Colocalization of neurotensin receptors and of the neurotensin-degrading enzyme endopeptidase 24-16 in primary cultures of neurons

Journal Article · Sat Dec 01 00:00:00 EST 1990 · Journal of Neuroscience; (USA)

OSTI ID:6250622

Chabry, J; Checler, F; Vincent, J P; Mazella, J ^[1]

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1. Institut de Pharmacologie Moleculaire et Cellulaire Centre National de la Recherche Scientifique, Valbonne (France)

This paper compares the localization of neurotensin receptors and of endopeptidase 24-16, a peptidase likely involved in the inactivation of neurotensin in primary cultures of neurons. Neurotensin binding sites were radiolabeled with {sup 125}I-Tyr3-neurotensin, whereas endopeptidase 24-16 was stained by immunohistochemical techniques using a monospecific polyclonal antibody. Endopeptidase 24-16 is present in 80-85% of the nondifferentiated neurons. The proportion of immunoreactive neurons decreased during maturation to reach 35-40% after 4-8 d of culture. By contrast, neurotensin receptors were not detectable in nondifferentiated cells and appear during maturation. Specific {sup 125}I-Tyr3-neurotensin labeling is maximal after 4 d of culture and is located on about 10% of differentiated neurons. Double-labeling experiments show that about 90% of cortical, hypothalamic, and mesencephalic neurons bearing the neurotensin receptor also contained endopeptidase 24-16, supporting the hypothesis that one of the functions of endopeptidase 24-16 is the physiological inactivation of neurotensin. However, the presence of endopeptidase 24-16 on numerous neurons that do not contain neurotensin receptors also suggests that the enzyme could be involved in the degradation and/or maturation of other neuropeptides.

• OSTI ID: 6250622
• Journal Information: Journal of Neuroscience; (USA), Vol. 10:12; ISSN 0270-6474
• Country of Publication: United States
• Language: English

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550201* - Biochemistry- Tracer Techniques