Protein phosphorylation: Localization in regenerating optic axons
Abstract
A number of axonal proteins display changes in phosphorylation during goldfish optic nerve regeneration. (1) To determine whether the phosphorylation of these proteins was closely linked to their synthesis in the retinal ganglion cell body, cycloheximide was injected intraocularly into goldfish whose optic nerves had been regenerating for 3 weeks. Cycloheximide reduced the incorporation of (3H)proline and 32P orthophosphate into total nerve protein by 84% and 46%, respectively. Of the 20 individual proteins examined, 17 contained less than 15% of the (3H)proline label measured in corresponding controls, whereas 18 proteins contained 50% or more of the 32P label, suggesting that phosphorylation was largely independent of synthesis. (2) To determine whether the proteins were phosphorylated in the ganglion cell axons, axonal transport of proteins was blocked by intraocular injection of vincristine. Vincristine reduced (3H)proline labeling of total protein by 88% and 32P labeling by 49%. Among the individual proteins (3H)proline labeling was reduced by 90% or more in 18 cases but 32P labeling was reduced only by 50% or less. (3) When 32P was injected into the cranial cavity near the ends of the optic axons, all of the phosphoproteins were labeled more intensely in the optic tract than in themore »
- Authors:
-
- Cornell Univ. Medical College, New York, NY (USA)
- Publication Date:
- OSTI Identifier:
- 5894603
- Resource Type:
- Journal Article
- Journal Name:
- Neurochemical Research; (USA)
- Additional Journal Information:
- Journal Volume: 15:9; Journal ID: ISSN 0364-3190
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; NERVE CELLS; BIOLOGICAL REGENERATION; PHOSPHOPROTEINS; PHOSPHORYLATION; ANTINEOPLASTIC DRUGS; AUTORADIOGRAPHY; BIOLOGICAL LOCALIZATION; FISHES; PHOSPHATES; PHOSPHORUS 32; PROLINE; RETINA; TRITIUM COMPOUNDS; TWO-DIMENSIONAL ELECTROPHORESIS; AMINES; AMINO ACIDS; ANIMAL CELLS; ANIMALS; AQUATIC ORGANISMS; AZOLES; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; BIOLOGICAL RECOVERY; BODY; BODY AREAS; CARBOXYLIC ACIDS; CHEMICAL REACTIONS; DAYS LIVING RADIOISOTOPES; DRUGS; ELECTROPHORESIS; EYES; FACE; HEAD; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; HYDROGEN COMPOUNDS; ISOTOPES; LIGHT NUCLEI; NUCLEI; ODD-ODD NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANS; OXYGEN COMPOUNDS; PHOSPHORUS COMPOUNDS; PHOSPHORUS ISOTOPES; PROTEINS; PYRROLES; PYRROLIDINES; RADIOISOTOPES; RECOVERY; SENSE ORGANS; SOMATIC CELLS; VERTEBRATES; 550501* - Metabolism- Tracer Techniques
Citation Formats
Larrivee, D. Protein phosphorylation: Localization in regenerating optic axons. United States: N. p., 1990.
Web. doi:10.1007/BF00965906.
Larrivee, D. Protein phosphorylation: Localization in regenerating optic axons. United States. https://doi.org/10.1007/BF00965906
Larrivee, D. 1990.
"Protein phosphorylation: Localization in regenerating optic axons". United States. https://doi.org/10.1007/BF00965906.
@article{osti_5894603,
title = {Protein phosphorylation: Localization in regenerating optic axons},
author = {Larrivee, D},
abstractNote = {A number of axonal proteins display changes in phosphorylation during goldfish optic nerve regeneration. (1) To determine whether the phosphorylation of these proteins was closely linked to their synthesis in the retinal ganglion cell body, cycloheximide was injected intraocularly into goldfish whose optic nerves had been regenerating for 3 weeks. Cycloheximide reduced the incorporation of (3H)proline and 32P orthophosphate into total nerve protein by 84% and 46%, respectively. Of the 20 individual proteins examined, 17 contained less than 15% of the (3H)proline label measured in corresponding controls, whereas 18 proteins contained 50% or more of the 32P label, suggesting that phosphorylation was largely independent of synthesis. (2) To determine whether the proteins were phosphorylated in the ganglion cell axons, axonal transport of proteins was blocked by intraocular injection of vincristine. Vincristine reduced (3H)proline labeling of total protein by 88% and 32P labeling by 49%. Among the individual proteins (3H)proline labeling was reduced by 90% or more in 18 cases but 32P labeling was reduced only by 50% or less. (3) When 32P was injected into the cranial cavity near the ends of the optic axons, all of the phosphoproteins were labeled more intensely in the optic tract than in the optic nerve. These results suggest that most of the major phosphoproteins that undergo changes in phosphorylation in the course of regeneration are phosphorylated in the optic axons.},
doi = {10.1007/BF00965906},
url = {https://www.osti.gov/biblio/5894603},
journal = {Neurochemical Research; (USA)},
issn = {0364-3190},
number = ,
volume = 15:9,
place = {United States},
year = {Sat Sep 01 00:00:00 EDT 1990},
month = {Sat Sep 01 00:00:00 EDT 1990}
}