PMID- 12483688
OWN - NLM
STAT- MEDLINE
DCOM- 20030306
LR  - 20061115
IS  - 0021-9967 (Print)
IS  - 0021-9967 (Linking)
VI  - 455
IP  - 3
DP  - 2003 Jan 13
TI  - Palmitoyl protein thioesterase 1 is targeted to the axons in neurons.
PG  - 368-77
AB  - Palmitoyl protein thioesterase 1 (PPT1) is a depalmitoylating enzyme whose 
      deficiency leads to infantile neuronal ceroid lipofuscinosis. The disease is 
      characterized by early loss of vision and massive neuronal death. Although PPT1 
      is expressed in many tissues, a deficiency of PPT1 damages neurons only in the 
      cerebral and cerebellar cortexes and retina; other cell types remain relatively 
      unaffected. We previously demonstrated that PPT1 is present in the synaptosomes 
      and synaptic vesicles of neurons. To understand the crucial role of PPT1 for 
      neuronal cells, we further investigated the expression and targeting of PPT1 in 
      retinal, hippocampal, and cortical neurons during their maturation in culture. We 
      found that PPT1 activity increases by neuronal maturation and is highest in 
      retinal neuron cultures. In retinal neurons the expression of PPT1 precedes that 
      of the synaptic vesicle protein 2 and synaptophysin, indicating a significant 
      role for PPT1 in the early development of neuronal cells. We also found by 
      quantitative confocal immunofluorescence microscopy that PPT1 is targeted 
      preferably to axons in mature neurons, as indicated by its colocalization with 
      the axonal marker microtubule-associated protein 1. In axons PPT1 is targeted 
      specifically to axonal varicosities and presynaptic terminals, as indicated by 
      its significant colocalization with growth-associated protein 43 and 
      synaptophysin. Axonal localization of PPT1 was confirmed by double labeling with 
      synaptophysin and postembedding immunoelectron microscopy. The polarized axonal 
      targeting of PPT1 may well indicate a role for PPT1 in the exocytotic pathway of 
      neurons.
CI  - Copyright 2002 Wiley-Liss, Inc.
FAU - Ahtiainen, Laura
AU  - Ahtiainen L
AD  - National Public Health Institute, Department of Molecular Medicine, 00290 
      Helsinki, Finland.
FAU - Van Diggelen, Otto P
AU  - Van Diggelen OP
FAU - Jalanko, Anu
AU  - Jalanko A
FAU - Kopra, Outi
AU  - Kopra O
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Comp Neurol
JT  - The Journal of comparative neurology
JID - 0406041
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Sv2a protein, mouse)
RN  - 0 (Synaptophysin)
RN  - EC 3.1.2.- (Thiolester Hydrolases)
RN  - EC 3.1.2.22 (palmitoyl-protein thioesterase)
SB  - IM
MH  - Animals
MH  - Axons/*enzymology/metabolism/ultrastructure
MH  - Blotting, Western
MH  - Cell Culture Techniques
MH  - Cerebral Cortex/chemistry/*growth & development/ultrastructure
MH  - Hippocampus/chemistry/*growth & development/ultrastructure
MH  - Membrane Glycoproteins/metabolism
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Microscopy, Electron
MH  - Microscopy, Immunoelectron
MH  - Microtubule-Associated Proteins/metabolism
MH  - Nerve Tissue Proteins/metabolism
MH  - Neurons/*enzymology/metabolism/ultrastructure
MH  - Presynaptic Terminals/metabolism
MH  - Retina/chemistry/*growth & development/ultrastructure
MH  - Synaptophysin/metabolism
MH  - Thiolester Hydrolases/*metabolism
EDAT- 2002/12/17 04:00
MHDA- 2003/03/07 04:00
CRDT- 2002/12/17 04:00
PHST- 2002/12/17 04:00 [pubmed]
PHST- 2003/03/07 04:00 [medline]
PHST- 2002/12/17 04:00 [entrez]
AID - 10.1002/cne.10492 [doi]
PST - ppublish
SO  - J Comp Neurol. 2003 Jan 13;455(3):368-77. doi: 10.1002/cne.10492.