Understanding the Interaction of Nanoparticles at the Cellular Interface
D. Sakthi Kumar, Aswathy Ravindran Girija in Bionanotechnology in Cancer, 2023
The Golgi apparatus is a vital organelle as it plays a crucial role in protein processing. The organelle functions as an integral unit in a cell because of its shape. Any anomaly in the condition of the Golgi apparatus is known to cause abnormalities in the cell. Once inside the cell, NPs interact with various cell organelles, one of which is the Golgi apparatus. Ma et al. have conducted a study to identify the effects of gold NPs on the Golgi apparatus [54]. Interestingly, gold NPs (50 nm) in normal rat kidney epithelial cells (NRK Line) have disrupted the calcium level inside the cell leading to the endoplasmic reticulum (ER) stress. The calcium ion concentration in cell organelles plays a crucial role in maintaining organelle function and structure. Similarly, the Golgi apparatus’s configuration changed from the familiar ribbon-like design into mini stacks, which were not linked or aligned. To study the Golgi apparatus’s functioning, mannosidase II and Galactosyltransferase were selected, and cells treated with gold NPs showed a significant decrease in their production. Cluster analysis of genes expressed in control and section treated with gold NPs showed substantial expression patterns. There is a change in the regulation of integrin-mediated cellular adhesion, which plays a crucial role in cell-extracellular matrix adhesion.
Structural Organization of the Liver
Robert G. Meeks, Steadman D. Harrison, Richard J. Bull in Hepatotoxicology, 2020
The discovery of the Golgi complex (apparatus) by Camillo Golgi, for whom it is named, took place in 1898. However, the controversy regarding whether the Golgi complex was a bona fide cell structure or an artifact continued until the mid-1950s. It stemmed from the question of whether one believed that the metallic impregnation methods (involving use of silver or OsO4) which Golgi and others used were staining a common structure with variable form and distribution in different cell types, or alternatively, that their methods produced artifactual deposition of heavy metals. With the introduction of electron microscopy in the early 1950s, those who believed in the existence of the Golgi complex began to outnumber those who did not, and by the early 1960s even the most skeptical accepted the concept (Farquhar and Palade, 1981).
Cells
Frank J. Dye in Human Life Before Birth, 2019
A human cell may contain one or more Golgi bodies (see Figure 2.2). The general functions of Golgi bodies are to chemically modify glycoproteins (chemical complexes of carbohydrate and protein) produced by the cell, act as a “traffic director” for macromolecules produced by the cell, and package cell products (e.g., enzymes) to be secreted from the cell. In addition, Golgi bodies play a role in the formation of organelles called lysosomes, which we will consider in the next section. In the formation of spermatozoa and eggs, Golgi bodies have the specialized functions of producing acrosomes (organelles found in sperm) and cortical granules (organelles found in eggs), respectively. These two highly specialized organelles, which are peculiar to gametes (sex cells), play important roles in fertilization.
Expression of endoplasmic reticulum stress mRNAs in otitis media
Published in Acta Oto-Laryngologica, 2021
Su Young Jung, Ki Jin Kwon, Hye Kyu Min, Dae Woong Kang, Dong Choon Park, Young Il Kim, Jeewon Ryu, Seung Geun Yeo
The endoplasmic reticulum (ER) is an important intracellular site for protein synthesis, folding, and secretion, with these proteins transported to the Golgi apparatus or cell membrane [1]. Collapse of homeostasis within the ER, because of pathophysiological factors or a sudden influx of proteins exceeding the folding ability of the ER, affects protein folding. This can result in an increase of misfolded or unfolded proteins, which subsequently impair ER function. This state is called ER stress [2]. Proteins should be folded and modified in proper order, yielding proteins with proper conformations. Unfolded or misfolded proteins cannot be transported to the Golgi apparatus and accumulate in the ER, interfering with the proper functioning of the ER and imperiling cell survival. Causes of ER stress can include an excessive increase of protein synthesis, disruption of protein maturation, reduced function of chaperone molecules, overexpression of disease-related abnormal proteins, reduced calcium concentration within the ER, oxidative stress, and virus infection [1–3].
In vitro effects of combustion generated carbon dots on cellular parameters in healthy and cancerous breast cells
Published in Nanotoxicology, 2022
Nikita Dinger, Valeria Panzetta, Carmela Russo, Paolo Antonio Netti, Mariano Sirignano
Similar to our studies, lysosomes entrapments of various CDs have been observed (Guo et al. 2020; H. Liu et al. 2021; Q. Liu et al. 2020; Tong et al. 2020). CDs tend to accumulate in subcellular organelles with lysosomes being one possible site and because of this they have been widely used as fluorescent probes for imaging intracellular organelles (Gao et al. 2017; Shen et al. 2020; Y. Zhang et al. 2015). Similarly, CdSe/ZnS quantum dot exposures have shown to affect other subcellular functions like the endoplasmic reticulum (ER) and Golgi apparatus(Y.-Y. Liu et al. 2021). The ER is responsible for protein synthesis, folding, modification, transport, and degradation while the Golgi apparatus is responsible for processing and packaging of secreted materials. Carbon nanodots have also been repurposed for such targeted signaling to be used in nanomedicine thereby allowing it to affect cell signaling to a great extent. In particular, this effect has been seen in cancer cells for varying concentrations of CDs (Y. Liu et al. 2021; Figures 6 and 7).
Pharmacoperone drugs: targeting misfolded proteins causing lysosomal storage-, ion channels-, and G protein-coupled receptors-associated conformational disorders
Published in Expert Review of Clinical Pharmacology, 2018
Zhi-Shuai Hou, Alfredo Ulloa-Aguirre, Ya-Xiong Tao
Proteins are required to pass the inspection of the stringent ER QCS in order to be incorporated into transport vesicles for delivery to the Golgi and thereafter to their site of function [8,30]. Nevertheless, some misfolded proteins bearing particular ER retention signals or when ERAD is saturated can escape the ER QCS and translocate to the Golgi [49], whereas others may misfold during trafficking. This relative inefficiency of the ER QCS is compensated by Golgi checkpoints [8,50,51], which upon recognition of non-native, misfolded membrane protein domains, promote either their ER retrieval via retrotranslocation through the ER-Golgi intermediate compartment (ERGIC) and ERAD or their retention in the Golgi for delivering to lysosomes [23,52]. Quality control at the Golgi apparatus also regulates proteostasis by sorting already mature proteins to their final destination or by processing the proteins imported from the ER before sorting to their site of function [53,54]. Quality control at the ER and Golgi are thus required for maintenance of proteostasis and adequate cell function.
Related Knowledge Centers
- Cytoplasm
- Endomembrane System
- Eukaryote
- Protein
- Vesicle
- Organelle
- Cell
- Protein Targeting
- Biological Membrane
- Endocytosis