Isolation and Characterization of Myelin

Norton, William T.; Cammer, Wendy

doi:10.1007/978-1-4757-1830-0_5

Cited by 273 publications

(233 citation statements)

References 320 publications

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“…Neurocan and brevican are highly expressed in embryonic brain and adult cerebellum, respectively (21,47). Sulfatides are a major component of myelin (48) and are expressed in oligodendrocytes and Schwann cells in culture (49,50). Versican has been shown to be expressed in cultured oligodendrocytes and Schwann cells (51,52) and brevican in oligodendrocytes (53).…”

Section: Discussionmentioning

confidence: 99%

The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion

Miura

Aspberg

Ethell

et al. 1999

Journal of Biological Chemistry

107

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The lecticans are a group of chondroitin sulfate proteoglycans characterized by the presence of C-type lectin domains. Despite the suggestion that their lectin domains interact with carbohydrate ligands, the identity of such ligands has not been elucidated. We previously showed that brevican, a nervous system-specific lectican, binds the surface of B28 glial cells (Yamada, H., Fredette, B., Shitara, K., Hagihara, K., Miura, R., Ranscht, B., Stallcup, W. B., and Yamaguchi, Y. (1997) J. Neurosci. 17, 7784 -7795). In this paper, we demonstrate that two classes of sulfated glycolipids, sulfatides and HNK-1-reactive sulfoglucuronylglycolipids (SGGLs), act as cell surface receptors for brevican. The lectin domain of brevican binds sulfatides and SGGLs in a calcium-dependent manner as expected of a C-type lectin domain. Intact, full-length brevican also binds both sulfatides and SGGLs. The lectin domain immobilized as a substrate supports adhesion of cells expressing SGGLs or sulfatides, which was inhibited by monoclonal antibodies against these glycolipids or by treatment of the substrate with SGGLs or sulfatides. Our findings demonstrate that the interaction between the lectin domains of lecticans and sulfated glycolipids comprises a novel cell substrate recognition system, and suggest that lecticans in extracellular matrices serve as substrate for adhesion and migration of cells expressing these glycolipids in vivo.The lecticans are a family of chondroitin sulfate proteoglycans (CSPGs) 1 characterized by the presence of a C-type lectin domain in their core proteins (1, 2). The C-terminal globular domains of lecticans, or "proteoglycan lectin domain" (PLD), consist of one or two epidermal growth factor (EGF)-like domains, a C-type lectin domain, and a complement regulatory protein (CRP) domain. This arrangement of domains is similar to that of selectins, suggesting that lecticans are also involved in the recognition of carbohydrate ligands.Lecticans are the most abundantly expressed family of proteoglycans in the nervous system. The lectican family includes aggrecan (3), versican (4), neurocan (5), and brevican (6), all of which are expressed in the nervous system at certain stages of development (1, 7). Although aggrecan and versican were initially characterized as connective tissue proteoglycans, their expression in the nervous system has been demonstrated in a number of reports (8 -12). Brevican and neurocan are specifically expressed in the nervous system (6, 13-15). Structural similarities with selectins and the abundant expression in the nervous system suggest that lecticans play major roles in carbohydrate recognition in the nervous system.The identity of the ligand to PLDs has been a focus of our interest. We previously showed that the PLD of versican binds tenascin-R, an extracellular matrix (ECM) protein predominantly expressed in the nervous system (16). More recently, we demonstrated that the PLDs of all lecticans bind tenascin-R, and that brevican and tenascin-R indeed form a complex in adult rat brain e...

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Section: Discussionmentioning

confidence: 99%

The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion

Miura

Aspberg

Ethell

et al. 1999

Journal of Biological Chemistry

107

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“…It is well established that both the GPI-anchored isoform of NCAM (NCAM 120; Ref. 41) and 5Ј-nucleotidase are synthesized by oligodendrocytes and found in myelin (3,22,(42)(43)(44).…”

Section: Oligodendroglial Cells Synthesize a Variety Of Gpi-anchoredmentioning

confidence: 99%

“…In addition, the GPI-anchored protein F3, galactocerebroside and sulfatide appear to be co-localized in double immunofluorescence stainings of cultured oligodendrocytes (45). 3 Two groups have recently generated mice deficient in the enzyme ceramide galactosyl transferase (59,60). These mice are unable to synthesize galactocerebroside and sulfatide.…”

