Tjelle T E, Brech A, Juvet L K, Griffiths G, Berg T
University of Oslo, Institute of Biology, Norway.
J Cell Sci. 1996 Dec;109 ( Pt 12):2905-14. doi: 10.1242/jcs.109.12.2905.
Although endosomal proteolysis has been reported (e.g. for peptide hormones and lysosomal enzymes), lysosomes are believed to be the main site of degradation in the endocytic pathway. We have studied the separate roles of lysosomes and prelysosomal endocytic organelles in the degradation of ovalbumin in J774 cells. The ovalbumin was labelled with 125I-tyramine cellobiose (125I-TC-ova). The labelled degradation products formed from this probe are trapped at the site of formation. To separate lysosomes efficiently from prelysosomal endocytic organelles we allowed the cells to endocytose a pulse of colloidal gold particles complexed with ovalbumin. By combining this density shift technique with subcellular fractionation of a postnuclear supernatant in Percoll gradients we could isolate three fractions that were sequentially involved in the endocytic pathway: a light Percoll fraction, a dense Percoll fraction and a gold fraction. The light Percoll fraction contained early endosomes since it was transferrin positive and received endocytic markers such as ovalbumin and horseradish peroxidase (HRP) early (< 5 minutes) after internalization. The dense Percoll fraction was transferrin negative, rab7 positive and received endocytic markers after 10-15 minutes of internalization. The gold-filled fraction was negative for both transferrin and rab7 but highly enriched in the lysosomal enzyme beta-hexosaminidase and was therefore defined as a lysosome. To study the role of endosomes and lysosomes in the degradation of endocytosed material we allowed the cells to take up (via the mannose receptor) 125I-TC-ova. It was found that the main degradation of 125I-TC-ova (measured as acid soluble radioactivity trapped in the organelle) took place in the late endosomes (and not in the lysosomes containing the bulk of the lysosomal enzymes). Our data therefore suggest that the late endosomes operate as an early lysosomal compartment. The terminal lysosomes may serve as storage bodies for acid hydrolases that may be called upon when needed (for instance during phagocytosis).
尽管已有报道称存在内体蛋白水解作用(如针对肽类激素和溶酶体酶),但溶酶体被认为是内吞途径中的主要降解场所。我们研究了溶酶体和前溶酶体内吞细胞器在J774细胞中卵清蛋白降解过程中的各自作用。用125I-酪胺纤维二糖(125I-TC-卵清蛋白)标记卵清蛋白。由该探针形成的标记降解产物被困在形成部位。为了有效地将溶酶体与前溶酶体内吞细胞器分离,我们让细胞内吞与卵清蛋白复合的胶体金颗粒脉冲。通过将这种密度转移技术与在Percoll梯度中对核后上清液进行亚细胞分级分离相结合,我们可以分离出依次参与内吞途径的三个组分:一个轻Percoll组分、一个重Percoll组分和一个金组分。轻Percoll组分含有早期内体,因为它转铁蛋白呈阳性,并且在内化后早期(<5分钟)接收内吞标记物,如卵清蛋白和辣根过氧化物酶(HRP)。重Percoll组分转铁蛋白呈阴性,rab7呈阳性,在内化10 - 15分钟后接收内吞标记物。充满金的组分转铁蛋白和rab7均呈阴性,但溶酶体酶β-己糖胺酶高度富集,因此被定义为溶酶体。为了研究内体和溶酶体在胞吞物质降解中的作用,我们让细胞(通过甘露糖受体)摄取125I-TC-卵清蛋白。发现125I-TC-卵清蛋白的主要降解(以细胞器中捕获的酸溶性放射性测量)发生在晚期内体中(而不是在含有大部分溶酶体酶的溶酶体中)。因此,我们的数据表明晚期内体作为早期溶酶体区室发挥作用。终末溶酶体可能作为酸性水解酶的储存体,在需要时(例如在吞噬过程中)可以被调用。