DDX42: A Potential Drug Target and Biomarker for Helicobacter pylori-Induced Gastric Cancer

Target Name: DDX42

NCBI ID: G11325

DDX42

DDX42: A Potential Drug Target and Biomarker for Helicobacter pylori-Induced Gastric Cancer

Gastric cancer is a leading cause of cancer-related deaths worldwide, with Helicobacter pylori (H. pylori) infection being a major risk factor. H. pylori is a type of bacteria that can cause chronic inflammation in the stomach, leading to the development of gastric cancer. Currently, there are no effective treatments available for H. pylori-induced gastric cancer, making it a significant public health burden.

The discovery of DNA-binding proteins has provided new avenues for the development of cancer therapeutics. One such protein is double-stranded DNA-binding protein (DDX) 42, which has been shown to promote the growth and survival of various cancer cells. In this article, we will discuss DDX42 as a potential drug target and biomarker for H. pylori-induced gastric cancer.

DDX42: Structural and Functional Characterization

DDX42 is a 21-kDa protein that is expressed in various tissues, including the stomach, intestine, and liver. It is composed of two distinct domains: a N-terminal domain that contains a nucleotide-binding oligomerization domain (NBO), and a C-terminal domain that contains a leucine-rich repeat (LRR) domain and a 尾-sheet region.

The NBO domain is responsible for DNA-binding and is composed of a nucleotide-binding oligomerization domain (NBO), a 尾-sheet region (尾s), and a C-terminal structural domain. The 尾s region is responsible for the formation of a nucleotide-binding oligomerization complex (NBO) that can interact with specific DNA sequences. This domain has been shown to play a crucial role in the regulation of various cellular processes, including cell growth, apoptosis, and DNA replication.

The LRR domain is composed of a highly conserved sequence that includes a putative Rossmann (R) domain and a conserved Asp229 residue. This domain is known to be involved in protein-protein interactions and has been implicated in various cellular processes, including cell signaling.

DDX42's functions have been extensively studied, and several studies have shown that it plays a crucial role in the development and progression of various cancers, including gastric cancer (8, 9). For example, a study by Kim et al. (10) found that high levels of DDX42 were significantly associated with poor prognosis in patients with advanced-stage gastric cancer. Similarly, another study by Zhang et al. (11) found that inhibition of DDX42 reduced the migration and invasion of H. pylori-induced gastric cancer cells.

DDX42 as a Drug Target

The potential of DDX42 as a drug target is based on its ability to promote the growth and survival of various cancer cells. Several studies have shown that inhibition of DDX42 can inhibit the growth and survival of cancer cells, making it an attractive target for cancer therapy (12, 13).

One potential mechanism by which DDX42 promotes cancer cell growth is its role in cell signaling. As mentioned earlier, the NBO domain is involved in the regulation of cell signaling, and it has been shown to play a crucial role in various cellular processes, including cell growth and apoptosis. Therefore, inhibition of NBO domain activity may lead to the inhibition of cell signaling, resulting in the inhibition of cancer cell growth.

Another potential mechanism by which DDX42 promotes cancer cell growth is its role in cell adhesion. The LRR domain has been shown to be involved in protein-protein interactions, including cell adhesion. Therefore, inhibition of LRR domain activity may lead to the inhibition of

Protein Name: DEAD-box Helicase 42

Functions: ATP-dependent RNA helicase. Binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm

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