Long-chain acyl CoA synthetase in microsomes from rat brain gray matter and white matter

1985 ◽  
Vol 10 (3) ◽  
pp. 377-386 ◽  
Author(s):  
T. Sanjeeva Reddy ◽  
Nicolas G. Bazan
Keyword(s):  
White Matter ◽  
Rat Brain ◽  
Gray Matter ◽  
Chain Acyl ◽  
Long Chain

Long-chain acyl CoA's and free fatty acids in rat brain after head injury

1997 ◽  
Vol 237 ◽  
pp. S25
Author(s):  
H. Heller ◽  
J. Deutsch ◽  
A.D. Purdon ◽  
S.I. Rapoport ◽  
M. Horowitz ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Head Injury ◽  
Free Fatty Acids ◽  
Rat Brain ◽  
Chain Acyl ◽  
Long Chain

Molecular Cloning and Expression of cDNAs Encoding Rat Brain and Liver Cytosolic Long-Chain Acyl-CoA Hydrolases

1997 ◽  
Vol 232 (1) ◽  
pp. 198-203 ◽  
Author(s):  
Junji Yamada ◽  
Takao Furihata ◽  
Noriko Iida ◽  
Takafumi Watanabe ◽  
Masakiyo Hosokawa ◽  
...  
Keyword(s):  
Rat Brain ◽  
Molecular Cloning ◽  
Cloning And Expression ◽  
Rat Brain And Liver ◽  
Chain Acyl ◽  
Long Chain

Long-Chain Acyl-CoA Hydrolase from Rat Brain Cytosol: Purification, Characterization, and Immunohistochemical Localization

1996 ◽  
Vol 326 (1) ◽  
pp. 106-114 ◽  
Author(s):  
Junji Yamada ◽  
Takao Furihata ◽  
Hiroshi Tamura ◽  
Takafumi Watanabe ◽  
Tetsuya Suga
Keyword(s):  
Rat Brain ◽  
Immunohistochemical Localization ◽  
Chain Acyl ◽  
Coa Hydrolase ◽  
Brain Cytosol ◽  
Long Chain

scholarly journals Widespread distribution of the major polypeptide component of MAP 1 (microtubule-associated protein 1) in the nervous system.

1984 ◽  
Vol 98 (1) ◽  
pp. 320-330 ◽  
Author(s):  
G S Bloom ◽  
T A Schoenfeld ◽  
R B Vallee
Keyword(s):  
Spinal Cord ◽  
Nervous System ◽  
Cerebral Cortex ◽  
White Matter ◽  
Rat Brain ◽  
Brain Tissue ◽  
Gray Matter ◽  
Neuronal Morphology ◽  
Double Labeling ◽  
Brain And Spinal Cord

We prepared a monoclonal antibody to microtubule-associated protein 1 (MAP 1), one of the two major high molecular weight MAP found in microtubules isolated from brain tissue. We found that MAP 1 can be resolved by SDS PAGE into three electrophoretic bands, which we have designated MAP 1A, MAP 1B, and MAP 1C in order of increasing electrophoretic mobility. Our antibody recognized exclusively MAP 1A, the most abundant and largest MAP 1 polypeptide. To determine the distribution of MAP 1A in nervous system tissues and cells, we examined tissue sections from rat brain and spinal cord, as well as primary cultures of newborn rat brain by immunofluorescence microscopy. Anti-MAP 1A stained white matter and gray matter regions, while a polyclonal anti-MAP 2 antibody previously prepared in this laboratory stained only gray matter. This confirmed our earlier biochemical results, which indicated that MAP 1 is more uniformly distributed in brain tissue than MAP 2 (Vallee, R.B., 1982, J. Cell Biol., 92:435-442). To determine the identity of cells and cellular processes immunoreactive with anti-MAP 1A, we examined a variety of brain and spinal cord regions. Fibrous staining of white matter by anti-MAP 1A was generally observed. This was due in part to immunoreactivity of axons, as judged by examination of axonal fiber tracts in the cerebral cortex and of large myelinated axons in the spinal cord and in spinal nerve roots. Cells with the morphology of oligodendrocytes were brightly labeled in white matter. Intense staining of Purkinje cell dendrites in the cerebellar cortex and of the apical dendrites of pyramidal cells in the cerebral cortex was observed. By double-labeling with antibodies to MAP 1A and MAP 2, the presence of both MAP in identical dendrites and neuronal perikarya was found. In primary brain cell cultures anti-MAP 2 stained predominantly cells of neuronal morphology. In contrast, anti-MAP 1A stained nearly all cells. Included among these were neurons, oligodendrocytes and astrocytes as determined by double-labeling with anti-MAP 1A in combination with antibody to MAP 2, myelin basic protein or glial fibrillary acidic protein, respectively. These results indicate that in contrast to MAP 2, which is specifically enriched in dendrites and perikarya of neurons, MAP 1A is widely distributed in the nervous system.

Neuron-specific distribution of long-chain acyl-CoA hydrolase in rat brain

1998 ◽  
Vol 31 ◽  
pp. S135
Author(s):  
Junji Yamada ◽  
Yu Kuramochi ◽  
Michiko Hirata ◽  
Takafumi Watanabe ◽  
Tetsuya Suga
Keyword(s):  
Rat Brain ◽  
Specific Distribution ◽  
Chain Acyl ◽  
Coa Hydrolase ◽  
Long Chain

scholarly journals Preliminary Observations on Sensitivity and Specificity of Magnetization Transfer Asymmetry for Imaging Myelin of Rat Brain at High Field

2015 ◽  
Vol 2015 ◽  
pp. 1-10 ◽  
Author(s):  
Jae-Woong Kim ◽  
Jiye Choi ◽  
Janggeun Cho ◽  
Chulhyun Lee ◽  
Daejong Jeon ◽  
...  
Keyword(s):  
White Matter ◽  
Rat Brain ◽  
Clinical Application ◽  
Sensitivity And Specificity ◽  
Gray Matter ◽  
High Field ◽  
Magnetization Transfer ◽  
High Sensitivity ◽  
Magnetization Transfer Ratio ◽  
Myelin Imaging

Magnetization transfer ratio (MTR) has been often used for imaging myelination. Despite its high sensitivity, the specificity of MTR to myelination is not high because tissues with no myelin such as muscle can also show high MTR. In this study, we propose a new magnetization transfer (MT) indicator, MT asymmetry (MTA), as a new method of myelin imaging. The experiments were performed on rat brain at 9.4 T. MTA revealed high signals in white matter and significantly low signals in gray matter and muscle, indicating that MTA has higher specificity than MTR. Demyelination and remyelination studies demonstrated that the sensitivity of MTA to myelination was as high as that of MTR. These experimental results indicate that MTA can be a good biomarker for imaging myelination. In addition, MTA images can be efficiently acquired with an interslice MTA method, which may accelerate clinical application of myelin imaging.

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