Growth inhibition and apoptotic/necrotic phenotype was observed in nanogold particle (AuNP)-treated human chronic myelogenous leukemia cells. To elucidate the underlying cellular mechanisms, proteomic techniques including two-dimensional electrophoresis/mass spectrometry and protein microarrays were utilized to study the differentially expressed proteome and phosphoproteome, respectively. Systems biology analysis of the proteomic data revealed that unfolded protein-associated endoplasmic reticulum (ER) stress response was the predominant event. Concomitant with transcriptomic analysis using mRNA expression, microarrays show ER stress response in the AuNP-treated cells. The ER stress protein markers' expression assay unveiled AuNPs as an efficient cellular ER stress elicitor. Upon ER stress, cellular responses, including reactive oxygen species increase, mitochondrial cytochrome c release, and mitochondria damage, chronologically occurred in the AuNP-treated cells. Conclusively, this study demonstrates that AuNPs cause cell death through induction of unmanageable ER stress.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/nn2027775 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The role of canopy family proteins: biological mechanism and disease function.
Mol Biol Rep
January 2025
Department of Gastroenterology, Beijing Friendship Hospital, Capital Medical University, No. 95, Yong An Road, Xi Cheng District, Beijing, 100050, China.
Canopy family proteins are highly sequence-conserved proteins with an N-terminal hydrophobic signal sequence, a unique pattern of six cysteine residues characteristic of the saposin-like proteins, and a C-terminal putative endoplasmic reticulum retention signal sequence. At present, the known canopy family proteins are canopy fibroblast growth factor signaling regulator 1 (CNPY1), CNPY2, CNPY3, and CNPY4. Despite similar structures, canopy family proteins regulate complex signal networks to participate in various biological processes.
View Article and Find Full Text PDFSeipin Deficiency Impairs Motor Coordination in Mice by Compromising Spinal Cord Myelination.
Neuromolecular Med
January 2025
Department of Anatomy, School of Basic Medical Sciences, Shanxi Medical University, No 56, Xinjian Nan Road, Taiyuan, 030001, Shanxi, China.
The integrity of the myelin sheath of the spinal cord (SC) is essential for motor coordination. Seipin is an endoplasmic reticulum transmembrane protein highly expressed in adipose tissue and motor neurons in the SC. It was reported Seipin deficiency induced lipid dysregulation and neurobehavioral deficits, but the underlying mechanism, especially in SC, remains to be elucidated.
View Article and Find Full Text PDFThe construction of a breast cancer prognostic model by combining genes related to hypoxia and endoplasmic reticulum stress.
Comput Methods Biomech Biomed Engin
January 2025
Department of the Third General Surgery, Anyang Tumor Hospital, Anyang, Henan, China.
Breast cancer (BC) is a malignant tumor that occurs in breast tissue. This project aims to predict the prognosis of BC patients using genes related to hypoxia and endoplasmic reticulum stress (ERS). RNA-seq and clinical data for BC were downloaded from TCGA and GEO databases.
View Article and Find Full Text PDFCellular systems that govern protein folding rely on a delicate balance of functional redundancy and diversification to maintain protein homeostasis (proteostasis). Here, we use to demonstrate how both overlapping and divergent activities of two homologous endoplasmic reticulum (ER)-resident HSP70 family chaperones, HSP-3 and HSP-4, orchestrate ER proteostasis and contribute to organismal physiology. We identify tissue-, age-, and stress-specific protein expression patterns and find both redundant and distinct functions for HSP-3 and HSP-4 in ER stress resistance, reproduction, and body size regulation.
View Article and Find Full Text PDFGoverned by the unfolded protein response (UPR), the ability to counteract endoplasmic reticulum (ER) stress is critical for maintaining cellular homeostasis under adverse conditions. Unresolved ER stress leads to cell death through mechanisms that are yet not completely known. To identify key UPR effectors involved in unresolved ER stress, we performed an ethyl methanesulfonate (EMS) suppressor screen on the Arabidopsis mutant, which is impaired in activating cytoprotective UPR pathways.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!