[HTML][HTML] Human homolog of mouse tescalcin associates with Na+/H+ exchanger type-1
J Mailänder, W Müller-Esterl, J Dedio - FEBS letters, 2001 - Elsevier
J Mailänder, W Müller-Esterl, J Dedio
FEBS letters, 2001•ElsevierA novel regulatory protein, tescalcin (TSC), recently isolated from mouse embryonic testes,
has been implicated in gonadal differentiation. Employing the yeast two-hybrid system with
the Na+/H+ exchanger type-1 (NHE1) carboxyterminal domain as a bait we have identified a
novel NHE1-associated protein of 214 amino acid residues representing the human
homolog of mouse TSC (96.7% identity). Co-precipitation experiments demonstrated the
interaction of human TSC with NHE1 in vitro and in vivo, and 45Ca2+ overlay assay …
has been implicated in gonadal differentiation. Employing the yeast two-hybrid system with
the Na+/H+ exchanger type-1 (NHE1) carboxyterminal domain as a bait we have identified a
novel NHE1-associated protein of 214 amino acid residues representing the human
homolog of mouse TSC (96.7% identity). Co-precipitation experiments demonstrated the
interaction of human TSC with NHE1 in vitro and in vivo, and 45Ca2+ overlay assay …
A novel regulatory protein, tescalcin (TSC), recently isolated from mouse embryonic testes, has been implicated in gonadal differentiation. Employing the yeast two-hybrid system with the Na+/H+ exchanger type-1 (NHE1) carboxyterminal domain as a bait we have identified a novel NHE1-associated protein of 214 amino acid residues representing the human homolog of mouse TSC (96.7% identity). Co-precipitation experiments demonstrated the interaction of human TSC with NHE1 in vitro and in vivo, and 45Ca2+ overlay assay revealed that TSC binds Ca2+. Immunofluorescence studies indicated that TSC is prominent in cellular lamellipodia where it colocalizes with NHE1. Abundant expression of TSC mRNA in the heart suggests that TSC may play important role(s) in concert with NHE1 in cardiac tissues.
Elsevier