Section: Specific Lipid Association Of Gpi-anchored Proteins In Oligomentioning

confidence: 99%

“…VIP 21/caveolin, which was initially thought to play a role in the formation of such complexes, has been reported to be absent from brain (17,47) and expressed neither in oligodendrocytes nor myelin. 3 For several cell types, including neuroblastoma cells, lymphocytes, and epithelial cells, glycosphingolipid-rich, detergent-insoluble microdomains have been shown to exist independently of caveolae and the expression of VIP 21/caveolin (16,47,48,61,62). For such caveolin-independent microdomains, it is feasible that other unknown proteins might be involved in their formation.…”

Section: Specific Lipid Association Of Gpi-anchored Proteins In Oligomentioning

confidence: 99%

“…In the central nervous system (CNS) 1 it is synthesized by oligodendrocytes, and in the peripheral nervous system it is synthesized by Schwann cells as a specialized domain of the plasma membrane (1). In contrast to most plasma membranes, myelin is enriched in lipids, which comprise 70% of the dry weight, and contains a restricted pattern of proteins when compared with the oligodendrocyte (2,3). During myelination, large diameter axons are encircled by the myelinating glial cell process.…”

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confidence: 99%

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Oligodendrocytes Direct Glycosyl Phosphatidylinositol-anchored Proteins to the Myelin Sheath in Glycosphingolipid-rich Complexes

Krämer¹,

Koch²,

Niehaus

et al. 1997

Journal of Biological Chemistry

118

127

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The myelin sheath synthesized by oligodendrocytes insulates central nervous system axons and is a specialized subdomain of the plasma membrane, containing a restricted pattern of proteins and lipids. Myelin is enriched in glycosphingolipids and cholesterol, a lipid environment favored by glycosylphosphatidylinositol (GPI)-anchored proteins, which associate with these lipids in detergent-insoluble complexes in many cell types. Since proteins regulating oligodendroglia-neuron interaction are largely unknown and GPI-anchored proteins are often involved in cell-cell interactions, we examined oligodendrocytes and myelin for their expression of these proteins. Oligodendrocyte precursors and maturing oligodendrocytes express a similar pattern of GPIanchored proteins, which unlike the majority of oligodendrocyte plasma membrane proteins, accumulate in myelin. To elucidate mechanisms underlying the expression of GPI-anchored proteins in myelin, we analyzed detergent-insoluble complexes from cells and myelin using TX-100 extraction and sucrose density gradients. In precursor cells, the GPI-anchored proteins are not incorporated in detergent-insoluble complexes. In contrast, GPI-anchored proteins from maturing oligodendrocytes and from myelin were isolated as complexes associated with glycosphingolipids and cholesterol. These results show a specific association of GPI-anchored proteins with glycosphingolipids and cholesterol during oligodendrocyte maturation and suggest sorting of these macromolecular complexes to myelin.

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Galactolipids in the formation and function of the myelin sheath

Dupree

Suzuki

Popko

1998

Microsc. Res. Tech.

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Among the most abundant components of myelin are the galactolipids galactocerebroside (GalC) and sulfatide. In spite of this abundance, the roles that these molecules play in the myelin sheath are not well understood. Until recently, our concept of GalC and sulfatide functions had been principally defined by immunological and chemical perturbation studies that implicate these lipids in oligodendrocyte differentiation, myelin formation, and myelin stability. Recently, however, genetic studies have allowed us to re‐analyze the functions of these lipids. Two laboratories have independently generated mice that are incapable of synthesizing either GalC or sulfatide by inactivating the gene encoding the enzyme UDP‐galactose:ceramide galactosyltransferase (CGT), which is required for myelin galactolipid synthesis. These galactolipid‐deficient animals exhibit a severe tremor, hindlimb paralysis, and display electrophysiological deficits in both the central and peripheral nervous systems. In addition, ultrastructural studies have revealed hypomyelinated white matter tracts with unstable myelin sheaths and a variety of myelin abnormalities including altered node length, reversed lateral loops, and compromised axo‐oligodendrocytic junctions. Collectively, these observations indicate that cell‐cell interactions, which are essential in the formation and maintenance of a properly functioning myelin sheath, are compromised in these galactolipid‐deficient mice. Microsc. Res. Tech. 41:431–440, 1998. © 1998 Wiley‐Liss, Inc.

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Isolation and Characterization of Myelin

Cited by 273 publications

References 320 publications

The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion

The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion

Oligodendrocytes Direct Glycosyl Phosphatidylinositol-anchored Proteins to the Myelin Sheath in Glycosphingolipid-rich Complexes

Galactolipids in the formation and function of the myelin sheath

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