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Expression of apolipoprotein E during nerve degeneration and regeneration.

Authors :
Ignatius, M J
Gebicke-Härter, P J
Skene, J H
Schilling, J W
Weisgraber, K H
Mahley, R W
Shooter, E M
Source :
Proceedings of the National Academy of Sciences of the United States of America; February 1986, Vol. 83 Issue: 4 p1125-1129, 5p
Publication Year :
1986

Abstract

A 37-kDa glycoprotein has been described recently, whose synthesis is dramatically increased after injury of the rat sciatic and optic nerves. Cells in the nerve sheath, distal to the site of injury, produce and secrete large amounts of this protein, so that by 3 weeks after injury, it represents 2-5% of the total soluble extracellular protein in the regenerating sciatic nerve sheath, although it fails to accumulate in damaged optic nerve. Results presented here reveal extensive homology between the 37-kDa nerve injury-induced protein and a well-studied serum protein, apolipoprotein E (apoE), that is involved in lipid and cholesterol metabolism and that has been shown recently to be present in adult and developing rat astroglia. Both proteins have identical isoelectric focusing points and similar molecular masses. Antibodies raised against the 37-kDa protein recognize apoE and anti-apoE serum crossreacts with the 37-kDa protein. Sequence data for two 14 amino acid stretches of the 37-kDa protein match identical regions of apoE. These data suggest that the 37-kDa protein is identical to serum apoE and that it could have similar functions to the latter. In the nervous system, for example, it may be involved in the mobilization and reutilization of lipid in the repair, growth, and maintenance of myelin and axonal membranes, both during development and after injury.

Details

Language :
English
ISSN :
00278424 and 10916490
Volume :
83
Issue :
4
Database :
Supplemental Index
Journal :
Proceedings of the National Academy of Sciences of the United States of America
Publication Type :
Periodical
Accession number :
ejs60447510
Full Text :
https://doi.org/10.1073/pnas.83.4.1125