Unstimulated amylase secretion is proteoglycan-dependent in rat parotid acinar cells
Unstimulated amylase secretion is proteoglycan-dependent in rat parotid acinar cells
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DOI：
10.1016/j.abb.2007.10.008
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发表时间：
2008-01-15
影响因子：
3.9
通讯作者：
Kumakura, Masahiko
中科院分区：
文献类型：
--
作者：
Nashida, Tomoko;Imai, Akane;Kumakura, Masahiko
众所周知，淀粉酶是响应于来自腺泡细胞的细胞外刺激而分泌的。然而，淀粉酶也在没有刺激的情况下分泌。用短时间脉冲法和S-35-氨基酸追踪法将泡状淀粉酶作为一种新合成的淀粉酶与分泌颗粒中积累的淀粉酶区分开来。在大鼠腮腺腺泡细胞中，新合成的淀粉酶在没有分泌囊泡刺激的情况下分泌。分泌过程不包括微管，但与微丝有关。对硝基苯基β-木糖苷，一种蛋白多糖合成的抑制剂，抑制新合成的淀粉酶的分泌。这表明新合成的淀粉酶是从分泌囊泡分泌的，而不是通过组成型分泌途径（包括不成熟的分泌颗粒）分泌的，并且分泌囊泡的形成需要蛋白聚糖合成。(C)2007年爱思唯尔公司All rights reserved.
It is well-known that amylase is secreted in response to extracellular stimulation from the acinar cells. However, amylase is also secreted without stimulation. We distinguished vesicular amylase as a newly synthesized amylase from the accumulated amylase in secretory granules by short time pulse and chased with S-35-amino acid. The newly synthesized amylase was secreted without stimulation from secretory vesicles in rat parotid acinar cells. The secretion process did not include microtubules, but was related to microfilaments. p-Nitrophenyl beta-xyloside, an inhibitor of proteoglycan synthesis, inhibited the newly synthesized amylase secretion. This indicated that the newly synthesized amylase was secreted from secretory vesicles, not via the constitutive-like secretory route, which includes the immature secretory granules, and that proteoglycan synthesis was required for secretory vesicle formation. (C) 2007 Elsevier Inc. All rights reserved.