Unstimulated amylase secretion is proteoglycan-dependent in rat parotid acinar cells

被引:6
|
作者
Nashida, Tomoko [1 ]
Imai, Akane [1 ]
Shimomura, Hiromi [1 ]
Yoshie, Sumio [2 ]
Yokosuka, Hiroyuki [2 ]
Kumakura, Masahiko [2 ]
机构
[1] Nippon Dental Univ, Sch Life Dent Niigata, Dept Biochem, Niigata 9518580, Japan
[2] Nippon Dental Univ, Sch Life Dent Niigata, Dept Histol, Niigata 9518580, Japan
关键词
amylase; unstimulated secretion; rat parotid; acinar cells; secretory vesicles; p-nitrophenyl beta-xyloside;
D O I
10.1016/j.abb.2007.10.008
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:165 / 173
页数:9
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