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PubMed2001

Heterodi- [MAg, MAu (M = Pd, Pt)], Tri- [PdAg(2), PtAg(2), PtAu(2), Pt(2)M (M = Ni, Pt, Cd, Hg)], and Tetranuclear (Pt(2)Ag(2), Pt(2)Au(2)) 1,1-ethylenedithiolato complexes.

The reactions of [M(PPh(3))(2)[S(2)C=C[C(O)Me](2)]] [M = Pd (1a), Pt (1b)] with AgClO(4) and PPh(3) or with [Au(PPh(3))(OCMe(2))]ClO(4) afford heterodinuclear [[M(PPh(3))(2)][M'(PPh(3))][S(2)C=C[C(O)Me](2)]]ClO(4) [M = Pd, M' = Ag (2a), M = Pt, M' = Ag (2b), Au (4)] or trinuclear [[M(PPh(3))(2)][M'(PPh(3))](2)[S(2)C=C[C(O)Me](2)]](ClO(4))(2) [M = Pd, M' = Ag (3a), M = Pt, M' = Ag (3b), Au (5)] 1,1-ethylenedithiolato complexes, depending on the molar ratio of the reagents. We have recently reported that, in the absence of added PPh(3), the reactions of [Pt[S(2)C=C[C(O)Me](2)]L(2)] [L = PPh(3) (1b), L(2) = 1,5-cyclooctadiene (cod) (1c)] with AgClO(4) produce the heterotetranuclear derivatives [[PtL(2)](2)Ag(2)[S(2)C=C[C(O)Me](2)](2)]](ClO(4))(2) [L = PPh(3) (6a), L(2) = cod (6b)], which have been used now as efficient transmetallating agents toward gold, platinum, mercury, nickel, copper, or cadmium metal centers to give new types of 1,1-ethylenedithiolato complexes: [[Pt(PPh(3))(2)](2)Au(2)[S(2)C=C[C(O)Me](2)](2)](ClO(4))(2) (7), [(PtL(2))(2)M[S(2)C=C[C(O)Me](2)](2)](ClO(4))(2) [L(2) = cod, M = Pt (8), L = PPh(3), M = Hg (9)], [[Pt(PPh(3))(2)](2)[S(2)C=C[C(Me)=O](2)](2)Ni](ClO(4))(2) (10), and [[Pt(PPh(3))(2)](2)[S(2)C=C[C(Me)=O](2)](2)[M(OClO(3))(2)]] [M = Cu (11), [C(O)Me](2)] moieties but, whereas in 7 they bridge two gold(I) centers through the sulfur atoms, in 11 they chelate the copper(II) center through the oxygen atoms. The last one is the first example of such a coordination mode for the 2,2-diacetyl-1,1-ethylenedithiolato ligand.

Journal Article↗
PubMed1999

Total synthesis of a cholinergic neuron-specific ganglioside GT1a alpha: a high affinity ligand for myelin-associated glycoprotein (MAG).

An efficient total synthesis of a cholinergic neuron-specific ganglioside GT1a alpha (IV3NeuAcIII6NeuAcII3NeuAc-GgOse4Cer) is described. The suitably protected sialyl-alpha(2-->6)-gangliotriose (III6NeuAc-GgOse3) derivative was glycosylated with the phenyl 2-thioglycoside of sialic acid in the presence of N-iodosuccinimide (NIS) and trimethylsilyl trifluoromethane-sulfonate (TMSOTf) in acetonitrile medium, giving the disialogangliotriose (III6NeuAcII3NeuAc-GgOse3) derivative which contains both sialyl-alpha(2-->6)-GalNAc and sialyl-alpha(2-->3)-Gal structures (Route I). This pentasaccharide was efficiently synthesized also by the coupling of (methyl 5-acetamido-4,7,8,9-tetra-O-acetyl-3,5-dideoxy-D-glycero-alpha-D-galacto -2-nonulopyranosylonate)-(2-->6)-2-deoxy-3,4-O-isopropylidene-2-ph thalimido-D-galactopyranosyl trichloroacetimidate with 2-(trimethylsilyl)ethyl (methyl 5-acetamido-4,7,8,9-tetra-O-acetyl-3,5-dideoxy-D-glycero-alpha-D-galacto -2-nonulopyranosylonate)-(2-->3)-(2,6-di-O-benzyl-beta-D-galactopy ranosyl)-(1-->4)-2,3,6-tri-O-benzyl-beta-D-glucopyranoside, followed by conversion of the phthalimido group to the acetamido group (Route II). O-Deisopropylidenation and further glycosylation with methyl (methyl 5-acetamido-4,7,8,9-tetra-O-acetyl-3,5-dideoxy-D-glycero-alpha-D-gala ct-2-nonulopyranosylonate)-(2-->3)-2,4,6-tri-O-benzoyl-1-thio-b eta-D-galactopyranoside, promoted by dimethyl(methylthio)sulfonium triflate (DMTST), gave the desired trisialogangliotetraose (IV3NeuAcIII6NeuAcII3NeuAc-GgOse4) derivative, which was converted stepwise into the title ganglioside GT1a alpha by the introduction of the ceramide part and then complete deprotection. The ganglioside obtained was shown to be identical with the native GT1a alpha on TLC-immunostaining.

