PSA-NCAM and B-50/GAP-43 are coexpressed by specific neuronal systems of the adult rat mediobasal hypothalamus that exhibit remarkable capacities for morphological plasticity.
The present study was designed to determine whether the mediobasal hypothalamus of adult rats contains neurons that continue to coexpress the highly polysialylated neural cell adhesion molecule (PSA-NCAM) and B-50/GAP-43, two proteins coexpressed by virtually all of the neurons of the fetal and neonatal rat central nervous system. Confocal laser scanning microscopy combined with double- or triple-fluorescence immunostaining was used to identify the hypothalamic neurons that express high levels of both PSA-NCAM and B-50/GAP-43 and to study the possible modifications of their morphological organization following a surgical lesion through the mediobasal hypothalamus. In intact animals, PSA-NCAM and B-50/GAP-43 were found to be colocalized within numerous fibers projecting throughout the external layer of the median eminence that were immunoreactive for either gamma-aminobutyric acid (GABA) or tyrosine hydroxylase (TH). Three to 30 days after a lesion through this region, numerous regenerating axonal sprouts, triple-immunostained for PSA-NCAM, B-50/GAP-43, and either GABA or TH, were detected along the ventricular surface of, and throughout the perivascular layer of, the median eminence. Surprisingly, high levels of PSA-NCAM and B-50/GAP-43 were also associated with numerous supraependymal neurons that exhibited long ramified processes and were immunoreactive for GABA but TH-negative. The use of the proliferation marker, 3H-thymidine, further indicated that the emergence of such supraependymal neurons after median eminence lesion was not related to the proliferation of preexisting quiescent cells. These data indicate that the mediobasal hypothalamus of the adult rat contains two neuronal systems, in which the continued coexpression of PSA-NCAM and B-50/GAP-43 is related to remarkable capacities for postlesional, morphological plasticity.
Alonso
G
G
INSERM U 336, University of Montpellier II, France.
Prieto
M
M
Legrand
A
A
Chauvet
N
N
D000818:Animals; D019922:GAP-43 Protein; D007033:Hypothalamus, Middle / Q000166:cytology / Q000378:metabolism* / Q000648:ultrastructure; D007150:Immunohistochemistry; D008297:Male; D008562:Membrane Glycoproteins / Q000096:biosynthesis*; D018613:Microscopy, Confocal; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence; D009416:Nerve Regeneration; D009419:Nerve Tissue Proteins / Q000096:biosynthesis*; D039842:Neural Cell Adhesion Molecule L1; D019006:Neural Cell Adhesion Molecules / Q000096:biosynthesis*; D016900:Neurofilament Proteins / Q000096:biosynthesis; D009473:Neuronal Plasticity / Q000502:physiology*; D009474:Neurons / Q000378:metabolism* / Q000648:ultrastructure; D051381:Rats; D017207:Rats, Sprague-Dawley; D012794:Sialic Acids / Q000096:biosynthesis*; D013936:Thymidine / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism; D005680:gamma-Aminobutyric Acid / Q000378:metabolism
D019922:GAP-43 Protein; D008562:Membrane Glycoproteins; D009419:Nerve Tissue Proteins; D039842:Neural Cell Adhesion Molecule L1; D019006:Neural Cell Adhesion Molecules; D016900:Neurofilament Proteins; D012794:Sialic Acids; C103469:polysialyl neural cell adhesion molecule; D005680:gamma-Aminobutyric Acid; D014446:Tyrosine 3-Monooxygenase; D013936:Thymidine