Protein NDRG1 Antibodies

Protein NDRG1 (NDRG1)

Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53- mediated caspase activation and apoptosis.

Has a role in cell trafficking, especially of the Schwann cell, and is necessary for the maintenance and development of the peripheral nerve myelin sheath. Required for vesicular recycling of CDH1 and TF.

Gene Information

Human
Gene Name:	NDRG1
Uniprot:	Q92597
Entrez:	10397

Family

Belongs to:
NDRG family

Alternative Names

CAP43; CMT4D; Differentiation-related gene 1 protein; DRG1; DRG-1; DRG1HMSNL; GC4; HMSNL; NDR1; NDRG1; Nickel-specific induction protein Cap43; NMSL; N-myc downstream regulated 1; N-myc downstream-regulated gene 1 protein; protein NDRG1; protein regulated by oxygen-1; PROXY1; Reducing agents and tunicamycin-responsive protein; RIT42; RTP; RTPGC4; TARG1; TDD5; tunicamycin-responsive protein

Molecular Weight

Mass (kDA):
42.835 kDA

Genomic Context

Human
Location:	8q24.22
Sequence:	8; NC_000008.11 (133237175..133297252, complement)

Tissue Specificity

Ubiquitous; expressed most prominently in placental membranes and prostate, kidney, small intestine, and ovary tissues. Also expressed in heart, brain, skeletal muscle, lung, liver and pancreas. Low levels in peripheral blood leukocytes and in tissues of the immune system. Expressed mainly in epithelial cells. Also found in Schwann cells of peripheral neurons. Reduced expression in adenocarcinomas compared to normal tissues. In colon, prostate and placental membranes, the cells that border the lumen show the highest expression.

Subcellular Localizations

Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cell membrane. Mainly cytoplasmic but differentially localized to other regions. Associates with the plasma membrane in intestinal epithelia and lactating mammary gland. Translocated to the nucleus in a p53/TP53-dependent manner. In prostate epithelium and placental chorion, located in both the cytoplasm and in the nucleus. No nuclear localization in colon epithelium cells. In intestinal mucosa, prostate and renal cortex, located predominantly adjacent to adherens junctions. Cytoplasmic with granul

Diseases

• Malignant Neoplasms
• Neoplasms
• Neoplasm Metastasis
• Carcinoma
• Hypoxia
• Cell Invasion
• Malignant Neoplasm Of Prostate
• Malignant Neoplasm Of Breast
• Prostatic Neoplasms
• Mammary Neoplasms
• Charcot-marie-tooth Disease
• Neoplasm Invasiveness

• Adenocarcinoma
• Malignant Paraganglionic Neoplasm
• Carcinogenesis
• Tumor Angiogenesis
• Liver Carcinoma
• Hereditary Motor And Sensory Neuropathies

Interacting Proteins

• AK6
• CANX
• CTNNB1
• XRCC6

Pathways

• Cell Proliferation
• Cell Cycle
• Cell Differentiation
• Cell Growth
• Angiogenesis
• Cell Death
• Pathogenesis
• Cell Migration
• Cell Cycle Arrest
• Localization
• Rna Interference
• Cell Adhesion
• Myelination

• Transport
• Reverse Transcription
• Translation
• Response To Hypoxia
• Senescence
• Cell Activation
• Cell Maturation

PTMs

• Phosphorylation
• Methylation
• Cleavage

• Glycosylation
• Deacetylation
• Acetylation

Research Areas

• Cancer

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/NDRG1

Best Uses Of The NDRG1 Marker

This article explains the possible uses for the NDRG1 gene to diagnose or detect cancer. It also discusses the function of NDRG1 as a glioma treatment and how it can be eliminated using microRNAs. The article also provides a description of how NDRG1 helps to promote the migration of cancer cells through the process of reoxygenation.

