Results 121 to 130 of about 6,136 (180)
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Myelin proteolipid protein—the first 50 years
The International Journal of Biochemistry & Cell Biology, 2002Myelin proteolipid protein (PLP), the most abundant protein of central nervous system (CNS) myelin, is a hydrophobic integral membrane protein. Because of its physical properties, which make it difficult to work with, progress towards determining the exact function(s) and disease associations of myelin PLP has been slow.
Greer, Judith M., Lees, Marjorie B.
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Electroblot analysis of the myelin proteolipid protein
Journal of Neuroscience Research, 1982AbstractThe myelin proteolipid has been studied by the electroblot method of Towbin et al [1979]. Samples were separated by SDS–polyacrylamide gel electrophoresis, transferred to nitrocellulose, and incubated with proteolipid antibody. The proteolipid band could be identified immunologically in CNS myelin and in whole brain homogenates.
W B, Macklin, P E, Braun, M B, Lees
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Minireview: Autoimmune responses to myelin proteolipid protein
Neurochemical Research, 1994The authors present a brief historical sketch of the development of our understanding of immune responses to myelin proteolipid protein (PLP) and the acceptance of PLP as a potent antigen in the induction of experimental allergic encephalomyelitis (EAE). The distinct characteristics of the PLP molecule that may contribute to complex immune responses to
Sobel, RA, Greer, JM, Kuchroo, VK
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Developmental Neuroscience, 1998
Sequences from the first intron of the mouse myelin proteolipid protein (PLP) gene were examined for their ability to modulate PLP gene expression. Glial (N20.1) or nonglial (NIH 3T3) cells were transiently transfected with constructs that contained 1.4 kb of PLP promoter sequence driving luciferase reporter gene expression, as well as various portions
P A, Wight, A, Dobretsova
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Sequences from the first intron of the mouse myelin proteolipid protein (PLP) gene were examined for their ability to modulate PLP gene expression. Glial (N20.1) or nonglial (NIH 3T3) cells were transiently transfected with constructs that contained 1.4 kb of PLP promoter sequence driving luciferase reporter gene expression, as well as various portions
P A, Wight, A, Dobretsova
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Interaction of myelin basic protein and proteolipid protein
Journal of Neuroscience Research, 1989AbstractThe interaction of myelin basic protein (MBP) and proteolipid protein (PLP) was studied using a microtitre well binding assay and the ligand‐blot overlay technique. The binding of iodinated PLP to MBP that was immobilized on microtitre wells was saturable and reversible.
A M, Edwards +3 more
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Myelin proteolipid protein induces demyelinating disease in mice
Journal of the Neurological Sciences, 1987Using two methods of immunization (A and B), 5/10 (A) and 27/45 (B), BALB/c by J mice immunized with human myelin proteolipid protein developed a demyelinating disease with a spectrum of chronic progressive to relapsing-remitting courses. Demyelinative lesions were seen histopathologically in all clinically affected animals that were examined.
J L, Trotter +4 more
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Regulation of murine myelin proteolipid protein gene expression
Journal of Neuroscience Research, 1997To identify putative sequences that direct cell type-specific expression and/or enhance proteolipid protein (PLP) gene expression, glial or nonglial cells were transfected with various PLP-luciferase constructs that collectively span the entire mouse PLP-specific DNA present in a transgene known to direct cell type specificity in transgenic mice. These
P A, Wight, A, Dobretsova, W B, Macklin
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Myelin Proteolipid Protein Contains Thioester‐Linked Fatty Acids
Journal of Neurochemistry, 1990Abstract: Myelin proteolipid protein (PLP) is known to contain long‐chain, covalently bound fatty acids. Previous studies, including our own, have suggested the occurrence of an oxyester type of linkage between fatty acids and PLP. However, we found that protein‐SH groups are required in the acylation reaction, suggesting the possible presence of ...
O A, Bizzozero, L K, Good
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Regulation of rodent myelin proteolipid protein gene expression
Neuroscience Letters, 1992The regulation of rodent proteolipid protein (PLP) gene expression was studied during rat development and in cultured cells. Nuclear run-on assays demonstrate a strong transcriptional component associated with the developmental regulation of the PLP mRNA.
J L, Cook +2 more
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Deacylation of myelin proteolipid protein in organic solvents
Journal of Neuroscience Research, 1985AbstractA procedure has been developed for the deacylation of the hydrophobic, myelin proteolipid apoprotein using hydroxylamine in an alkaline organic solvent medium. Complete removal of covalently bound fatty acids was obtained after 4 hr of treatment.
O A, Bizzozero +3 more
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