N-cadherin is stably associated with and is an acceptor for a cell surface N-acetylgalactosaminylphosphotransferase - PubMed (original) (raw)
. 1990 Feb 15;265(5):2923-8.
Affiliations
- PMID: 2154466
Free article
N-cadherin is stably associated with and is an acceptor for a cell surface N-acetylgalactosaminylphosphotransferase
J Balsamo et al. J Biol Chem. 1990.
Free article
Abstract
Calcium-dependent cell-cell adhesion among embryonic chick neural retina cells is mediated by N-cadherin, a 130,000-Da integral membrane protein. We have reported that the ability of chick neural retina cells to form calcium-dependent cell-cell adhesion is also correlated with the presence of an N-acetylgalactosaminyltransferase at the cell surface (Balsamo, J., and Lilien, J. (1982) J. Biol. Chem. 257, 349-354). This enzyme transfers N-acetylgalactosaminephosphate to endogenous acceptors (Balsamo, J., Pratt, R. S., and Lilien, J. (1986) Biochemistry 25, 5402-5407) and is tightly associated with these acceptors forming a complex which can be isolated from neutral detergent extracts of plasma membranes. We now report that N-cadherin is present in the complex and is an acceptor for the N-acetylgalactosaminylphosphotransferase. Antibodies prepared against N-cadherin precipitate the transferase containing complexes from neutral detergent extracts; however, when the complexes are dissociated by treatment with sodium dodecyl sulfate prior to immunoprecipitation, only N-cadherin is precipitated. Similarly, anti-transferase antibodies immunoprecipitate N-cadherin containing complexes prior to disruption of the complex with sodium dodecyl sulfate. Catalysis of the transferase reaction in the complex results in the transfer of N-acetylgalactosamine phosphate to oligosaccharide chains on N-cadherin. Glycosylation of N-cadherin by the transferase also occurs in situ; labeling of retina cells with [32P] orthophosphate results in N-cadherin molecules containing terminal N-acetylgalactosamine linked to an oligosaccharide chain via a phosphodiester bond.
Similar articles
- Regulated binding of PTP1B-like phosphatase to N-cadherin: control of cadherin-mediated adhesion by dephosphorylation of beta-catenin.
Balsamo J, Leung T, Ernst H, Zanin MK, Hoffman S, Lilien J. Balsamo J, et al. J Cell Biol. 1996 Aug;134(3):801-13. doi: 10.1083/jcb.134.3.801. J Cell Biol. 1996. PMID: 8707857 Free PMC article. - Antibodies to the retina N-acetylgalactosaminylphosphotransferase inhibit neurite outgrowth.
Gayá-González L, Balsamo J, Swaminathan N, Lilien J. Gayá-González L, et al. J Neurosci Res. 1991 Aug;29(4):474-80. doi: 10.1002/jnr.490290407. J Neurosci Res. 1991. PMID: 1665187 - The retina cell-surface N-acetylgalactosaminylphosphotransferase is anchored by a glycophosphatidylinositol.
Balsamo J, Lilien J. Balsamo J, et al. Biochemistry. 1993 Aug 17;32(32):8246-50. doi: 10.1021/bi00083a027. Biochemistry. 1993. PMID: 8394131
Cited by
- Regulated binding of PTP1B-like phosphatase to N-cadherin: control of cadherin-mediated adhesion by dephosphorylation of beta-catenin.
Balsamo J, Leung T, Ernst H, Zanin MK, Hoffman S, Lilien J. Balsamo J, et al. J Cell Biol. 1996 Aug;134(3):801-13. doi: 10.1083/jcb.134.3.801. J Cell Biol. 1996. PMID: 8707857 Free PMC article. - Cell phenotype in normal epithelial cell lines with high endogenous N-cadherin: comparison of RPE to an MDCK subclone.
Youn YH, Hong J, Burke JM. Youn YH, et al. Invest Ophthalmol Vis Sci. 2006 Jun;47(6):2675-85. doi: 10.1167/iovs.05-1335. Invest Ophthalmol Vis Sci. 2006. PMID: 16723486 Free PMC article. - N-cadherin regulates ingrowth and laminar targeting of thalamocortical axons.
Poskanzer K, Needleman LA, Bozdagi O, Huntley GW. Poskanzer K, et al. J Neurosci. 2003 Mar 15;23(6):2294-305. doi: 10.1523/JNEUROSCI.23-06-02294.2003. J Neurosci. 2003. PMID: 12657688 Free PMC article. - Cell surface sialic acid inhibits Cx43 gap junction functions in constructed Hela cancer cells involving in sialylated N-cadherin.
Li J, Cheng L, Wang LJ, Liu HC, Li L, Wang XL, Geng MY. Li J, et al. Mol Cell Biochem. 2010 Nov;344(1-2):241-51. doi: 10.1007/s11010-010-0548-9. Epub 2010 Aug 29. Mol Cell Biochem. 2010. PMID: 20803237 - A polycystin-1 multiprotein complex is disrupted in polycystic kidney disease cells.
Roitbak T, Ward CJ, Harris PC, Bacallao R, Ness SA, Wandinger-Ness A. Roitbak T, et al. Mol Biol Cell. 2004 Mar;15(3):1334-46. doi: 10.1091/mbc.e03-05-0296. Epub 2004 Jan 12. Mol Biol Cell. 2004. PMID: 14718571 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials