Myosin I is associated with zymogen granule membranes in the rat pancreatic acinar cell.
Myosin I is associated with zymogen granule membranes in the rat pancreatic acinar cell.
复制标题
肌球蛋白 I 与大鼠胰腺腺泡细胞中的酶原颗粒膜相关。
DOI：
10.1053/gast.1997.v113.pm9247487
复制
发表时间：
1997
期刊：
影响因子：
29.4
通讯作者：
Pandol,SJ
中科院分区：
文献类型：
--
作者：
Poucell-Hatton,S;Perkins,PS;Deerinck,TJ;Ellisman,MH;Hardison,WG;Pandol,SJ
背景和目的细胞内不同肌球蛋白 I 及其亚型的机制。一种独特的信使介导两种最广泛研究的酶原颗粒转运特征和胰腺腺泡细胞中的胞吐作用不是肌球蛋白I，而是它们与磷脂mem结合的能力。电子显微镜显示了管腔周围的膜。 A.castellanii 肌球蛋白 IA 和 IB 直接与腺泡细胞中的肌动蛋白网络结合，表明从该种肌动蛋白和肌球蛋白中分离出的 NaOH 提取膜在运输过程中发挥作用。可能以及含有磷酸盐的磷脂囊泡参与分泌型丝氨酸或磷脂酰肌醇4, 5-二磷酸中的两种类型的肌球蛋白。研究了8-11过程，并确定了它们在aci中的分布。尾部与膜的结合可能允许这种nar细胞被确定。方法抗体特异性运动分子在细胞器运动中发挥作用，吞噬肌球蛋白I或肌球蛋白II用于免疫细胞分裂和细胞运动。 10, 12 来自 A. 化学和蛋白质印迹分析的肌球蛋白 I。还进行了超微结构castellanii 具有不依赖于ATP 的肌动蛋白结合位点的研究。结果尾部的Western blot 以及ATP 敏感的肌动蛋白丝分析表明，肌球蛋白I 和肌球蛋白II 存在于全胰腺匀浆中，但仅存在于头部的肌结合位点。尾部结合位点可能位于分离的酶原颗粒上，并且对于锚定至肌动蛋白丝很重要。它们的膜的尾巴。通过免疫细胞化学，肌球蛋白 I 被认为含有腺泡细胞共局部膜亚结构域顶端的靶向信号，并确定糖蛋白 2 的类型，糖蛋白 2 是酶原转运所需的标记物。一些肌球蛋白我已定位为ules和肌动蛋白。通过免疫细胞化学，肌球蛋白 I 定位于细胞内的特定膜结构。 1、5、13-16 也位于分离的酶原颗粒上。结论-几种棘阿米巴肌球蛋白 I 亚型已被研究：通过免疫定位鉴定肌球蛋白 I 对酶原的免疫定位，并显示出独特的细胞颗粒膜及其与每质模式的密切关联。 17 肌球蛋白 IA 几乎完全出现在腔肌动蛋白中，表明肌球蛋白 I 在细胞质、吞噬杯下方的皮层、酶原的运输和胞吐过程以及与小细胞质囊泡相关的过程中发挥直接作用。胰腺腺泡细胞中的肌颗粒。 sin IB 是与质膜、大液泡膜和吞噬细胞相关的主要亚型
Background & AimsThe mechanisms whereby intracel- different myosins I and their isoforms. One distinguish-lular messengers mediate zymogen granule transport ing characteristic of two of the most extensively studied and exocytosis in the pancreatic acinar cell are not well myosins I is their ability to attach to phospholipid mem-defined. Electron microscopy has shown a periluminal branes. A. castellanii myosins IA and IB bind directly to network of actin in the acinar cell, suggesting a role for NaOH-extracted membranes isolated from this species actin and myosin in the transport process. The possible as well as to phospholipid vesicles containing phosphati-involvement of two types of myosin in the secretory dylserine or phosphatidylinositol 4, 5-biphosphate. 8–11 process was investigated, and their distribution in aci-The binding of the tail to membranes may allow this nar cells was determined.MethodsAntibodies specific motor molecule to act in organellar movement, phagocy-to myosin I or to myosin II were used for immunocyto-tosis, and cell movement. 10, 12 The myosins I from A. chemistry and Western blot analysis. Ultrastructural castellanii have an ATP-independent actin-binding site studies were also performed.ResultsWestern blot in the tail as well as the ATP-sensitive actin filament analysis showed that myosin I and myosin II were present in total pancreatic homogenate but that only myo- binding site in the head. The tail-binding site may be sin I was present on isolated zymogen granules and important for anchoring to actin filaments. The tails of their membranes. By immunocytochemistry, myosin I myosins are thought to contain targeting signals for was shown in the apical aspect of acinar cells colocal- membrane subdomains and to determine the type of ized with glycoprotein 2, a marker for zymogen gran- transport required. Some myosins I have been localized ules, and actin. By immunocytochemistry, myosin I was to specific membranous structures within cells. 1, 5, 13–16 also localized on isolated zymogen granules. Conclu-Several Acanthamoeba myosin I isoforms have been sions: The immunolocalization of myosin I to zymogen identified by immunolocalization and show unique cyto-granule membranes and its close association with per-plasmic patterns. 17 Myosin IA occurs almost exclusively iluminal actin suggest that myosin I plays a direct role in the cytoplasm, in the cortex beneath phagocytic cups, in the process of transport and exocytosis of zymogen and in association with small cytoplasmic vesicles. Myo-granules in the pancreatic acinar cell. sin IB is the main isoform associated with the plasma membrane, large vacuole membranes, and phagocytic