myelin-basic-protein and Muscular-Dystrophy--Animal

myelin-basic-protein has been researched along with Muscular-Dystrophy--Animal* in 2 studies

Other Studies

2 other study(ies) available for myelin-basic-protein and Muscular-Dystrophy--Animal

Article	Year
Microheterogeneity of myelin basic proteins in the partially myelinated spinal roots of the Bar Harbor 129 ReJ muscular dystrophic mouse. Neuroscience letters, 1990, Feb-16, Volume: 109, Issue:3 The protein composition of normal spinal roots and the partially myelinated spinal roots of Bar Harbor 129 ReJ dystrophic mice was analyzed by 2D-gel electrophoresis which resolved basic proteins. The normal roots contained proteins with mobilities identical to two of the three 18.5 kDa and two of the three 14 kDa myelin basic protein spots resolved in purified spinal cord myelin suggesting that normal root myelin may have some of the characteristics of CNS myelin. In contrast dystrophic roots contained spots with mobilities identical to only one of the spots resolved for each myelin basic protein. The possibility that the difference in microheterogeneity may be responsible for the decreased myelination is discussed. Topics: Animals; Mice; Molecular Weight; Muscular Dystrophy, Animal; Myelin Basic Protein; Nerve Fibers, Myelinated; Spinal Nerve Roots	1990
Calcium ion stimulated endogenous protein kinase catalyzed phosphorylation of peripheral and central nerve myelin proteins: comparison between normal and genetically dystrophic mouse. Enzyme, 1980, Volume: 25, Issue:2 Myelin isolated from the peripheral (PNS) and central nervous system (CNS) of mouse contained a protein kinase which catalyzed phosphorylation of myelin proteins. In the case of CNS myelin, small and large basic proteins were phosphorylated whereas in the case of PNS myelin, a glycoprotein (Po) as well as other basic proteins (P1 and P2) were phosphorylated. Ca2+, but not adenosine 3',5'-monophosphate (cyclic AMP), markedly (5- to 10-fold) stimulated phosphorylation of PNS and CNS myelin proteins. There was no difference between the normal and dystrophic mouse CNS myelin phosphorylation. However, a marked decrease in the cauda equina PNS myelin phosphorylation ofthe dystrophic mouse was observed. Interestingly, the dystrophic sciatic nerve myelin phosphorylation, compared to normal, was higher. Topics: Animals; Brain Stem; Calcium; Cauda Equina; Mice; Muscular Dystrophy, Animal; Myelin Basic Protein; Myelin Proteins; Phosphorylation; Protein Kinases; Sciatic Nerve; Spinal Cord	1980

Article

Year

Microheterogeneity of myelin basic proteins in the partially myelinated spinal roots of the Bar Harbor 129 ReJ muscular dystrophic mouse.

Neuroscience letters, 1990, Feb-16, Volume: 109, Issue:3

The protein composition of normal spinal roots and the partially myelinated spinal roots of Bar Harbor 129 ReJ dystrophic mice was analyzed by 2D-gel electrophoresis which resolved basic proteins. The normal roots contained proteins with mobilities identical to two of the three 18.5 kDa and two of the three 14 kDa myelin basic protein spots resolved in purified spinal cord myelin suggesting that normal root myelin may have some of the characteristics of CNS myelin. In contrast dystrophic roots contained spots with mobilities identical to only one of the spots resolved for each myelin basic protein. The possibility that the difference in microheterogeneity may be responsible for the decreased myelination is discussed.

Topics: Animals; Mice; Molecular Weight; Muscular Dystrophy, Animal; Myelin Basic Protein; Nerve Fibers, Myelinated; Spinal Nerve Roots

1990

Calcium ion stimulated endogenous protein kinase catalyzed phosphorylation of peripheral and central nerve myelin proteins: comparison between normal and genetically dystrophic mouse.

Enzyme, 1980, Volume: 25, Issue:2

Myelin isolated from the peripheral (PNS) and central nervous system (CNS) of mouse contained a protein kinase which catalyzed phosphorylation of myelin proteins. In the case of CNS myelin, small and large basic proteins were phosphorylated whereas in the case of PNS myelin, a glycoprotein (Po) as well as other basic proteins (P1 and P2) were phosphorylated. Ca2+, but not adenosine 3',5'-monophosphate (cyclic AMP), markedly (5- to 10-fold) stimulated phosphorylation of PNS and CNS myelin proteins. There was no difference between the normal and dystrophic mouse CNS myelin phosphorylation. However, a marked decrease in the cauda equina PNS myelin phosphorylation ofthe dystrophic mouse was observed. Interestingly, the dystrophic sciatic nerve myelin phosphorylation, compared to normal, was higher.

Topics: Animals; Brain Stem; Calcium; Cauda Equina; Mice; Muscular Dystrophy, Animal; Myelin Basic Protein; Myelin Proteins; Phosphorylation; Protein Kinases; Sciatic Nerve; Spinal Cord

1980