EIF5A Antibodies

Eukaryotic translation initiation factor 5A-1 (EIF5A)

Has an important role at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity.

With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF- alpha-mediated apoptosis.

Gene Information

Human
Gene Name:	EIF5A
Uniprot:	P63241
Entrez:	1984

Family

Belongs to:
eIF-5A family

Alternative Names

eIF4D; eIF-4D; eIF5A; EIF-5A; EIF5A1; eIF-5A1; eIF-5A-1; eIF5AI; Eukaryotic initiation factor 5A isoform 1; eukaryotic initiation factor 5A; eukaryotic translation initiation factor 5A; eukaryotic translation initiation factor 5A-1; MGC104255; MGC99547; Rev-binding Factor

Molecular Weight

Mass (kDA):
16.832 kDA

Genomic Context

Human
Location:	17p13.1
Sequence:	17; NC_000017.11 (7306999..7312463)

Tissue Specificity

Expressed in umbilical vein endothelial cells and several cancer cell lines (at protein level).

Subcellular Localizations

Cytoplasm. Nucleus. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus, nuclear pore complex. Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions.

Diseases

• Malignant Neoplasms
• Neoplasms
• Carcinoma
• Malaria
• Inflammation
• Malignant Paraganglionic Neoplasm
• Neoplasm Metastasis
• Diabetes Mellitus
• Liver Carcinoma
• Diabetes Mellitus, Non-insulin-dependent
• Hiv Infections
• Cell Invasion
• Hyperplasia

• Malignant Tumor Of Colon
• Colonic Neoplasms
• Cell Transformation, Neoplastic
• Immunologic Deficiency Syndromes
• Malignant Neoplasm Of Breast
• Physiological Stress
• Liver Neoplasms

Interacting Proteins

• CRX
• DHPS
• MEOX2
• REL

Pathways

• Translation
• Cell Proliferation
• Cell Growth
• Cell Cycle
• Localization
• Cell Death
• Transport
• Nuclear Export
• Induction Of Apoptosis
• Cell Differentiation
• Cell Cycle Arrest
• Regulation Of Cell Proliferation
• Rna Interference

• Senescence
• Drug Resistance
• Nucleocytoplasmic Transport
• Cell Migration
• Cell Division
• Programmed Cell Death
• Stem Cell Differentiation

PTMs

• Hydroxylation
• Phosphorylation
• Acetylation
• Reduction
• Cleavage

• Deacetylation
• Methylation
• Carboxylation
• Decarboxylation
• Oxidation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/EIF5A

Best Uses of the EIF5A Marker in Protein Synthesis

If you want to know how the eIF5A marker aids in the detection of malignancies This article will aid you in understanding it. This protein regulates both phases of synthesis of proteins, induces apoptosis and regulates cell growth. We'll explore these aspects in this article as well as how to use them in the purpose of determining if they're a good biomarker.

The biomarker eIF5A can be used to detect malignancy

The expression of eIF5A is linked to several cancers. In fact, the protein has been implicated in the pathogenesis of many different diseases, including diabetes, viral infections, and cancers of the nervous system. Numerous studies have shown that low levels of eIF5A are associated with poor prognosis, lower survival rates and a worse prognosis for patients with large B-cell lymphomas that are diffuse.

eIF5A1 expression is elevated in tumor tissues. This suggests that it could be a biomarker for malignancy. eIF5A activity is associated with poor prognosis, a poor response to chemotherapeutic drugs and metastasis. The altered gene activity is associated with a variety of cancers. eIF5A is a priority target for cancer diagnostics and therapeutics.

In human melanoma, nuclear as well as cytoplasmic eIF5A levels were not correlated with patient survival, with patients who were positive for eIF5A2 having a poorer 5-year survival rate than patients with negative staining. However, knockdown of eIF5A2 could have no effect on cell proliferation or the process of apoptosis. However, it did enhance the extent of invasion. Additionally, knockdown of eIF5A2 reduced the expression of epithelial markers and increased mesenchymal-like cells.

The overexpression of eIF5A2 protein within tumor tissues is associated with an advanced stage of T and local invasion in NSCLC patients. NSCLC patients with high levels of eIF5A2 protein may be an insufficient indicator of their prognosis. The targeting of eIF5A2 protein in A549 cells after TGF-b1 treatment reversed the effect of TGF-b1. The inhibition of eIF5A2 also reduces cell proliferation, causes apoptosis, and enhances the cancer-causing cytotoxicity of the chemotherapy drug cisplatin.

The overexpression of eIF5A2 in ESCC cells has been linked with invasion, lymph node metastasis and lower survival rates among patients. In CRC cells, eIF5A2 was expressed in a higher level. This is a major factor in tumor invasion. It also stimulated mesenchymal markers, such as N-cadherin or fibronectin. It also stimulated lamellipodia.

It regulates both phases of protein synthesis

The function of the EIF5A protein is unclear. It is believed to recruit subsets of mRNA from nucleus for translation and translocation to the cytoplasm. Its association with mitochondria enhances cell survival in arsenate-intolerant circumstances. Below are some examples of the most effective uses of EIF5A in protein synthesizing.

The EIF5A marker is crucial in the process of protein synthesis. eIF5A facilitates the initiation of protein synthesis. It regulates the expression of the mRNA methionyl-puromycin, which is vital for the synthesis of proteins. Elimination of eIF5A causes a slight decrease to the production of protein. It is interesting to note that the protein is a specific factor for specific mRNAs. Mandal and his colleagues found 104 proteins affected by eIF5A loss in the course of a study.

