Characterization of a novel polyclonal anti-hypusine antibody.

Springerplus

Departments of Medicine, Cellular and Integrative Physiology, and Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202 USA.

Published: September 2013

The translation factor eIF5A is the only protein known to contain the amino acid hypusine, which is formed posttranslationally. Hypusinated eIF5A is necessary for cellular proliferation and responses to extracellular stressors, and has been proposed as a target for pharmacologic therapy. Here, we provide the first comprehensive characterization of a novel polyclonal antibody (IU-88) that specifically recognizes the hypusinated eIF5A. IU-88 will be useful for the investigation of eIF5A biology and for the development of assays recognizing hypusinated eIF5A.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3765601PMC
http://dx.doi.org/10.1186/2193-1801-2-421DOI Listing

Publication Analysis

Top Keywords

hypusinated eif5a
12
characterization novel
8
novel polyclonal
8
eif5a
5
polyclonal anti-hypusine
4
anti-hypusine antibody
4
antibody translation
4
translation factor
4
factor eif5a
4
eif5a protein
4

Similar Publications

Hypusinated and unhypusinated isoforms of the translation factor eIF5A exert distinct effects in models of pancreas development and function.

J Biol Chem

January 2025

Kovler Diabetes Center; Biological Sciences Division; Department of Medicine; Department of Pediatrics, The University of Chicago, Chicago, IL 60637, USA. Electronic address:

Hypusination of eukaryotic translation initiation factor 5A (eIF5A) is essential for its role in translation elongation and termination. Although the function of hypusinated eIF5A (eIF5A) in cellular proliferation is well-characterized, the role of its unhypusinated form (eIF5A) remains unclear. We hypothesized that eIF5A exerts independent, negative effects on cellular replication and metabolism, distinct from the loss of eIF5A.

View Article and Find Full Text PDF

The structural biology of deoxyhypusination complexes.

Structure

January 2025

Małopolska Centre of Biotechnology, Jagiellonian University, Kraków, Poland. Electronic address:

Deoxyhypusination is the first rate-limiting step of the unique post-translational modification-hypusination-that is catalyzed by deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). This modification is essential for the activation of translation factor 5A in eukaryotes (eIF5A) and Archaea (aIF5A). This perspective focuses on the structural biology of deoxyhypusination complexes in eukaryotic and archaeal organisms.

View Article and Find Full Text PDF

Purpose: Understanding the molecular mechanisms of adaptive regulation in the tumor microenvironment is crucial for precision therapy in hepatocellular carcinoma (HCC). We hypothesized that cargo proteins carried by extracellular vesicles (EVs) released in a hypoxic microenvironment might promote HCC progression by remodeling tumor-associated macrophages (TAMs).

Methods: EV protein analysis by label-free proteomics mass spectrometry of HCC cell lines of different tumor grades was performed.

View Article and Find Full Text PDF

The polyamines putrescine, spermidine, and spermine are polycations ubiquitously present in cells, where they exert pleiotropic functions in cellular mechanisms like proliferation, protein synthesis (through the hypusination of the transcription factor EIF5a), redox balance, autophagy, and different forms of cell death [...

View Article and Find Full Text PDF

Deoxyhypusine synthase (DHPS) is an enzyme encoded by the DHPS gene, with high expression in various cancers, including ovarian cancer (OC). DHPS regulates the translation initiation factor EIF5A, and EIF5A2 knockout inhibits OC tumor growth and metastasis by blocking the epithelial-to-mesenchymal transition (EMT) and the TGFβ pathway. In this study, we show that DHPS is amplified in OC patients, and its elevated expression correlates with poor survival.

View Article and Find Full Text PDF

Want 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!