PMID- 11906819
OWN - NLM
STAT- MEDLINE
DCOM- 20020628
LR  - 20190922
IS  - 1357-2725 (Print)
IS  - 1357-2725 (Linking)
VI  - 34
IP  - 5
DP  - 2002 May
TI  - Prenylcysteine carboxymethyltransferase type III activity is decreased in 
      retinoic acid-treated SH-SY5Y neuroblastoma cells.
PG  - 477-86
AB  - Prenylcysteine carboxymethyltransferase (pcCMT) is an enzyme that catalyzes the 
      post-translational carboxymethylation of isoprenylated proteins ensuring a more 
      efficient membrane attachment and proper guiding to a specific target membrane. 
      In this paper, we report on modulation of pcCMT activity in retinoic acid 
      (RA)-treated SH-SY5Y neuroblastoma cells using N-acetyl-S-farnesyl-L-cysteine 
      (AFC) as artificial methyl acceptor. In addition, the methylation of endogenous 
      proteins was followed by the vapor phase equilibrium assay and the storage 
      phosphor screen (P-screen) technique with S-adenosyl-[3H-methyl] methionine 
      (AdoMet) as methyl donor. Methylation of AFC was reduced to 75% of that of the 
      control, the most prominent decrease being observed with the post-nuclear 
      membrane fraction as enzyme source. With regard to protein methylation both 
      screening methods yielded analogous results showing the [3H]-labeling of 
      endogenous proteins in the 21-25kDa molecular mass (MM) range to be diminished by 
      nearly 50%. This questions the role of protein carboxymethylation as an essential 
      component of the differentiation process in SH-SY5Y neuroblastoma cells. The 
      P-screen technique revealed that the methylation of other molecular mass proteins 
      was also affected. Both S-adenosylhomocysteine (AdoHcy) and AFC (AdoHcy being the 
      most effective) inhibited endogenous methylation. An interesting feature was that 
      AFC inhibited the protein methylation proportionally more effective in RA-treated 
      cells. Finally, the levels of three small guanosine-5'-triphosphate (GTP) binding 
      proteins were screened upon differentiation showing rab3A to be increased while 
      rhoA and H-ras were decreased.
FAU - Van Dessel, Guido A F
AU  - Van Dessel GA
AD  - RUCA-Laboratory for Human Biochemistry, University of Antwerp, Groenenborgerlaan 
      171, B-2020 Antwerp, Belgium. guvades@ruca.ua.ac.be
FAU - De Busser, Hilde M
AU  - De Busser HM
FAU - Lagrou, Albert R
AU  - Lagrou AR
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Int J Biochem Cell Biol
JT  - The international journal of biochemistry & cell biology
JID - 9508482
RN  - 0 (Antineoplastic Agents)
RN  - 0 (Membrane Proteins)
RN  - 0 (Protein Isoforms)
RN  - 5688UTC01R (Tretinoin)
RN  - 979-92-0 (S-Adenosylhomocysteine)
RN  - EC 2.1.1.- (Protein Methyltransferases)
RN  - EC 2.1.1.100 (protein-S-isoprenylcysteine O-methyltransferase)
RN  - EC 3.6.5.2 (rab3A GTP-Binding Protein)
RN  - EC 3.6.5.2 (rhoA GTP-Binding Protein)
RN  - KK6984C8O3 (N-acetyl-S-farnesylcysteine)
RN  - WYQ7N0BPYC (Acetylcysteine)
RN  - X4W3ENH1CV (Norepinephrine)
SB  - IM
MH  - Acetylcysteine/*analogs & derivatives/metabolism
MH  - Antineoplastic Agents/pharmacology
MH  - Cell Differentiation
MH  - Genes, ras
MH  - Humans
MH  - Membrane Proteins/metabolism
MH  - Methylation
MH  - Neuroblastoma/*enzymology/pathology
MH  - Norepinephrine/metabolism
MH  - Nuclear Envelope/chemistry/metabolism
MH  - Protein Isoforms
MH  - Protein Methyltransferases/*metabolism
MH  - S-Adenosylhomocysteine/metabolism
MH  - Tretinoin/*pharmacology
MH  - Tumor Cells, Cultured
MH  - rab3A GTP-Binding Protein/metabolism
MH  - rhoA GTP-Binding Protein/metabolism
EDAT- 2002/03/22 10:00
MHDA- 2002/06/29 10:01
CRDT- 2002/03/22 10:00
PHST- 2002/03/22 10:00 [pubmed]
PHST- 2002/06/29 10:01 [medline]
PHST- 2002/03/22 10:00 [entrez]
AID - S1357272501001510 [pii]
AID - 10.1016/s1357-2725(01)00151-0 [doi]
PST - ppublish
SO  - Int J Biochem Cell Biol. 2002 May;34(5):477-86. doi: 
      10.1016/s1357-2725(01)00151-0.