NDRG1 could be a diagnostic or prognostic indicator

There is a possibility that NDRG1 could be a diagnostic or prognostic marker for breast cancer. Moreover, breast cancer cells and a small percentage of solid tumors have been found to have an increased level of NDRG1. Charcot-Marie Tooth disease type 4D is a severe condition that causes peripheral neuropathy. Researchers believe that the Schwann complex's deficiency in lipid metabolism is the cause of the disease.

NDRG1 expression in cancer cells has been linked with several cellular processes, including cell cycle and Apoptosis. The gene's expression has been induced by differentiation in cancer cells. In addition, tumors with high NDRG1 expression are more likely to survive than those with low levels of expression. The expression of this gene is typically reduced in prostate and breast cancers.

However, the distinct phosphorylation states of NDRG1 are not related to divergent localization. Additionally, phosphorylation on Thr346 is unique to the decapeptide triple repeat of NDRG1. However, the phosphorylation of Ser330 is shared by all NDRG proteins. Notably, phosphorylation at Thr346 in the NDRG1 protein is associated with punctate cytoplasmic patterns.

Additionally, NDRG1 expression inhibits glioma growth in a mouse-derived xenograft nude model. These studies showed that mice injected with NDRG1 overexpressed cells of glioma had significantly smaller tumors than mice that were injected with siRNA control. NDRG1 expression also inhibited Ki67 expression and produced less tumor microvessels stained with CD31. Western blot was employed to determine NDRG1 expression in glioma cell line lines.

TNM staging is not a comprehensive method for stratifying patients. Functional genomic analysis has confirmed GLUT1 as a possible diagnostic or prognostic marker of OAC. It is also associated with an increase in survival for patients suffering from psoriasis. This study is a promising first step towards discovering molecular biomarkers of cancer.

NDRG1 may be a novel therapeutic target for the treatment of glioma

Research in the past has revealed that NDRG1 is a key factor in the development of multidrug resistance neuroblastoma cell lines. It also causes resistance to HER3 in TNBC cells that are not in TNBC. This resistance can be overcome by targeting PYK2. This approach is promising and could lead to the development of new drugs for the glioma.

NDRG1 was found to be overexpressed in mice with subcutaneous tumors. The increased expression led to a reduction in the rate of proliferation and an increase in the rate of apoptosis. However downregulation of this gene stimulated proliferation and reduced apoptosis in SHG-44 glioma cell lines. In in vitro, NDRG1 transfection in U87MG glioma cell lines resulted n less formation of tubes. In addition, transfection of NDRG1 increased TNFSF15 promoter activity in the glioma cells.

Although NDRG1 is not a known therapeutic target for glioma specifically, it is believed that it could be a great candidate drug candidate for treatment. Cell Signaling Technology, Epitypicomics and Epitypicomics are working on anti-NDRG1 compounds that target the ERK pathway. Both compounds boost p-NDRG1 levels in T and HepG2 cells.

N-myc downstream-regulated gene 1 (NDRG1) also has multi-factorial activities and blocks metastasis arising from different types of tumors. It is a potential anti-cancer target, and thiosemicarbazone-based chemotherapy drugs have been shown to up-regulate NDRG1 and inhibit tumor growth. To know the exact mechanism behind this promising drug's effect further research is needed.

NDRG1 is a biomarker for colorectal cancer. It has a distinct expression pattern within the gut. NDRGs also influence cell proliferation and epithelial-mesenchymal transition, and may play a similar role in cancer. Furthermore, NDRG1 has been linked to breast cancer because its mutations hinder myelination. Mutations that activate NDRG1 cause severe demyelinating neuropathy.

NDRG1 is an oncogene identified to be involved in human brain tumors. Furthermore, NDRG1 inhibits the expression of c-Myc, a transcription factor that is required by glioma cells. This mechanism is not able to explain the entire mechanism that lead to TMZ resistance.

Certain microRNAs may degrade NDRG1

In cancer cells, NDRG1 promotes apoptosis via the death receptor pathway. NDRG1 boosts the activity of death receptor 4 (DR4) and its expression can promote the apoptosis of CRC cells via the TRAIL. Certain microRNAs can be degraded by NDRG1 too. Here, we will examine the mechanisms by which NDRG1 may be degraded by microRNAs.

