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Studies on Subcellular Fractions Which Are Involved in Myelin Assembly: Labeling of Myelin Proteins by a Double Radioisotope Approach Indicates Developmental Relationships
Author(s) -
Pereyra Pedro M.,
Braun Peter E.,
Greenfield S.,
Hogan E. L.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb09041.x
Subject(s) - myelin , proteolipid protein 1 , context (archaeology) , biochemistry , biology , leucine , myelin basic protein , membrane , microbiology and biotechnology , chemistry , neuroscience , central nervous system , amino acid , paleontology
The question of developmental relationships amongst myelin‐related membranes in subfractions of myelinating mouse brain (15 days) was investigated by a time‐staggered double isotope protocol using [ 3 H]leucine and [ 14 C]leucine. Preliminary results are interpreted and discussed in the context of a mathematical conceptualization of pulse‐labeling kinetic analyses of myelin proteins in subcellular membrane compartments. Differences in ratio of the two leucine labels among proteins of myelin‐containing subfractions are interpreted as confirming metabolic differences relating to various stages of development rather than precursor‐product relationships. The incorporation into myelin of 14K, 17K, and 18.5K basic proteins (MBPs) occurs with relatively short delay times, following their synthesis (less than 5 min), and seems to occur simultaneously into all compartments. The 21.5K MBP and the proteolipid protein, on the other hand, require 10–14 min and 14–20 min, respectively. A scheme is presented to illustrate the probable assignment of subfractions to various myelin “compartments” during myelination, and to serve as a working hypothesis for studies on precursor‐product relationships.