Evidence that 5'-nucleotidase is associated with malleable synapses--an enzyme cytochemical investigation of the olfactory bulb of adult rats.
The adenosine-producing ecto-enzyme 5'-nucleotidase has recently been assigned to malleable axon terminals in both the developing and regenerating adult nervous system, but is otherwise only glia-bound. Using a cytochemical lead method, we now show that 5'-nucleotidase activity is localized predominantly at glomerular and mitral synapses within the main olfactory bulb of normal, adult rats. As these terminals are prone to synaptic turnover even at maturity, the present findings favour the view that this enzyme constitutes a marker molecule for plastic synapses. It is suggested that functions of 5'-nucleotidase in purinergic neuromodulation and cell adhesion are unique to the olfactory bulb, and implied in synaptic arrangements and information processing.
Schoen
S W
SW
Department of Neurology, Aachen University Medical School, Germany.
Kreutzberg
G W
GW
D000818:Animals; D001369:Axons; D002448:Cell Adhesion; D006651:Histocytochemistry; D009457:Neuroglia; D009708:Nucleotidases / Q000502:physiology*; D009830:Olfactory Bulb / Q000502:physiology*; D017729:Presynaptic Terminals; D011687:Purines; D051381:Rats; D017208:Rats, Wistar; D013569:Synapses / Q000502:physiology*
D011687:Purines; D009708:Nucleotidases