Asanuma N, Nomura H
Department of Oral Physiology, Matsumoto Dental College, Shiojiri, Japan.
Histochem J. 1993 May;25(5):348-56. doi: 10.1007/BF00159499.
Cyclic 3',5'-nucleotide phosphodiesterase activity was demonstrated cytochemically in the rat olfactory mucosa using cyclic AMP as substrate. Strong activity was observed on the plasma membrane of the cilia, dendritic knob and axon of olfactory cells; weak activity was apparent on the membrane of the dendritic shaft and cell body. This suggests that the cyclic AMP produced by odorant-sensitive adenylate cyclase in the dendritic terminal acts mainly in its original site and to a lesser extent in the dendritic shaft and cell body. The enzyme also hydrolysed cyclic GMP but the hydrolysis was not as great as in the case of cyclic AMP. Besides its presence in olfactory cells, enzymatic activity was also observed on the plasma membrane of basal cells and certain supporting cells with an astrocyte-like morphology.
利用环磷酸腺苷(cAMP)作为底物,通过细胞化学方法在大鼠嗅黏膜中证实了环3',5'-核苷酸磷酸二酯酶的活性。在嗅细胞的纤毛、树突棘和轴突的质膜上观察到强活性;在树突干和细胞体的膜上则有较弱的活性。这表明由树突末端对气味敏感的腺苷酸环化酶产生的环磷酸腺苷主要在其产生的原位起作用,而在树突干和细胞体中的作用较小。该酶也能水解环磷酸鸟苷(cGMP),但水解程度不如环磷酸腺苷。除了在嗅细胞中存在外,在基底细胞和某些具有星形胶质细胞样形态的支持细胞的质膜上也观察到了酶活性。