It has been shown that eIF5A can alter levels of polyamine and also controlling metabolite levels. These findings suggest that eIF5A might be involved in epigenetic changes such as cell lineage fidelity as well as polyamine levels. Its crystal structure gives insight into the functional relationship of the EIF5A marker and mTOR within the cell. This discovery is promising for the development of novel therapies that target eIF5A.

eIF5A is a key component in the expression of poly(Pro) proteins. The eIF5A gene has to be expressed to make poly(Pro) proteins. eIF5A knockdown results is decreased expression of these polyproline motifs. This gene is crucial for human trypanosomiasis , as well as polyproline protein synthesis. Therefore the knockdown of eIF5A could result in the eIF5A protein not being able to produce enough of the polyproline motifs.

It induces apoptosis

The study suggests that the alternative start codon eIF5A helps in stress granule assembly. This is a process that reprograms protein expression and enhances cell survival. The findings suggest that eIF5A deficiency may trigger Apoptosis. Researchers also suggested that this protein may contribute to arsenic-induced demise.

Its physiological function isn't yet understood but its upregulation in colorectal and normal mucosa has been believed to encourage tumorigenesis. Furthermore, eIF5A2 expression is associated with ovarian tumors and is strongly associated with tumor stage. Thus, the recently discovered physiological properties of eIF5A are expected to generate many opportunities for clinical studies. This novel pathway has tremendous potential for the treatment of many diseases and is a promising target for new drug development.

eIF5A was first identified to be a part of the nuclear pore complex, and interact with HIV-1 Rev trans-activator protein. These findings led to discovery of a conserved protein within the protein, now referred to as p53. Likewise, Parreiras-e-Silva et al. eIF5A was found to have two distinct cytoplasmic sites. This could suggest that eIF5A could be associated with the endoplasmic retina.

Utilizing an inactive eIF5A mutation hinders the export of the Rev-CRM1 complex to the cytoplasm. This drug hinders HIV-1 replication. eIF5A inhibition also results in the expression of the paralog eIF5A2 which has recently been discovered to be expressed in various cancers. The study suggests that a decreased expression of eIF5A may promote mitochondrial fission, production of reactive oxygen species, and apoptosis. The authors concluded that DFMO blocks the nuclear export system which, in turn, blocks HIV-1 infection.

Several studies have shown that inhibiting eIF5A is an effective and safe method to induce anapoptosis. The results have been replicated in mice as well as drosophila, and the effects of amino acids, protein-rich diets, and sucrose-rich diets have been significant in reducing the number of cells that underwent Apoptosis. These results also prove that eIF5A inhibition is effective in the cells of brain injury.

It regulates cell proliferation.

The enzyme EIF5A inhibits the growth of cells by regulating the synthesis of several factors, such as cytokines and integrins. The presence of the enzyme in cells can indicate if a particular protein is responsible to the proliferation of cells. eIF5A is believed to regulate the growth of various kinds of proteins. Several methods are available to detect eIF5A and its precursors.

eIF5A is a key player in the regulation of cell growth, however, it also plays a role in embryogenesis and differentiation. Parreiras-e -Silva and. observed that eIF5A gene expression was evident at all stages of post-implantation growth in mice. eIF5A levels increased in areas of active differentiation. Additionally the inhibition of eIF5A decreased the number of MyoD transcripts. Interestingly, stem cells taken from skeletal muscle cells of rat expressed eIF5A during differentiation.

This enzyme is most commonly found in isoforms A, which is composed of 154 amino acids. Isoform A, on other hand, contains an extended N-terminal sequence that contains 30 amino acids. This extended N-terminal domain is responsible for its association with mitochondria. When inhibition of eIF5A hinders the expression of eIF5A in cell cultures the cells are protected from kidney damage caused by hypoxia.

eIF5A is involved in a variety of crucial biological functions in eukaryotes. These include protein translation initiation. Its eIF5A activity blocks translation of certain proteins like methionylpuromycin. In the same way, eIF5A regulates the activity of a number of other proteins including those involved in the biogenesis of ribosomes.

It regulates programmed cell death

Many tissues and cells contain the eIF5A gene. There are two versions of eIF5A1, eIF5A2, which are both present. The first is found in almost all cells and tissues. The latter is found in cancer cells, testicles and the brain. The eIF5A1 gene is located on chromosome 3q25-q27.

In 1976, Kemper et al. purified homogeneous factors from rabbit reticulocytes, and called them eIF5A. This small acidic protein can be found in Archaea and is composed of 157 amino acids. It plays an important biological function and has been linked to embryonic development. It is also relatively abundant, accounting for about 1% of the cellular protein pool.

CRC is a result of the EIF5A-DHPS the axis. In mice deficient in DHPS or EIF5A the tumors grew considerably slower than those with controls. They also had reduced size and weight, as well as Ki67 staining and EIF5A hyperusination were significantly decreased. This is a promising strategy to fight CRC. In fact, reducing EIF5A in mice has been proven to reduce the growth of tumors.

The EIF5A mRNA was immunoprecipitated using an antibody against eIF5A. Inhibition of DHPS hindered the translation of MYC, which led to lower MYC levels. These experiments demonstrated that eIF5A is required to facilitate the polyproline motif's translation. This could explain why EIF5A is present in cancer cells.

Recent studies have revealed that the overexpression of EIF5A in cancer cells can result in poor prognosis. Different kinds of cancer have been proven to be expressing EIF5A, a translational regulator. However, only a handful of studies have shown that inhibiting EIF5A in tumor cells has an adverse effect on tumour growth. It is not yet clear what potential translational targets EIF5A may have.