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Human homolog of mouse tescalcin associates with Na + /H + exchanger type‐1
Author(s) -
Mailänder Jens,
Müller-Esterl Werner,
Dedio Jürgen
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02986-6
Subject(s) - microbiology and biotechnology , lamellipodium , in vitro , immunofluorescence , chemistry , messenger rna , yeast , biology , biochemistry , gene , genetics , antibody , cell migration
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 45 Ca 2+ overlay assay revealed that TSC binds Ca 2+ . 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.