Opposing changes in N-acetylglucosaminyltransferase-V and -III during the cell cycle and all-trans retinoic acid treatment of hepatocarcinoma cell line

Biochim Biophys Acta. 2000 Feb 28;1495(3):297-307. doi: 10.1016/s0167-4889(99)00157-3.

Abstract

The changes in N-acetylglucosaminyltransferase-V and -III (GnT-V, GnT-III) during the cell-cycle of synchronized 7721 human hepatocarcinoma cell line were investigated. Using an HPLC method to assay GnT and flow cytometry (FCM) for cell cycle analysis, it was found that GnT-V showed the highest activity, but GnT-III reached the lowest activity when G(2)/M cells were most abundant. In contrast, GnT-V declined to the minimum while GnT-III elevated to maximum when G(0)/G(1) cells were most predominant. The opposing changes were more obvious when the activities of GnT-V and GnT-III were expressed as relative activities (activity of GnT-V or GnT-III/the sum of activities of GnT-V plus GnT-IV plus GnT-III). These opposing changes of GnT-V and GnT-III during the cell cycle might result from the different regulatory mechanisms of GnT-V and GnT-III expression in the cell cycle. The alterations in the structures of cell surface N-glycans were compatible with the changes of the activities of GnTs. The results from immunocytochemistry and Northern blot showed that the protein and mRNA contents of GnT-V were not significantly changed during the cell cycle. The activity of a cell cycle regulating protein kinase, p34(cdc2) kinase, correlated to the activity of GnT-V. These findings suggested that the change of GnT-V activity in cell cycle was not the consequence of the alteration of gene transcription or enzyme protein synthesis, but might be caused by the post-translational regulation. The decrease in GnT-V and the corresponding increase in GnT-III activities were also found after the cells were treated with all-trans retinoic acid (ATRA), and the mechanism of this might be different from that in the cell cycle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / pharmacology
  • Carcinoma, Hepatocellular / pathology
  • Cell Cycle / physiology
  • Cyclin-Dependent Kinase-Activating Kinase
  • Cyclin-Dependent Kinases*
  • Flow Cytometry
  • G1 Phase / physiology
  • G2 Phase / physiology
  • Horseradish Peroxidase / metabolism
  • Humans
  • Immunohistochemistry
  • Lectins / metabolism
  • Mitosis / physiology
  • N-Acetylglucosaminyltransferases / analysis
  • N-Acetylglucosaminyltransferases / genetics
  • N-Acetylglucosaminyltransferases / metabolism*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • RNA, Messenger / metabolism
  • Resting Phase, Cell Cycle / physiology
  • Tretinoin / pharmacology*
  • Tumor Cells, Cultured

Substances

  • Antineoplastic Agents
  • Lectins
  • RNA, Messenger
  • Tretinoin
  • Horseradish Peroxidase
  • N-Acetylglucosaminyltransferases
  • beta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase
  • alpha-1,6-mannosylglycoprotein beta 1,6-N-acetylglucosaminyltransferase
  • Protein Serine-Threonine Kinases
  • Cyclin-Dependent Kinases
  • Cyclin-Dependent Kinase-Activating Kinase