The neuronal adhesion protein TAG-1 is expressed by Schwann cells and oligodendrocytes and is localized to the juxtaparanodal region of myelinated fibers

被引:101
作者
Traka, M
Dupree, JL
Popko, B
Karagogeos, D
机构
[1] Univ Crete, Sch Med, Dept Basic Sci, Iraklion 71110, Crete, Greece
[2] Univ N Carolina, Ctr Neurosci, Chapel Hill, NC 27599 USA
[3] Fdn Res & Technol, Inst Mol Biol & Biotechnol, Iraklion 71110, Crete, Greece
关键词
glia; TAG-1; ensheathing; potassium channels; juxtaparanode; galactolipid; axoglial interactions;
D O I
10.1523/JNEUROSCI.22-08-03016.2002
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The neural cell adhesion molecule TAG-1, which is a glycosylphosphatidylinositol-linked member of the Ig superfamily, is expressed by various neuronal populations in the developing CNS and PNS. We demonstrate here that Schwann cells and oligodendrocytes also express TAG-1. In the PNS, TAG-1 is detected in ensheathing Schwann cells early postnatally and is maintained throughout adulthood. In mature myelinated fibers of the CNS and PNS, TAG-1 is localized to the juxtaparanodal region. The CNS of the UDP-galactose ceramide galactosyl transferase(-/-) (CGT(-/-)) mouse mutants, which do not synthesize the abundant galactolipids of myelin, display severely disrupted axoglial interactions at the paranodal region. In contrast, axoglial interactions in the PNS of these mutants are less affected. Interestingly, TAG-1 localization is completely undetected in myelinated fibers of the CNS. In the PNS of these mutants, TAG-1 abnormally localizes in the paranodal region. These data raise the intriguing possibility that TAG-1 localization in the juxtaparanodal area mediates, or at least requires, the axoglial contact normally displayed in this region. The abnormal localization of TAG-1 in the CGT mutants might contribute to the disrupted axoglial interactions observed in these animals.
引用
收藏
页码:3016 / 3024
页数:9
相关论文
共 49 条
[11]   Molecular composition of the node of Ranvier: Identification of ankyrin-binding cell adhesion molecules neurofascin (Mucin+ third FNIII domain-) and NrCAM at nodal axon segments [J].
Davis, JQ ;
Lambert, S ;
Bennett, V .
JOURNAL OF CELL BIOLOGY, 1996, 135 (05) :1355-1367
[12]   SPATIAL REGULATION OF AXONAL GLYCOPROTEIN EXPRESSION ON SUBSETS OF EMBRYONIC SPINAL NEURONS [J].
DODD, J ;
MORTON, SB ;
KARAGOGEOS, D ;
YAMAMOTO, M ;
JESSELL, TM .
NEURON, 1988, 1 (02) :105-116
[13]   Genetic dissection of myelin galactolipid function [J].
Dupree, JL ;
Popko, B .
JOURNAL OF NEUROCYTOLOGY, 1999, 28 (4-5) :271-279
[14]   Axo-glial interactions regulate the localization of axonal paranodal proteins [J].
Dupree, JL ;
Girault, JA ;
Popko, B .
JOURNAL OF CELL BIOLOGY, 1999, 147 (06) :1145-1151
[15]  
Dupree JL, 1998, J NEUROSCI, V18, P1642
[16]   The axonal membrane protein Caspr, a homologue of neurexin IV, is a component of the septate-like paranodal junctions that assemble during myelination [J].
Einheber, S ;
Zanazzi, G ;
Ching, W ;
Scherer, S ;
Milner, TA ;
Peles, E ;
Salzer, JL .
JOURNAL OF CELL BIOLOGY, 1997, 139 (06) :1495-1506
[17]   THE AXONAL GLYCOPROTEIN TAG-1 IS AN IMMUNOGLOBULIN SUPERFAMILY MEMBER WITH NEURITE OUTGROWTH PROMOTING ACTIVITY [J].
FURLEY, AJ ;
MORTON, SB ;
MANALO, D ;
KARAGOGEOS, D ;
DODD, J ;
JESSELL, TM .
CELL, 1990, 61 (01) :157-170
[18]   Heterophilic binding of L1 on unmyelinated sensory axons mediates schwann cell adhesion and is required for axonal survival [J].
Haney, CA ;
Sahenk, Z ;
Li, C ;
Lemmon, VP ;
Roder, J ;
Trapp, BD .
JOURNAL OF CELL BIOLOGY, 1999, 146 (05) :1173-1183
[19]   MYELIN MEMBRANE BIOGENESIS BY OLIGODENDROCYTES - DEVELOPMENTAL REGULATION OF LOW-MOLECULAR-WEIGHT GTP-BINDING PROTEINS [J].
HUBER, LA ;
MADISON, DL ;
SIMONS, K ;
PFEIFFER, SE .
FEBS LETTERS, 1994, 347 (2-3) :273-278
[20]   SCHWANN-CELL PRECURSORS AND THEIR DEVELOPMENT [J].
JESSEN, KR ;
MIRSKY, R .
GLIA, 1991, 4 (02) :185-194