Punnonen E L, Autio S, Kaija H, Reunanen H
Department of Cell Biology, University of Jyväskylä, Finland.
Eur J Cell Biol. 1993 Jun;61(1):54-66.
We previously demonstrated both mannose 6-phosphate receptor (MPR) and cathepsin L in early autophagic vacuoles of cultured rat fibroblasts. This suggested that the enzyme may originate either from the receptor-enriched prelysosomal compartment (PLC) or from the trans-Golgi network (TGN). In the present ultrastructural study, we elucidated the roles of the PLC and TGN in lysosomal enzyme delivery to autophagic vacuoles. Firstly, we studied whether endocytic markers, cationized ferritin (CF), bovine serum albumin-gold or horseradish peroxidase (HRP), can be detected in autophagic vacuoles. Autophagy was induced by serum removal from the medium with or without leupeptin, an inhibitor of cysteine proteinases. Endocytic markers were not detected in autophagic vacuoles after short uptake which filled the early endosome, but only after longer labeling which filled the PLC. The markers were usually found in advanced autophagic vacuoles containing partially degraded cytoplasm and complex internal membranes which are the characteristic of the PLC. HRP-positive vesicles were also observed in continuity with early autophagic vacuoles containing intact cytoplasm. After uptake and transport of CF and HRP to the PLC, these markers were delivered to autophagic vacuoles even if microtubules were disrupted in vinblastine before the induction of autophagy. Secondly, we studied whether MPRs transport cathepsin L to autophagic vacuoles directly from the TGN. Two inhibitors of MPR-mediated enzyme transport, tunicamycin and chloroquine, were used. Quantitative immunocytochemistry showed that neither of these drugs prevented cathepsin L delivery to autophagic vacuoles. The results suggest that a large proportion of lysosomal enzymes is delivered to autophagic vacuoles from the PLC by a microtubule-independent manner. The first enzymes may be transported in small PLC-derived vesicles or tubules which are reached by HRP but not by CF and gold. Later, the autophaged cytoplasm is delivered to larger vacuolar parts of the PLC. Mannose 6-phosphate receptors transport no or only trace amounts of lysosomal enzymes to autophagic vacuoles directly from the TGN.
我们先前在培养的大鼠成纤维细胞的早期自噬泡中证实了甘露糖 6 - 磷酸受体(MPR)和组织蛋白酶L的存在。这表明该酶可能起源于富含受体的前溶酶体区室(PLC)或反式高尔基体网络(TGN)。在本超微结构研究中,我们阐明了PLC和TGN在溶酶体酶传递至自噬泡中的作用。首先,我们研究了内吞标记物,即阳离子铁蛋白(CF)、牛血清白蛋白 - 金或辣根过氧化物酶(HRP),是否能在自噬泡中被检测到。通过从培养基中去除血清,无论有无半胱氨酸蛋白酶抑制剂亮抑酶肽来诱导自噬。在短时间摄取使早期内体充满后,自噬泡中未检测到内吞标记物,但在长时间标记使PLC充满后才检测到。这些标记物通常存在于含有部分降解的细胞质和复杂内膜的晚期自噬泡中,这些是PLC的特征。还观察到HRP阳性囊泡与含有完整细胞质的早期自噬泡相连。在将CF和HRP摄取并转运至PLC后,即使在自噬诱导前用长春花碱破坏微管,这些标记物仍被传递至自噬泡。其次,我们研究了MPR是否直接从TGN将组织蛋白酶L转运至自噬泡。使用了两种MPR介导的酶转运抑制剂,衣霉素和氯喹。定量免疫细胞化学显示,这两种药物均未阻止组织蛋白酶L传递至自噬泡。结果表明,很大一部分溶酶体酶以不依赖微管的方式从PLC传递至自噬泡。首批酶可能通过源自PLC的小囊泡或小管进行转运,HRP可到达这些小囊泡或小管,但CF和金不能。后来,自噬的细胞质被传递至PLC中较大的液泡部分。甘露糖6 - 磷酸受体从TGN直接向自噬泡转运的溶酶体酶极少或仅为痕量。