Serum IgG antibody to ganglioside GQ1b is a possible marker of Miller Fisher syndrome
- A. Chiba, S. Kusunoki, Teruo Shimizu, I. Kanazawa
- Biology, MedicineAnnals of Neurology
- 1 June 1992
Increased activity of IgG antibody against ganglioside GQ1b was present in the early phase and reduced with time, whereas such activity was not detected in normal control subjects and disease control subjects including those with Guillain‐Barrë syndrome.
Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity.
A method to detect protein O-mannosyltransferase activity in mammalian cells was developed and it was shown that coexpression of both PomT1 and POMT2 was necessary for the enzyme activity, but expression of either POM t1 or POMt2 alone was insufficient.
Differential regulation of expression of hyaluronan-binding proteoglycans in developing brain: aggrecan, versican, neurocan, and brevican.
- P. Milev, P. Maurel, R. U. Margolis
- BiologyBiochemical and Biophysical Research…
- 18 June 1998
Striking and distinctive changes in the concentrations of the different members of this family of structurally related proteoglycans in developing brain, including changes in opposite directions for versican mRNA splice variants, indicate that the individual proteoglyCans and their isoforms probably serve unique functions during nervous tissue histogenesis.
High Affinity Binding and Overlapping Localization of Neurocan and Phosphacan/Protein-tyrosine Phosphatase-ζ/β with Tenascin-R, Amphoterin, and the Heparin-binding Growth-associated Molecule*
- P. Milev, A. Chiba, R. U. Margolis
- Biology, ChemistryJournal of Biological Chemistry
- 20 March 1998
Differences in the interactions of neurocan and phosphacan with the two major members of the tenascin family of extracellular matrix proteins are revealed, and it is suggested that chondroitin sulfate proteoglycans play an important role in the binding and/or presentation of differentiation factors in the developing central nervous system.
Serum anti-GQ1b IgG antibody is associated with ophthalmoplegia in Miller Fisher syndrome and Guillain-Barré syndrome: Clinical and immunohistochemical studies
- A. Chiba, S. Kusunoki, H. Obata, R. Machinami, I. Kanazawa
- MedicineNeurology
- 16 August 2011
Ganglioside composition of the human cranial nerves, with special reference to pathophysiology of Miller Fisher syndrome
- A. Chiba, S. Kusunoki, H. Obata, R. Machinami, I. Kanazawa
- Medicine, BiologyBrain Research
- 16 January 1997
Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin.
- A. Chiba, K. Matsumura, T. Endo
- Biology, ChemistryJournal of Biological Chemistry
- 1997
The major sialylated O-glycosidically-linked oligosaccharide of the alpha-dystroglycan was a novel O-mannosyl-type oligosACcharide, the structure of which was Siaalpha2-3Gal beta1-4GlcNAcbeta1-2Man-Ser/Thr (where Sia is sialic acid).
GM1b is a new member of antigen for serum antibody in Guillain-Barre syndrome
- S. Kusunoki, M. Iwamori, A. Chiba, S. Hitoshi, M. Arita, I. Kanazawa
- Biology, MedicineNeurology
- 1 July 1996
Antibody to a minor monosialoganglioside, GM1b, was found to be a useful diagnostic marker for Guillain-Barre syndrome and further study is needed to determine whether this antibody plays a role in the pathogenetic mechanism of the syndrome.
Serum anti‐GQ1b IgG antibody is associated with ophthalmoplegia in Miller Fisher syndrome and Guillain‐Barré syndrome
- A. Chiba, S. Kusunoki, H. Obata, R. Machinami, I. Kanazawa
- Medicine, BiologyNeurology
- 1 October 1993
It is concluded that serum IgG antibody against GQ1b is very closely associated with acute postinfectious ophthalmoplegia in MFS and GBS and with other neurologic or non-neurologic disorders.
Structures of Sialylated O-Linked Oligosaccharides of Bovine Peripheral Nerve α-Dystroglycan
- A. Chiba, K. Matsumura, T. Endo
- Biology, ChemistryJournal of Biological Chemistry
- 24 January 1997
The major sialylated O-glycosidically-linked oligosaccharide of the α-dystroglycan was a novel O-mannosyl-type oligosACcharide, the structure of which was Siaα2-3Gal β1-4GlcNAcβ1-2Man-Ser/Thr (where Sia is sialic acid).
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