Promotion of cell migration by neural cell adhesion molecule (NCAM) is enhanced by PSA in a polysialyltransferase-specific manner

PLoS One. 2015 Apr 17;10(4):e0124237. doi: 10.1371/journal.pone.0124237. eCollection 2015.


Neural cell adhesion molecule 140 (NCAM-140) is a glycoprotein and always highly polysialylated in cancer. Functions of polysialic acid (PSA) that binds to N-glycan termini on NCAM remain unclear. ldlD-14 cells, a CHO cell mutant deficient in UDP-Gal 4-epimerase, are useful for structural and functional studies of Gal-containing glycoproteins because their abnormal glycosylation can be converted to normal status by exogenous addition of galactose (Gal). We cloned the genes for NCAM-140 and for polysialyltransferases STX and PST (responsible for PSA synthesis) from normal murine mammary gland epithelial (NMuMG) cells and transfected them into ldlD-14 and human breast cancer cells MCF-7. The effect of PSA on NCAM-mediated cell proliferation, motility, migration and adhesion was studied. We found that NCAM-140 significantly promoted cell proliferation, motility and migration, while polysialylation of NCAM-140 catalyzed by STX, but not by PST, enhanced NCAM-mediated cell migration, but not cell proliferation or motility. In addition, PSA catalyzed by different polysialyltransferases affected the adhesion of NCAM to different extracellular matrix (ECM) components.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CD56 Antigen / chemistry
  • CD56 Antigen / genetics
  • CD56 Antigen / physiology*
  • CHO Cells
  • Cell Adhesion
  • Cell Division
  • Cell Movement
  • Cells, Cultured
  • Cricetinae
  • Cricetulus
  • Extracellular Matrix Proteins / metabolism
  • Female
  • Galactosemias
  • Humans
  • MCF-7 Cells
  • Mammary Glands, Animal / cytology
  • Mice
  • Polysaccharides / analysis
  • Protein Processing, Post-Translational*
  • Recombinant Fusion Proteins / metabolism
  • Sialic Acids / metabolism*
  • Sialyltransferases / genetics
  • Sialyltransferases / metabolism*


  • CD56 Antigen
  • Extracellular Matrix Proteins
  • Ncam1 protein, mouse
  • Polysaccharides
  • Recombinant Fusion Proteins
  • Sialic Acids
  • polysialic acid
  • CMP-N-acetylneuraminate-poly-alpha-2,8-sialosyl sialyltransferase
  • Sialyltransferases
  • ST8SiaIV protein, mouse

Grant support

This study was supported by the National Science Foundation for Young Scientists of China (No. 81201572), the Natural Science Foundation of Jiangsu Province, China (No. BK2012113), Jiangsu Province Recruiting Plan for High-level, Innovative and Entrepreneurial Talents, the Fundamental Research Funds for the Central Universities (No. JUSRP51319B), Jiangsu Province "Six Summit Talent" Foundation (2013-SWYY-019) and the 111 Project (No. 111-2-06). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.