Chemistry, 1999, 274(33): 23223-23228.
[5] Roger P, Gascard J P, Bara J, et al. EGTA treatment of human airways in vitro unmasks M1/MUC5AC mucin in submucosal glands[J]. European Respiratory Journal, 2001, 18(1): 176-183.
[6] Fisher A E O, Hague T A, Clarke C L, et al. Catalytic superoxide scavenging by metal complexes of the calcium chelator EGTA and contrast agent EHPG[J]. Biochemical and biophysical research communications, 2004, 323(1): 163-167.