PMID- 10739571
OWN - NLM
STAT- MEDLINE
DCOM- 20000721
LR  - 20231213
IS  - 0300-4864 (Print)
IS  - 0300-4864 (Linking)
VI  - 28
IP  - 4-5
DP  - 1999 Apr-May
TI  - Myelin glycosphingolipid/cholesterol-enriched microdomains selectively sequester 
      the non-compact myelin proteins CNP and MOG.
PG  - 281-93
AB  - Plasma membranes are complex arrays of protein and lipid subdomains. 
      Detergent-insoluble, glycosphingolipid/cholesterol-enriched micro-domains 
      (DIGCEMs) have been implicated in protein sorting and/or as sites for signaling 
      cascades in the plasma membrane. We previously identified the presence of DIGCEMs 
      in oligodendrocytes in culture and purified myelin and characterized a novel 
      DIGCEM-associated tetraspan protein, MVP17/rMAL (Kim et al. (1995) Journal of 
      Neuroscience Research 42, 413-422). We have now analyzed the association of known 
      myelin proteins with DIGCEMs in order to provide a better understanding of their 
      roles during myelin biogenesis. We used four well-established criteria to 
      identify myelin DIGCEM-associated proteins: insolubility in a non-ionic detergent 
      Triton X-100 at low temperature (4 degrees C), flotation of the insoluble 
      complexes to low density fractions in sucrose gradients, and TX-100 
      solubilization at 37 degrees C, or at 4 degrees C following treatment with the 
      cholesterol-binding detergent saponin. We demonstrate that these proteins fall 
      into four distinct groups. Although all tested proteins could be floated to a 
      low-density fraction, proteolipid protein (PLP), myelin basic protein (MBP) and 
      myelin associated glycoprotein (MAG) were solubilized by the detergent 
      extraction, and connexin32 (Cx32) and oligodendrocyte-specific protein (OSP) met 
      only some of the criteria for DIGCEMs. Only the non-compact myelin proteins 
      2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP) and myelin/oligodendrocyte 
      glycoprotein (MOG) satisfied all four criteria for DIGCEM-associated proteins. 
      Significantly, only approximately 40% of CNP and MOG were selectively associated 
      with DIGCEMs. This suggests that they may have both non-active "soluble", and 
      functionally active DIGCEM-associated, forms in the membrane, consistent with 
      current views that DIGCEMs provide platforms for bringing together and activating 
      components of the signal transduction apparatus. We therefore propose that CNP 
      and MOG may have unique roles among the major myelin proteins in signaling 
      pathways mediated by lipid-protein microdomains formed in myelin.
FAU - Kim, T
AU  - Kim T
AD  - Department of Microbiology, MC-3205, University of Connecticut Health Center, 263 
      Farmington Ave., Farmington, CT 06030-3205, USA.
FAU - Pfeiffer, S E
AU  - Pfeiffer SE
LA  - eng
GR  - NS10861/NS/NINDS NIH HHS/United States
GR  - RG2189/RG/CSR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Neurocytol
JT  - Journal of neurocytology
JID - 0364620
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Connexins)
RN  - 0 (Mog protein, rat)
RN  - 0 (Myelin Basic Protein)
RN  - 0 (Myelin Proteins)
RN  - 0 (Myelin Proteolipid Protein)
RN  - 0 (Myelin-Associated Glycoprotein)
RN  - 0 (Myelin-Oligodendrocyte Glycoprotein)
RN  - 97C5T2UQ7J (Cholesterol)
RN  - EC 3.1.4.- (2',3'-Cyclic-Nucleotide Phosphodiesterases)
SB  - IM
MH  - 2',3'-Cyclic-Nucleotide Phosphodiesterases/analysis/immunology/*metabolism
MH  - Animals
MH  - Antibodies, Monoclonal
MH  - Blotting, Western
MH  - Brain Chemistry/physiology
MH  - Cholesterol/*metabolism
MH  - Connexins/analysis/metabolism
MH  - Myelin Basic Protein/analysis/metabolism
MH  - Myelin Proteins
MH  - Myelin Proteolipid Protein/analysis/metabolism
MH  - Myelin Sheath/chemistry/*enzymology
MH  - Myelin-Associated Glycoprotein/analysis/immunology/*metabolism
MH  - Myelin-Oligodendrocyte Glycoprotein
MH  - Rats
MH  - Signal Transduction/physiology
MH  - Subcellular Fractions/chemistry/enzymology
MH  - Gap Junction beta-1 Protein
EDAT- 2000/03/30 09:00
MHDA- 2000/08/01 11:00
CRDT- 2000/03/30 09:00
PHST- 2000/03/30 09:00 [pubmed]
PHST- 2000/08/01 11:00 [medline]
PHST- 2000/03/30 09:00 [entrez]
AID - 10.1023/a:1007001427597 [doi]
PST - ppublish
SO  - J Neurocytol. 1999 Apr-May;28(4-5):281-93. doi: 10.1023/a:1007001427597.