Ultrastructural localization of hyaluronan in myelin sheaths of the rat central and rat and human peripheral nervous systems using hyaluronan-binding protein-gold and link protein-gold

Eggli, Peter; Lucocq, John M.; P, Ott; Graber, Werner; Zypen, E. van der

doi:10.1016/0306-4522(92)90417-z

Cited by 41 publications

(36 citation statements)

References 40 publications

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“…Ultrastructural studies have demonstrated the presence of both HA (Eggli et al, 1992) and HA-binding proteins in rat and human peripheral nerve myelin sheaths and in the periaxonal space between neurons and nonmyelinating Schwann cell plasma membranes (Eggli and Graber, 1996). Rat schwannoma cell lines and primary cultures of normal rat Schwann cells express HA (Sherman et al, 1995; and unpublished observations).…”

Section: Ha Expression and Functions In The Pnsmentioning

confidence: 96%

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Hyaluronate‐based extracellular matrix: Keeping glia in their place

Sherman

Struve

Rangwala

et al. 2002

Glia

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Section: Ha Expression and Functions In The Pnsmentioning

confidence: 96%

“…Numerous studies have identified HA as a component of CNS extracellular matrix, where it is expressed predominantly by astrocytes and possibly, to a lesser degree, by other glial cells (Asher et al, 1991;Eggli et al, 1992). The synthases responsible for this HA expression have not been identified.…”

Section: Ha Expression and Functions In The Cnsmentioning

confidence: 99%

Hyaluronate‐based extracellular matrix: Keeping glia in their place

Sherman

Struve

Rangwala

et al. 2002

Glia

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“…It is a non-sulfated, linear molecule comprised of repeating units of (β,1→4)-D-glucuronic acid-(β,1→3)-N-acetyl-D-glucosamine that reach sizes in excess of 10 6 Da. HA is localized around myelinated fibers in WM, while it is a component of perineuronal nets surrounding neuron cell bodies in GM (Asher et al 1991;Eggli et al 1992).…”

Section: Mechanisms Of Wm Changes During Normative Agingmentioning

confidence: 99%

Age-related changes in human and non-human primate white matter: from myelination disturbances to cognitive decline

Kohama

Rosene

Sherman

2011

AGE

121

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The cognitive decline associated with normal aging was long believed to be due primarily to decreased synaptic density and neuron loss. Recent studies in both humans and non-human primates have challenged this idea, pointing instead to disturbances in white matter (WM) including myelin damage. Here, we review both cross-sectional and longitudinal studies in humans and non-human primates that collectively support the hypothesis that WM disturbances increase with age starting at middle age in humans, that these disturbances contribute to age-related cognitive decline, and that age-related WM changes may occur as a result of free radical damage, degenerative changes in cells in the oligodendrocyte lineage, and changes in microenvironments within WM.

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“…HA is present at high levels within the developing vertebral column, the neural crest-derived mesenchyme of the craniofacial region, and the heart and smooth muscle throughout the midgestation embryo (52). In adult tissues, HA expression has been detected in tissues including brain and central nervous system, cartilage, skin, cardiac and skeletal muscle, lung, and lymph node (45,(53)(54)(55)(56)(57)(58).…”

Section: Fig 6 Southern Analysis Of Mouse Has2mentioning

confidence: 99%

Molecular Cloning and Characterization of a Putative Mouse Hyaluronan Synthase

Spicer

Augustine

McDonald

1996

Journal of Biological Chemistry

157

104

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We report the isolation of a novel mouse gene which encodes a putative hyaluronan synthase. The cDNA was identified using degenerate reverse transcriptase-polymerase chain reaction. Degenerate primers were designed based upon an alignment of the amino acid sequences of Streptococcus pyogenes HasA, Xenopus laevis DG42, and Rhizobium meliloti NodC. A mouse embryo cDNA library was screened with the resultant polymerase chain reaction product, and multiple cDNA clones spanning 3 kilobase pairs (kb) were isolated. The open reading frame predicted a 63-kDa protein with several transmembrane sequences, multiple consensus phosphorylation sites, and four putative hyaluronan binding motifs. The amino acid sequence displayed 55% identity to mouse HAS, 56% identity to Xenopus DG42, and 21% identity to Streptococcus HasA. Northern analysis identified transcripts of 4.8 kb and 3.2 kb, which were expressed highly in the developing mouse embryo and at lower levels in adult mouse heart, brain, spleen, lung, and skeletal muscle. Transfection experiments demonstrated that mouse Has2 could direct hyaluronan coat biosynthesis in transfected COS cells, as evidenced by a classical particle exclusion assay. These results suggest that mammalian HA synthase activity is regulated by at least two related genes. Accordingly, we propose the name Has2 for this gene.Hyaluronan (HA 1 ) is a linear unbranched polymer made up of repeating disaccharide units of D-glucuronic acid(␤133)Nacetylglucosamine(␤134). More than 60 years after the isolation of hyaluronan from the vitreous humor (1), its synthetic pathway remains incompletely characterized. HA is synthesized as a free, linear polymer at the inner face of the plasma membrane of eukaryotic cells and is subsequently extruded to the outside of the cell (2-7). HA biosynthesis in mammalian cells may be regulated in part through signaling cascades (8, 9).Certain bacteria can synthesize an HA polymer that is identical to the polymer synthesized by mammalian cells (10 -12). Indeed, investigation of HA biosynthesis in the Group A Streptococcus, Streptococcus pyogenes, has recently led to the identification and cloning of several genes that encode enzymes critical for HA biosynthesis in this bacterium (11). However, until very recently, no genes have been identified that encode enzymes with similar activities in mammalian cells.Degenerate reverse transcriptase-PCR has been a useful tool in the identification and cloning of many genes and gene families (13-15). This approach relies upon conserved sequences deduced from alignments of related gene or protein sequences. The hasA gene of S. pyogenes encodes hyaluronan synthase in this bacterium (11). Sequence analysis predicts that this protein is a membrane protein with a large intracellular loop encoding the active site of the enzyme (11). Similarly, in mammalian cells, the HA synthase has been localized to the plasma membrane, with the active site on the inner face of the membrane (4, 5). Data base searches have identified the Rhizobium sp. nodulation fa...

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Ultrastructural localization of hyaluronan in myelin sheaths of the rat central and rat and human peripheral nervous systems using hyaluronan-binding protein-gold and link protein-gold

Cited by 41 publications

References 40 publications

Hyaluronate‐based extracellular matrix: Keeping glia in their place

Hyaluronate‐based extracellular matrix: Keeping glia in their place

Age-related changes in human and non-human primate white matter: from myelination disturbances to cognitive decline

Molecular Cloning and Characterization of a Putative Mouse Hyaluronan Synthase

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