Mouse Na K -ATPase 1-subunit has a K -dependent cell adhesion activity for -GlcNAc-terminating glycans
نویسندگان
چکیده
Departments of *Biosignal Research and ¶Enzyme Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173-0015, Japan; †Faculty of Science and Technology, Tokyo University of Science, Chiba 278-8510, Japan; ‡Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan; and §Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, Japan
منابع مشابه
O-10: A Marked Animal-Vegetal Polarity in The Localization of Na+,K+-ATPase Activity and Its Down-Regulation Following Progesterone-Induced Maturation
Background: Polarized cells are key to the process of differentiation. Xenopus oocyte is a polarized cell that has complete blue-print to differentiate 3 germ layers following fertilization, as key determinant molecules (Proteins and RNAs) are asymmetrically localized. The objective of this work was to localize Na+, K+-ATPase activity along animal-vegetal axis of polarized Xenopus oocyte and fo...
متن کاملThe Na-K-ATPase α₁β₁ heterodimer as a cell adhesion molecule in epithelia.
The ion gradients generated by the Na-K-ATPase play a critical role in epithelia by driving transepithelial transport of various solutes. The efficiency of this Na-K-ATPase-driven vectorial transport depends on the integrity of epithelial junctions that maintain polar distribution of membrane transporters, including the basolateral sodium pump, and restrict paracellular diffusion of solutes. Th...
متن کاملThe Na-K-ATPase 1 1 heterodimer as a cell adhesion molecule in epithelia
Vagin O, Dada LA, Tokhtaeva E, Sachs G. The Na-K-ATPase 1 1 heterodimer as a cell adhesion molecule in epithelia. Am J Physiol Cell Physiol 302: C1271–C1281, 2012. First published January 25, 2012; doi:10.1152/ajpcell.00456.2011.—The ion gradients generated by the Na-K-ATPase play a critical role in epithelia by driving transepithelial transport of various solutes. The efficiency of this Na-K-A...
متن کاملThe O-glycosylated ectodomain of FXYD5 impairs adhesion by disrupting cell-cell trans-dimerization of Na,K-ATPase β1 subunits.
FXYD5 (also known as dysadherin), a regulatory subunit of the Na,K-ATPase, impairs intercellular adhesion by a poorly understood mechanism. Here, we determined whether FXYD5 disrupts the trans-dimerization of Na,K-ATPase molecules located in neighboring cells. Mutagenesis of the Na,K-ATPase β1 subunit identified four conserved residues, including Y199, that are crucial for the intercellular Na,...
متن کاملThe adhesion molecule on glia (AMOG) is a homologue of the beta subunit of the Na,K-ATPase
AMOG (adhesion molecule on glia) is a Ca2(+)-independent adhesion molecule which mediates selective neuron-astrocyte interaction in vitro (Antonicek, H., E. Persohn, and M. Schachner. 1987. J. Cell Biol. 104:1587-1595). Here we report the structure of AMOG and its association with the Na,K-ATPase. The complete cDNA sequence of mouse AMOG revealed 40% amino acid identity with the previously clon...
متن کامل