NDLI: Developmental regulation of myelin basic protein in dispersed cultures.

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Formation of 11-trans slow reacting substances.

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Selective inhibition of Escherichia coli protein synthesis and growth by nonionic oligonucleotides complementary to the 3' end of 16S rRNA.

Site-specific cleavage by T1 RNase of U-1 RNA in u-1 ribonucleoprotein particles.

Partial purification and characterization of human gamma (immune) interferon.

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Related 5S RNA transcription factors in Xenopus oocytes and somatic cells.

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Detection of a recombinant murine leukemia virus-related glycoprotein on virus-negative thymoma cells.

Developmental regulation of myelin basic protein in dispersed cultures.

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Developmental regulation of myelin basic protein in dispersed cultures.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Pfeiffer, S. E. Barbarese, E.
Abstract	The expression of myelin basic protein, a major component of the myelin membrane, was studied in the absence of myelin formation in a unique situation in which these two processes have been uncoupled. The oligodendrocytes that contained myelin basic protein were identified by immunofluorescence in primary dispersed cultures derived from 20-day-old fetal rat brain. Their number increased 20-fold between 15 and 34 days in culture. Morphologically identifiable myelin was never observed. The oligodendrocytes elaborated a complex network of processes and membranous sheets resembling 'unfurled' myelin. Myelin basic protein appeared concomitantly in the perikaryon, processes, and membranous sheets of the oligodendrocytes and remained distributed in these compartments throughout the culture period. The oligodendrocytes synthesized the four forms of myelin basic protein found in rodent brain with molecular weights of 21,500, 18,500, 17,000, and 14,000 and modulated their expression with time in culture. The onset of rapid myelin basic protein accumulation, as measured by radioimmunoassay, took place after 25 days in culture. Myelin basic protein accumulated at the rate of 0.2 fmol per oligodendrocyte per day and reached a level of 300 pmol/mg of protein by 34 days. By 60 days, the amount of myelin basic protein had declined to 100 pmol/mg of protein, a level maintained up until at least 120 days. When the amount of myelin basic protein was correlated with the number of oligodendrocytes, it was estimated that each induced cell contained on average 1 fmol of this protein at the three time points (15, 28, and 34 days in culture) at which cells were counted. Our results indicate that the accumulation, modulation of the molecular forms, and insertion of myelin basic protein into the membrane can occur in the absence of myelin formation, but that continued metabolic stability, subcellular sequestration, and fine control of the relative proportions of the different forms of myelin basic protein may be dependent on myelin morphogenesis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	78
Language	English
Publisher	National Academy of Sciences
Publisher Date	1981-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Brain Metabolism Myelin Basic Protein Biosynthesis Animals Antigen-Antibody Complex Cells, Cultured Fetus Fluorescent Antibody Technique Kinetics Molecular Weight Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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