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) after ischemia-induced intracellular acidosis. Nine isoforms of NHE (NHE1-9) have been identified in mammalian tissues (Orlowski & Grinstein, 2004). These isoforms differ in their tissue expression, subcellular distribution, kinetic properties, inhibitor sensitivity, and physiological functions. NHE-1 is ubiquitously expressed on the plasma membrane of virtually all mammalian cell types (Sardet et al., 1989). NHE-2-4 are expressed on the plasma membrane, predominantly in the epithelia of the kidney and gastrointestinal tract (Orlowski & Grinstein, 2004). NHE-3 is the only isoform known to recycle between the plasma membrane and the endosomal compartment (D'Souza et al., 1998). NHE-5 expression is concentrated in neurons (Attaphitaya et al., 1999) and may modulate the pH of synaptic vesicles (Szaszi et al., 2002). NHE-6 and NHE-9 are expressed predominantly in endosomal vesicles (Nakamura et al., 2005) and NHE-7 localizes to the trans-Golgi network and associated endosomes (Numata & Orlowski, 2001). NHE-8 has been localized to the plasma membrane of renal proximal tubule epithelial cells, and to endosomal vesicles and the trans-Golgi network (Goyal et al., 2003; Nakamura et al., 2005). NHE-1 is the most extensively studied isoform, and the most abundant isoform in the CNS (Ma & Haddad, 1997; Orlowski et al., 1992). Research over the past two decades has expanded our understanding of the role of NHE-1 beyond that of simply maintenance of ion homeostasis and cell volume, to an emerging picture of a regulator of many cell functions. NHE-1 plays a role in regulation of cell proliferation, migration (Bussolino et al., 1989), and the microglial respiratory burst (Liu et al., 2010). NHE-1 protein consists of 815 amino acids with a calculated molecular weight of 85 kDa. However, NHE-1 has an apparent size of ~110 kDa due to its N- and O- linked glycosylation in the extracellular loop 1. NHE-1 has

The Na+/H+ Exchanger-1 as a New Molecular Target in Stroke Interventions