NDRG1 is involved in tumor metastasis. It reduces tumor growth by increasing p21 protein expression. Its role in the process of tumor metastasis is not understood. It does , however, block the growth of tumors by controlling PI3K/Akt signals pathways. Some microRNAs are capable of degrading NDRG1 and causes tumor growth to slow down.

According to the study, certain microRNAs may regulate NDRG1's function. One of them, miR-769-3p, has been proven to inhibit NDRG1 after the reoxygenation process. The results also suggest that miR-769-3p has several additional target genes that may be responsible for the reoxygenation-induced reduction in NDRG1.

Certain microRNAs are also able to degrade NDRG1. In particular, some of these microRNAs alter the expression of genes related to apoptosis. For instance, NDRG1 knockdown results in an increase in the expression of Bcl-2 protein, while reduction in NDRG1 decreases the expression of Bax. Additionally, the PI3K/Akt pathway is also essential in the glioma. However, increased p-Akt expression is linked to the loss of an phosphatase and homologs of tensin. A previous study found that NDRG1 knockdown leads to increased expression of caspase-8 protein and Bcl-2 protein. Both of them promote apoptosis.

NDRG1 protein expression was found to be low in human Glioma cell lines. However, it was significantly expressed in the normal astroglial cell line 1800. This study suggests that NDRG1 may be a novel therapeutic target or a diagnostic marker. The International Science and Technology Cooperation Project of Ministry of Science and Technology funded the study.

Certain microRNAs could interfere with the expression of NDRG1. NDRG1 can also be blocked by certain microRNAs. Further studies are required to fully comprehend the function of NDRG1.

NDRG1 encourages the migration of cancer cells through the process of reoxygenation

NDRG1 is a growth and cancer-related gene that regulates gene expression and function in both normal and disease states. In this article, we explore the role of NDRG1 in cancer cell migration and reoxygenation adaptation. Our findings show that NDRG1 plays a significant part in the process of tumor adaptation. Further research is needed to determine if NDRG1 could be used as a therapeutic target in the treatment of cancer.

The knockdown of NDRG1 significantly increased the number of tumor cells that express Ki-67. This also decreased the proliferation of NPC cells in vitro and in vivo. These results indicate that knockdown of NDRG1 can cause alterations of tumor cell morphology impacting lymphatic metastasis. Further research is needed to study the therapeutic potential of the knockdown of NDRG1 in humans cancers.

The NDRG1 protein is studied extensively in cancer cells, although crystal structures of NDRG1 as well as NDRG3 may shed light on their function. These proteins are sensitive to changes in O2 levels and respond differently to hypoxia. Moreover their spatial distribution has been studied in different animal models, including zebrafish, frog, and mammalian embryos.

The expression of NDRG1 in breast cancer is a part of an angiogenesis-related gene signature that is associated with metastasis. Breast tumors that have high levels of angiogenic or glycolytic genes are more likely to have NDRG1-induced metastatic disease. This suggests that NDRG1 may protect cancer cells from starvation and increase their lipid utilization.

MiR-769-3p reduces NDRG1 expression Moreover, miR-769-3p regulates NDRG1 during reoxygenation. In addition, miR-769-3p inhibits cell proliferation and the process of apoptosis. However, the exact mechanisms regulating NDRG1 during oxygen changes are not clear. In addition to NDRG1 miR-769-3p has also been discovered to affect cell growth and migration in breast cancer cells.

Recent research has demonstrated that NDRG1 expression is linked with survival rates. Immunohistochemistry (IHC) staining of the samples revealed that NDRG1 expression was highly expressed in normal squamous epithelium , however it was markedly reduced in nasopharyngeal cancers with poor differentiation. It was also determined that NDRG1 protein expression was not present in cancer-free cells.