Expression of a glycosyl phosphatidylinositol-anchored adhesion molecule, the glycoprotein F3, in the adult rat hypothalamo-neurohypophysial system.
The F3 cell surface glycoprotein consists of six immunoglobulin-like domains, four fibronectin type III repeats and a glycosylphosphatidylinositol anchor and is found in membrane-bound and soluble form. Until now, it has been localized mainly on axons of subsets of developing and postnatal neurons and has been implicated in axonal growth and synaptogenesis. We here examined its expression in the adult rat hypothalamo-neurohypophysial system composed of magnocellular neurons whose axons can undergo remodelling in adulthood in response to lesion or physiological stimulation. Immunoblot analyses demonstrated high levels of F3 immunoreactivity in the hypothalamic nuclei containing the somata of the neurons, in the median eminence, through which pass their axons and in the neurohypophysis, where they terminate. The amount of F3 detected in the latter was 2-fold that in the hypothalamus. In addition, soluble forms predominated in the neurohypophysis and GPI-linked forms in the hypothalamus. Immunocytochemistry revealed a strong F3 immunoreactivity throughout the neurohypophysis and internal layer of the median eminence, characterized by a punctate labeling of fibers and dense filling of dilatations. In the hypothalamic nuclei, staining of variable intensity was visible in the cytoplasm of some magnocellular somata. In contrast, in colchicine-treated rats, all magnocellular somata throughout the hypothalamus displayed intense labeling while staining in the neurohypophysis was greatly reduced. Our observations reveal that neurons of the adult hypothalamo-neurohypophysial system express high level of F3, even under normal conditions. In view of its distribution and the differing proportions of membrane-bound and soluble forms, we propose that, after synthesis in the hypothalamus, F3 is targeted to the neurohypophysis where it accumulates in neurosecretory terminals or is released into the extracellular space. It remains to be seen whether its expression is linked to the secretion of the neurohypophysial peptides and in particular, to the ability of these neurons to undergo structural remodelling in adulthood.
Olive
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S
Laboratoire de Génétique et Physiologie du Développement, CNRS UMR 9943, Parc Scientifique de Luminy, Marseille, France.
Rougon
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G
Pierre
K
K
Theodosis
D T
DT
D000595:Amino Acid Sequence; D000818:Animals; D015816:Cell Adhesion Molecules, Neuronal / Q000096:biosynthesis*; D058966:Contactins; D005260:Female; D007030:Hypothalamo-Hypophyseal System / Q000033:anatomy & histology / Q000378:metabolism*; D007031:Hypothalamus / Q000033:anatomy & histology / Q000378:metabolism; D015151:Immunoblotting; D007150:Immunohistochemistry; D008297:Male; D008969:Molecular Sequence Data; D009473:Neuronal Plasticity / Q000502:physiology; D051381:Rats; D017208:Rats, Wistar
D015816:Cell Adhesion Molecules, Neuronal; D058966:Contactins