实验鼠和人鼻腔中氨基肽酶M、氨基肽酶A和γ -谷氨酰转移酶的组织化学研究。

I Kubisová, B Pospísilová
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引用次数: 0

摘要

在光镜下研究了实验室啮齿动物(大鼠、小鼠、豚鼠)和人胎鼻腔器官中氨基肽酶M (APM)、氨基肽酶A (APA)和γ -谷氨酰转移酶(GGT)活性的定位。利用偶氮偶联方法在氯仿丙酮预处理的低温冷冻切片中证实了所有这些酶的组织化学特性(5,9)。这些膜结合的氨基肽酶可能参与鼻腔内肽的代谢。它们具有调节上皮细胞生长和分化的特殊作用。结果显示嗅觉上皮和呼吸上皮之间的酶模式存在差异。GGT似乎只存在于呼吸上皮和鲍曼腺导管中。APM和APA的活性主要存在于粘附于上皮和腺体基底膜的纤维细胞中。
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Histochemical study of aminopeptidase M, aminopeptidase A, and gamma-glutamyltransferase in the nasal cavity of laboratory rodents andman.

The localization of aminopeptidase M (APM), aminopeptidase A (APA) and gama-glutamyltransferase (GGT) activity was studied at light microscope level in the nasal cavity organs of the laboratory rodents (rat, mouse, guinea pig) and human foetuses. All the enzymes were demonstrated histochemically in chloroform-acetone pretreated cryostat sections with application of azocoupling methods (5, 9). These membrane-bound aminopeptidases may participate in the metabolism of peptides in the nasal cavity. They have specific roles as modulators of growth and differentiation of the epithelial cells. The results revealed differences in enzyme patterns between olfactory and respiratory epithelium. GGT seemed to be present only in respiratory epithelium and in the ducts of Bowman's glands. Activity of APM and APA was found mostly in the fibrocytes which adhered to the basal membrane of the epithelium and glands.

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