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通过酸性磷酸酶、硫胺素焦磷酸酶和ATP二磷酸水解酶活性的超微结构细胞化学研究胰腺腺泡细胞酶原颗粒膜的起源。

The origin of the zymogen granule membrane of the pancreatic acinar cell as examined by ultrastructural cytochemistry of acid phosphatase, thiamine pyrophosphatase, and ATP-diphosphohydrolase activities.

作者信息

Beaudoin A R, Grondin G, Lord A, Roberge M, St-Jean P

出版信息

Eur J Cell Biol. 1983 Jan;29(2):218-25.

PMID:6131821
Abstract

Cytochemical distributions of acid phosphatase, thiamine pyrophosphatase, and ATP-diphosphohydrolase activities have been examined on thin sections of rat pancreas and on isolated zymogen-granule membranes. Acid phosphatase was found in the rigid lamellae separated from the Golgi stacked cisternae, in condensing vacuoles, and in the trans-saccules of Golgi apparatus; it was not detected in purified zymogen-granule membranes. Thiamine pyrophosphatase was detected in trans-saccules of the Golgi apparatus, in purified zymogen-granule membranes, and in the plasmalemma of the acinar cell. It was absent in condensing vacuoles. The ATP-diphosphohydrolase activity has a distribution similar to thiamine pyrophosphatase. These observations illustrate the similarity between the trans-saccules of the Golgi apparatus and the membrane of mature zymogen granules and the disparity between the latter membrane and the membrane of the condensing vacuole. They suggest that the condensing vacuole might not be the immediate precursor of the zymogen granule as commonly assumed. An alternative possibility would be that condensing vacuoles would fuse with the trans-saccule (transition) of the Golgi apparatus which in turn would form mature zymogen granules.

摘要

已对大鼠胰腺薄片和分离的酶原颗粒膜进行了酸性磷酸酶、硫胺素焦磷酸酶和ATP二磷酸水解酶活性的细胞化学分布研究。在从高尔基体堆叠池分离出的刚性薄片、浓缩泡和高尔基体的反式扁平囊泡中发现了酸性磷酸酶;在纯化的酶原颗粒膜中未检测到。硫胺素焦磷酸酶在高尔基体的反式扁平囊泡、纯化的酶原颗粒膜和腺泡细胞的质膜中被检测到。在浓缩泡中不存在。ATP二磷酸水解酶活性的分布与硫胺素焦磷酸酶相似。这些观察结果说明了高尔基体反式扁平囊泡与成熟酶原颗粒膜之间的相似性,以及后一种膜与浓缩泡膜之间的差异。它们表明,浓缩泡可能不像通常所认为的那样是酶原颗粒的直接前体。另一种可能性是,浓缩泡会与高尔基体的反式扁平囊泡(过渡区)融合,而反式扁平囊泡反过来会形成成熟的酶原颗粒。

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1
The origin of the zymogen granule membrane of the pancreatic acinar cell as examined by ultrastructural cytochemistry of acid phosphatase, thiamine pyrophosphatase, and ATP-diphosphohydrolase activities.通过酸性磷酸酶、硫胺素焦磷酸酶和ATP二磷酸水解酶活性的超微结构细胞化学研究胰腺腺泡细胞酶原颗粒膜的起源。
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引用本文的文献

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Characterization and localization of an ATP diphosphohydrolase activity (EC 3.6.1.5) in sarcolemmal membrane from rat heart.大鼠心肌肌膜中ATP二磷酸水解酶活性(EC 3.6.1.5)的鉴定与定位
Mol Cell Biochem. 1997 May;170(1-2):115-23. doi: 10.1023/a:1006848701467.
2
Purification of pancreas type-I ATP diphosphohydrolase and identification by affinity labelling with the 5'-p-fluorosulphonylbenzoyladenosine ATP analogue.胰腺I型ATP二磷酸水解酶的纯化及其用5'-对氟磺酰苯甲酰腺苷ATP类似物进行亲和标记的鉴定
Biochem J. 1995 Dec 1;312 ( Pt 2)(Pt 2):351-6. doi: 10.1042/bj3120351.
3
The protein content and morphogenesis of zymogen granules.
酶原颗粒的蛋白质含量与形态发生
Cell Tissue Res. 1995 Jun;280(3):519-30. doi: 10.1007/BF00318356.
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Cytochemical localization of beta-NADPase and TMPase in B cells of pancreas.胰腺B细胞中β-烟酰胺腺嘌呤二核苷酸磷酸酶和三磷酸腺苷酶的细胞化学定位
Int J Pancreatol. 1989 Mar;4(2):199-205. doi: 10.1007/BF02931321.