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P 2 Protein in Oligodendrocytes and Myelin of the Rabbit Central Nervous System
Author(s) -
Trapp Bruce D.,
Itoyama Yasuto,
MacIntosh Tracy D.,
Quarles Richard H.
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.tb12651.x
Subject(s) - myelin , antiserum , myelin basic protein , central nervous system , biology , immunocytochemistry , microbiology and biotechnology , anatomy , chemistry , endocrinology , immunology , antibody
P 2 protein, a myelin‐specific protein, was detected immunocyto‐chemically and biochemically in rabbit central nervous system (CNS) myelin. P 2 protein was synthesized by rabbit oligodendrocytes and was present in varying amounts throughout the rabbit CNS. Comparison of P 2 and myelin basic protein (MBP) stained sections revealed that P 2 antiserum did not stain all myelin sheaths within the rabbit CNS. The proportion of myelin sheaths stained by P 2 antiserum and the amount of P 2 detected biochemically were greater in more caudal regions of the rabbit CNS. The highest concentration of P 2 protein was found in rabbit spinal cord myelin, where P 2 antiserum stained the majority of myelin sheaths. P 2 protein was barely detectable biochemically in myelin isolated from frontal cortex, and in sections of frontal cortex only occasional myelin sheaths reacted with P 2 antiserum. These results suggest that the regional variations in the amount of P 2 protein are due to regional differences in the number of myelin sheaths that contain P 2 protein. P 2 protein was detected immunocytochemically and biochemically in rabbit sciatic nerve myelin. Immunocytochemically, P 2 antiserum only stained a portion of the myelin sheaths present. The myelin sheaths not reacting with P 2 antiserum had small diameters and represented less than 10% of the total myelinated fibers.