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硫胺素焦磷酸酶和酸性磷酸酶活性在小鼠胰腺腺泡细胞中的精细结构定位

Fine structural localization of thiamine pyrophosphatase and acid phosphatase activities in the mouse pancreatic acinar cell.

作者信息

Fujita H, Okamoto H

出版信息

Histochemistry. 1979;64(3):287-95. doi: 10.1007/BF00495029.

DOI:10.1007/BF00495029
PMID:521317
Abstract

The fine structural localization of thiamine pyrophosphatase (TPPase) and acid phosphatase (AcPase) was examined in pancreatic acinar cells of fasting and fed mice. The results were not affected by these conditions. TPPase activity was positive in two and sometimes three cisternae of the inner Golgi lamellae as well as in the condensing vacuoles of the trans area, but negative in the rigid lamellae and small vesicles of the trans area. AcPase activity was demonstrated in two and sometimes three cisternae of inner Golgi lamellae, condensing vacuoles, rigid lamellae, lysosomes and smooth or coated vesicles in the trans area. The inner Golgi lamellae and the condensing vacuoles were positive for both enzyme activities. From these facts, the lysosome is considered to be formed not only in the GERL system but also through the rough endoplasmic reticulum-Golgi apparatus route. It is reasonable to consider that Novikoff's GERL is not independent from the Golgi apparatus but represents a part of this organelle.

摘要

对禁食和喂食小鼠的胰腺腺泡细胞中硫胺素焦磷酸酶(TPPase)和酸性磷酸酶(AcPase)进行了精细结构定位研究。这些条件对结果没有影响。TPPase活性在内侧高尔基体片层的两个,有时是三个潴泡以及反面区域的浓缩泡中呈阳性,但在反面区域的致密片层和小泡中呈阴性。AcPase活性在内侧高尔基体片层的两个,有时是三个潴泡、浓缩泡、致密片层、溶酶体以及反面区域的光滑或有被小泡中被证实。内侧高尔基体片层和浓缩泡对两种酶活性均呈阳性。基于这些事实,认为溶酶体不仅在GERL系统中形成,也通过粗面内质网-高尔基体途径形成。有理由认为诺维科夫的GERL并非独立于高尔基体,而是该细胞器的一部分。

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