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敲低热休克蛋白家族 D 成员 1（HSPD1）通过破坏线粒体 3-氧酰基辅酶 A 合酶（OXSM）的稳定性促进卵巢癌细胞的增殖和迁移。

Knockdown of heat shock protein family D member 1 (HSPD1) promotes proliferation and migration of ovarian cancer cells via disrupting the stability of mitochondrial 3-oxoacyl-ACP synthase (OXSM).

机构信息

Division of Uterine Vascular Biology, Guangdong Provincial Clinical Research Center for Child Health, Guangzhou Institute of Pediatrics, Guangzhou Women and Children's Medical Center, Guangzhou Medical University, 510623, Guangzhou, China.

School of Medicine, South China University of Technology, Guangzhou, China.

出版信息

J Ovarian Res. 2023 Apr 22;16(1):81. doi: 10.1186/s13048-023-01156-8.

DOI:10.1186/s13048-023-01156-8
PMID:37087461
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10122320/
Abstract

BACKGROUND

Heat shock protein 60 (HSP60) is essential for the folding and assembly of newly imported proteins to the mitochondria. HSP60 is overexpressed in most types of cancer, but its association with ovarian cancer is still in dispute. SKOV3 and OVCAR3 were used as experimental models after comparing the expression level of mitochondrial HSP60 in a normal human ovarian epithelial cell line and four ovarian cancer cell lines.

RESULTS

Low HSPD1 (Heat Shock Protein Family D (HSP60) Member 1) expression was associated with unfavorable prognosis in ovarian cancer patients. Knockdown of HSPD1 significantly promoted the proliferation and migration of ovarian cancer cells. The differentially expressed proteins after HSPD1 knockdown were enriched in the lipoic acid (LA) biosynthesis and metabolism pathway, in which mitochondrial 3-oxoacyl-ACP synthase (OXSM) was the most downregulated protein and responsible for lipoic acid synthesis. HSP60 interacted with OXSM and overexpression of OXSM or LA treatment could reverse proliferation promotion mediated by HSPD1 knockdown.

CONCLUSIONS

HSP60 interacted with OXSM and maintained its stability. Knockdown of HSPD1 could promote the proliferation and migration of SKOV3 and OVCAR3 via lowering the protein level of OXSM and LA synthesis.

摘要

背景

热休克蛋白 60（HSP60）对于新导入的蛋白质在到线粒体中的折叠和组装是必需的。HSP60 在大多数类型的癌症中过度表达，但它与卵巢癌的关联仍有争议。在比较正常人类卵巢上皮细胞系和四种卵巢癌细胞系中线粒体 HSP60 的表达水平后，SKOV3 和 OVCAR3 被用作实验模型。

结果

低 HSPD1（热休克蛋白家族 D（HSP60）成员 1）表达与卵巢癌患者的不良预后相关。HSPD1 的敲低显著促进了卵巢癌细胞的增殖和迁移。HSPD1 敲低后差异表达的蛋白质富集在硫辛酸（LA）生物合成和代谢途径中，其中线粒体 3-氧酰基-ACP 合酶（OXSM）是下调最明显的蛋白质，负责 LA 合成。HSP60 与 OXSM 相互作用，过表达 OXSM 或 LA 处理可以逆转 HSPD1 敲低介导的增殖促进作用。

结论

HSP60 与 OXSM 相互作用并维持其稳定性。HSPD1 的敲低可通过降低 OXSM 和 LA 合成的蛋白水平促进 SKOV3 和 OVCAR3 的增殖和迁移。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/a09f8eff0c3b/13048_2023_1156_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/44820e9ba7f3/13048_2023_1156_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/9bb3317ba3bb/13048_2023_1156_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/83543b82ef79/13048_2023_1156_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/153d3e858826/13048_2023_1156_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/d5e65bc79bb4/13048_2023_1156_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/a09f8eff0c3b/13048_2023_1156_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/44820e9ba7f3/13048_2023_1156_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/9bb3317ba3bb/13048_2023_1156_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/83543b82ef79/13048_2023_1156_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/153d3e858826/13048_2023_1156_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/d5e65bc79bb4/13048_2023_1156_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/37a7/10122320/a09f8eff0c3b/13048_2023_1156_Fig6_HTML.jpg

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