Ir. Griffiths et al., EXPRESSION OF THE PROTEOLIPID PROTEIN GENE IN GLIAL-CELLS OF THE POSTNATAL PERIPHERAL NERVOUS-SYSTEM OF RODENTS, Neuropathology and applied neurobiology, 21(2), 1995, pp. 97-110
The proteolipid protein (PLP) gene encodes for two proteins, PLP and D
M-20, which are produced by alternative splicing of exon 3B. PLP is th
e major CNS myelin protein and is postulated to play a structural role
at the intraperiod line. Its developmental expression mirrors that of
CNS myelination. DM-20 predominates in the embryo and prior to myelin
ation of the CNS and may be involved in glial cell development. The PL
P gene is expressed in the PNS in which DM-20 is the predominant isofo
rm at all ages, In this study we describe the localization of the two
isoforms in the post-natal rodent PNS using immunostaining and reverse
transcriptase PCR. DM-20 is present in relatively high abundance in n
on-myelin-forming Schwann cells and within cytoplasmic regions of myel
inated internodes, particularly the paranodes and Schmidt-Lanterman in
cisures and also the outer Schwann cytoplasm and perinuclear cytoplasm
. DM-20 is also located in the perineuronal satellite cells of spinal,
cranial and autonomic ganglia and in the ensheathing cells of the olf
actory nerve layer of the olfactory bulb. PLP was detected by immunocy
tochemistry in the perinuclear region of myelinated internodes; PCR an
alysis indicated small amounts of PLP mRNA in the other locations but
protein was not detected by immunostaining. Neither protein was identi
fied in compact myelin of the PNS. DM-20 is the predominant product of
the PLP gene expressed in a wide variety of peripheral glia. Its pres
ence is not correlated to a myelin-forming state. Other studies have d
emonstrated early embryonic expression of the PLP gene throughout the
PNS and all these features support the hypothesis that any putative ro
le for DM-20 is unrelated to myelination but may involve glial cell de
velopment.