In vivo acylation of proteolipid protein and DM-20 in myelin and myelin subfractions of developing rat brain: Immunoblot identification of acylated PLP and DM-20

1983 ◽  
Vol 8 (5) ◽  
pp. 649-659 ◽  
Author(s):  
Margaret M. Garwood ◽  
William R. Gilbert ◽  
Harish C. Agrawal





1974 ◽  
Vol 142 (3) ◽  
pp. 499-507 ◽  
Author(s):  
M. I. Sabri ◽  
A. H. Bone ◽  
A. N. Davison

1. Protein metabolism of myelin and other subcellular components from developing rat brain was studied for periods from 5h to 210 days after intraperitoneal injection of [3H]lysine and [14C]glucose. 2. Half-lives for total brain proteins (t0.5) were 27 days after [3H]lysine and 4 days after [14C]glucose injection. 3. Factors accounting for the difference in the turnover rates obtained with different precursors, and the problem of reutilization of the label were investigated. 4. The catabolism of purified myelin proteins was studied and the half-lives of individual myelin proteins were calculated. 5. Myelin basic proteins turned over at two different rates. Half-life of the fast component of myelin basic proteins was 19–22 days and the slow component exhibited a high degree of metabolic stability. 6. Proteolipid protein underwent slow turnover. High-molecular-weight Wolfgram (1966) proteins underwent (relatively) fast metabolism (t0.5 of 17–22 days).



1997 ◽  
Vol 137 (2) ◽  
pp. 459-468 ◽  
Author(s):  
Bruce D. Trapp ◽  
Akiko Nishiyama ◽  
David Cheng ◽  
Wendy Macklin

Previous studies have indicated that newly formed oligodendrocytes are dynamic cells whose production, survival, and differentiation depend upon axonal influences. This study has characterized the appearance and fate of newly formed oligodendrocytes in developing rat brain. Oligodendrocytes appear in predictable locations and radially extend DM-20–positive processes that cover 80-μm domains in the cortex and 40-μm domains in the corpus callosum. These premyelinating oligodendrocytes have one of two fates: they myelinate axons or degenerate. Between 7 and 21 d after birth, ∼20% of premyelinating oligodendrocytes identified in the cerebral cortex were degenerating. Oligodendrocytes that ensheathed axons expressed and selectively targeted proteolipid protein to compact myelin and did not degenerate. These observations support the hypothesis that axonal influences affect oligodendrocyte survival, differentiation, and expression of proteolipid protein gene products.



2006 ◽  
Vol 10 (1) ◽  
pp. 17-29 ◽  
Author(s):  
Ursula Felderhoff-Mueser ◽  
Deanna L. Taylor ◽  
Kirsty Greenwood ◽  
Mary Kozma ◽  
Dietger Stibenz ◽  
...  


1976 ◽  
Vol 154 (2) ◽  
pp. 319-325 ◽  
Author(s):  
M S. Patel ◽  
O E. Owen

The effect of hyperphenylalaninaemia on the metabolism of ketone bodies in vivo and in vitro by developing rat brain was investigated. The incorporation in vivo of [14C]acetoacetate into cerebral lipids was decreased by both chronic (for 3 days) and acute (for 6h) hyperphenylalaninaemia induced by injecting phenylalanine into 1-week-old rats. In studies in vitro it was observed that the incorporation of the radioactivity from [14C]acetoacetate and 3-hydroxy[14C]butyrate into cerebral lipids was inhibited by phenyl-pyruvate, but not by phenylalanine. Phenylpyruvate also inhibited the incorporation of 3H from 3H2O into lipids by brain slices metabolizing either 3-hydroxybutyrate or acetoacetate in the presence of glucose. These findings suggest that the decrease in the incorporation in vivo of [14C]acetoacetate into cerebral lipids in hyperphenylalaninaemic rats is most likely caused by phenylpyruvate and not by phenylalanine. Phenylpyruvate as well as phenylalanine had no inhibitory effects on ketone-body-catabolizing enzymes, namely 3-hydroxybutyrate dehydrogenase, 3-oxo acid CoA-transferase and acetoacetyl-CoA thiolase, in rat brain. Phenylpyruvate but not phenylalanine inhibited the activity of the 2-oxoglutarate dehydrogenase complex from rat and human brain. These findings suggest that the metabolism of ketone bodies is impaired in brains of untreated phenylketonuric patients, and in turn may contribute to the diminution of mental development and function associated with phenylketonuria.







1982 ◽  
Vol 257 (8) ◽  
pp. 4588-4592 ◽  
Author(s):  
H C Agrawal ◽  
C L Randle ◽  
D Agrawal


Neuroreport ◽  
2003 ◽  
Vol 14 (10) ◽  
pp. 1395-1399 ◽  
Author(s):  
Ryozo Tsuji ◽  
Marina Guizzetti ◽  
Lucio G. Costa


Sign in / Sign up

Export Citation Format

Share Document