PMID- 18353664
OWN - NLM
STAT- MEDLINE
DCOM- 20081013
LR  - 20231213
IS  - 1095-953X (Electronic)
IS  - 0969-9961 (Print)
IS  - 0969-9961 (Linking)
VI  - 30
IP  - 2
DP  - 2008 May
TI  - Human oligodendrocytes express Cx31.3: function and interactions with Cx32 
      mutants.
PG  - 221-33
LID - 10.1016/j.nbd.2008.01.009 [doi]
AB  - Murine oligodendrocytes express the gap junction (GJ) proteins connexin32 (Cx32), 
      Cx47, and Cx29. CNS phenotypes in patients with X-linked Charcot-Marie-Tooth 
      disease may be caused by dominant effects of Cx32 mutations on other connexins. 
      Here we examined the expression of Cx31.3 (the human ortholog of murine Cx29) in 
      human brain and its relation to the other oligodendrocyte GJ proteins Cx32 and 
      Cx47. Furthermore, we investigated in vitro whether Cx32 mutants with CNS 
      manifestations affect the expression and function of Cx31.3. Cx31.3 was localized 
      mostly in the gray matter along small myelinated fibers similar to Cx29 in rodent 
      brain and was co-expressed with Cx32 in a subset of human oligodendrocytes. In 
      HeLa cells Cx31.3 was localized at the cell membrane and appeared to form 
      hemichannels but no GJs. Cx32 mutants with CNS manifestations were retained 
      intracellularly, but did not alter the cellular localization or function of 
      co-expressed Cx31.3. Thus, Cx31.3 shares many characteristics with its ortholog 
      Cx29. Cx32 mutants with CNS phenotypes do not affect the trafficking or function 
      of Cx31.3, and may have other toxic effects in oligodendrocytes.
FAU - Sargiannidou, Irene
AU  - Sargiannidou I
AD  - Clinical Neurosciences Section, Cyprus Institute of Neurology and Genetics, 
      Nicosia, Cyprus.
FAU - Ahn, Meejin
AU  - Ahn M
FAU - Enriquez, Alan D
AU  - Enriquez AD
FAU - Peinado, Alejandro
AU  - Peinado A
FAU - Reynolds, Richard
AU  - Reynolds R
FAU - Abrams, Charles
AU  - Abrams C
FAU - Scherer, Steven S
AU  - Scherer SS
FAU - Kleopa, Kleopas A
AU  - Kleopa KA
LA  - eng
GR  - R01NS43560/NS/NINDS NIH HHS/United States
GR  - R01 NS042878/NS/NINDS NIH HHS/United States
GR  - NS50345/NS/NINDS NIH HHS/United States
GR  - R01 NS055284-02/NS/NINDS NIH HHS/United States
GR  - R01 NS055284/NS/NINDS NIH HHS/United States
GR  - K02 NS050345-05/NS/NINDS NIH HHS/United States
GR  - R01 NS050705/NS/NINDS NIH HHS/United States
GR  - K02 NS050345/NS/NINDS NIH HHS/United States
GR  - R01 NS043560/NS/NINDS NIH HHS/United States
GR  - NS050705/NS/NINDS NIH HHS/United States
GR  - R01 NS050705-05/NS/NINDS NIH HHS/United States
GR  - NS42878/NS/NINDS NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20080215
PL  - United States
TA  - Neurobiol Dis
JT  - Neurobiology of disease
JID - 9500169
RN  - 0 (Connexins)
RN  - 0 (GJC3 protein, human)
RN  - 0 (Nerve Tissue Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Cell Communication/genetics
MH  - Connexins/*biosynthesis/genetics/physiology
MH  - Gene Expression Regulation/*physiology
MH  - HeLa Cells
MH  - Humans
MH  - Molecular Sequence Data
MH  - *Mutation
MH  - Nerve Tissue Proteins/*biosynthesis/genetics/physiology
MH  - Oligodendroglia/chemistry/*physiology
MH  - Gap Junction beta-1 Protein
PMC - PMC2704064
MID - NIHMS50241
EDAT- 2008/03/21 09:00
MHDA- 2008/10/14 09:00
PMCR- 2009/06/30
CRDT- 2008/03/21 09:00
PHST- 2007/03/29 00:00 [received]
PHST- 2008/01/23 00:00 [revised]
PHST- 2008/01/26 00:00 [accepted]
PHST- 2008/03/21 09:00 [pubmed]
PHST- 2008/10/14 09:00 [medline]
PHST- 2008/03/21 09:00 [entrez]
PHST- 2009/06/30 00:00 [pmc-release]
AID - S0969-9961(08)00018-1 [pii]
AID - 10.1016/j.nbd.2008.01.009 [doi]
PST - ppublish
SO  - Neurobiol Dis. 2008 May;30(2):221-33. doi: 10.1016/j.nbd.2008.01.009. Epub 2008 
      Feb 15.