Tamm-Horsfall protein, a kidney marker is expressed on brain sulfogalactosylceramide-positive astroglial structures

Zalc, B.; Collet, Agnès; Monge, M.; Ollier-Hartmann, M.-P.; Jacque, C.; Hartmann, L; Baumann, Nicole

doi:10.1016/0006-8993(84)90669-3

Cited by 22 publications

(8 citation statements)

References 19 publications

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“…The probable sources of vasopressin are circumventricular organs or vasopressinergic axons which terminate in the ependymal layer (Dubois-Dauphin et al, 1990;Lepetit et al, 1993). Little is known about ion and water transport mechanisms in ependymal cells which differ from those on choroid plexus and tanycytes (Barres et al, 1989;Cardy and Fifth, 1993;Nielson et al, 1993;Wenzel et al, 1970;Zalc et al, 1984).…”

Section: Movement Of Water Across Ependymamentioning

confidence: 96%

The ependyma: A protective barrier between brain and cerebrospinal fluid

Bigio

1995

Glia

289

182

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This review summarizes the current scientific literature concerning the ependymal lining of the cerebral ventricles of the brain with an emphasis on selective barrier function and protective roles for the common ependymal cell. Topics covered include the development, morphology, protein and enzyme expression including reactive changes, and pathology. Some cells lining the neural tube are committed at an early stage to becoming ependymal cells. They serve a secretory function and perhaps act as a cellular/axonal guidance system, particularly during fetal development. In the mature mammalian brain ependymal cells possess the structural and enzymatic characteristics necessary for scavenging and detoxifying a wide variety of substances in the CSF, thus forming a metabolic barrier at the brain-CSF interface.

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Section: Movement Of Water Across Ependymamentioning

confidence: 96%

The ependyma: A protective barrier between brain and cerebrospinal fluid

Bigio

1995

Glia

289

182

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“…Furthermore, a novel sulfated, sialylated, triantennary compound occurs, in which G a l 4 is 3-0-sulfated and Gal-6 6-0-sialylated (see N3.6.5 in Table 6). Interestingly, immunohistochemical studies using antibodies against 3-0-sulfated galactosylceramide and T-H glycoprotein, respectively, have shown a tightly linked topological association of 3-0-sulfated galactosylceramide and T-H glycoprotein in the kidney as well as in the brain (Zalc et al, 1984). In view of the presence of 3-0-sulfated galactose in T-H glycoprotein, attention has to be paid to the possibility that antibodies recognizing 3-0-sulfated galactosyl residues may also cross-react with T-H glycoprotein.…”

Section: Discussionmentioning

confidence: 99%

The Asn‐linked carbohydrate chains of human Tamm‐Horsfall glycoprotein of one male

Hård

Zadelhoff

Moonen

et al. 1992

European Journal of Biochemistry

277

154

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Human Tamm-Horsfall glycoprotein has been purified from the urine of one male. The Asn-linked carbohydrate chains were enzymically released by peptide-N4-(N-acetyl-~-glucosaminyl)asparagine amidase F, and separated from the remaining protein by gel-permeation chromatography on BioGel P-100. Fractionation of the intact (sulfated) sialylated carbohydrate chains was achieved by a combination of three liquid-chromatographic techniques, namely, anion-exchange FPLC on QSepharose, amine-adsorption HPLC on Lichrospher-NH2, and high-pH anion-exchange chromatography on CarboPac PA1. In total, more than 1 SO carbohydrate-containing fractions were obtained, some of which still contained mixtures of oligosaccharides. The primary structure of 30 N-glycans, including 10 novel oligosaccharides, were determined by one-and two-dimensional 'H-NMR spectroscopy at 500 MHz or 600 MHz. The types of compounds identified range from non-fucosylated, monosialylated, diantennary to fucosylated, tetrasialylated, tetraantennary carbohydrate chains, possessing the following terminal structural elements :NeuSAccl2 -3GalP1!-4GlcNAcPI - \ .The largest GalNAc-containing compound has the following structure : GalNAcPl

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“…using purified rabbit polyclonal antiGalC antibody prepa rations similar to the one used in the present study [Zalc et al. 1981[Zalc et al. .…”

Section: Discussionmentioning

confidence: 99%

Oligodendroglial Expression and Deposition of Four Major Myelin Constituents in the Myelin Sheath during Development

et al. 1986

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We have studied the sequence of expression in the oligodendrocyte of four myelin constituents: galactosylceramide (GalC), myelin basic protein (MBP), proteolipid protein (PLP) and Wolfgram protein (W₁). These investigations were performed on freshly dissociated cell preparations from mouse olfactory bulb and cerebellum before and during early myelinogenesis. Our data showed that the first myelin antigen to be detected in the oligodendrocyte was GalC, followed 24 h later by W₁ and after a 5-day time lag (relative to GalC) by MBP. Expression of PLP occurred shortly after that of MBP. This sequence of events was identical in the cerebellum and in the olfactory bulb, but it commenced earlier in the cerebellum (E18) than in the olfactory bulb (P2). Deposition of these components in the nascent myelin sheaths was studied on tissue sections. These histological preparations showed that the temporal order of deposition of the myelin constituents did not correlate with their order of expression in the oligodendrocyte. As judged both by the intensity of the labeling and the number of positive fibers, W₁ and MBP were the first antigens to be deposited, followed by PLP and finally by GalC. Furthermore, this deposition process was initiated immediately after completion of expression of these antigens in the oligodendrocyte.

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Tamm-Horsfall protein, a kidney marker is expressed on brain sulfogalactosylceramide-positive astroglial structures

Cited by 22 publications

References 19 publications

The ependyma: A protective barrier between brain and cerebrospinal fluid

The ependyma: A protective barrier between brain and cerebrospinal fluid

The Asn‐linked carbohydrate chains of human Tamm‐Horsfall glycoprotein of one male

Oligodendroglial Expression and Deposition of Four Major Myelin Constituents in the Myelin Sheath during Development

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