Animals↗
PubMedDate not supplied

Mag sulfate.

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Female↗
PubMed2005

Expression of MBP, PLP, MAG, CNP, and GFAP in the Human Alcoholic Brain.

BACKGROUND: Chronic and excessive alcohol misuse results in neuropathological damage in the cerebral cortex. The damage includes white matter loss, brain atrophy, and selective loss of neurons in the superior frontal gyrus. Chronic alcohol misuse also results in alterations in the expression of a number of genes, including a selective reprogramming of myelin gene expression in the frontal cortex. METHODS: The expression of cyclic nucleotide phosphodiesterase, glial fibrillary acidic protein, myelin-associated glycoprotein, myelin basic protein, and myelin proteolipid protein were assessed in the superior frontal gyrus and the primary motor cortex of control, uncomplicated alcoholic, and cirrhotic alcoholic cases. RESULTS: Overall, the expression of cyclic nucleotide phosphodiesterase, glial fibrillary acidic protein, myelin-associated glycoprotein, and myelin basic protein were significantly lower in the cirrhotic alcoholic cases compared with controls, with a similar tendency for myelin proteolipid protein. There was a strong correlation between the expression of the proteins studied and the brain weight of the individual case, but this interaction did not confound the overall analysis. There was no significant difference between controls and uncomplicated alcoholics. CONCLUSIONS: The loss of myelin proteins occurred without gross changes in brain pathology or brain weight and was not restricted to pathologically susceptible brain regions. It is not possible to determine whether the loss of myelin proteins in cirrhotic alcoholics is the result of cirrhosis per se or the combination of alcohol misuse and liver cirrhosis. Future studies comparing cases with alcoholic and nonalcoholic cirrhosis of the liver disease are required to elucidate this further.

2',3'-Cyclic-Nucleotide Phosphodiesterases↗
PubMed1987

Neural protein 1B236/myelin-associated glycoprotein (MAG) defines a subgroup of the immunoglobulin superfamily.

We have reviewed the structure and properties of the neural protein 1B236/MAG. This molecule consists largely of five Ig-like domains separated from its carboxyl terminal tail by a single membrane-spanning region. Two forms of the protein differ in the length and sequence of the carboxyl terminus: these are encoded by alternatively spliced mRNAs that are differentially expressed during postnatal neural development. The Ig-like domains of 1B236/MAG are unusual in having structural similarities to Ig V domains but with short Cys-Cys distances characteristic of C domains. Several other Ig-like molecules exhibit this structural feature, including the cell adhesion molecule N-CAM, which is most closely related in sequence to 1B236/MAG. We have proposed 1B236/MAG as the prototype for this subgroup of the Ig family and offer a model for this type of Ig domain structure. 1B236/MAG probably acts as a cell adhesion molecule to mediate interactions between cells in a fashion similar to that proposed for N-CAM. In particular, 1B236/MAG may be involved in interactions between myelinating oligodendrocytes or Schwann cells and axons or between adjacent layers of myelin membrane during the process of myelin compaction. It is most likely that the homophilic or heterophilic interactions of 1B236/MAG occur through binding to the Ig-like domains. The structure of 1B236/MAG is therefore quite consistent with its proposed function and may serve as the model for this class of cell-cell interaction molecules. One would predict, for example, that the neuron-glia cell adhesion molecule Ng-CAM, also known as NILE or L1 (Bock et al. 1985, Friedlander et al. 1985), which mediates interactions between neurons and glial cells, would have a very similar structure to those of N-CAM and 1B236/MAG. In addition, the carboxyl terminal tails of the 1B236/MAG proteins may also be involved in interactions with cytoskeletal components, during membrane vesicle transport through the glial cytoplasm during myelination or through neuronal axoplasm or cytoplasm. The availability of full-length cDNA clones of 1B236/MAG mRNAs with the ability to express these products in vitro will enable the structure and interactions of 1B236/MAG to be tested in detail.

Amino Acid Sequence↗
PubMed2004

SLOW-MAG.

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Calcium Channel Blockers↗