Proteomics and Protein Post-Translational Modification

A special issue of Journal of Cardiovascular Development and Disease (ISSN 2308-3425).

Deadline for manuscript submissions: closed (31 March 2019) | Viewed by 5177

Special Issue Editors


E-Mail Website
Guest Editor
Cardiovascular Research Center, Icahn School of Medicine at Mount Sinai, One Gustave Levy Place, New York, NY 10029, USA
Interests: heart failure; protein-protein interaction; post-translational modifications; gene therapy; small molecule therapy

E-Mail Website
Guest Editor
Cardiovascular Research Center, Icahn School of Medicine at Mount Sinai, New York, NY, USA
Interests: cardiac gene therapy; heart failure; translational research; large animal experiment; cardiac physiology; LV unloading
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

JCDD is launching a Special Issue on "Proteomics and Protein Post-Translational Modification in Heart Disease". Post-translational modifications (PTMs) have been shown to alter protein function by creating new protein binding sites, abrogating protein–protein interactions, or inducing allosteric regulation. Furthermore, the rapid and transient nature of many PTMs allow efficient signal transmission in response to internal and environmental stimuli. PTMs are predominantly triggered by enzymes, and the enzymes responsible are thus attractive targets for therapeutic interventions. Modifications can be grouped according to their stability or transience (reversible versus irreversible): Irreversible types (such as irreversible redox modifications or protein deamidation) are often associated with aging or tissue injury, whereas transient modifications are associated with signal propagation and regulation. This is particularly important in the setting of heart disease, which comprises a diverse range of acute (such as ischemia/reperfusion), chronic (such as heart failure, dilated cardiomyopathy) and genetic (such as hypertrophic cardiomyopathy) disease states, all of which have been associated with protein PTM. This field is rapidly evolving, using multiple approaches, including but not restricted to computational biology, protein arrays, and biochemical analyses, proteomic mapping, molecular and transgenic techniques both in vivo and in vitro. This interesting combination of applications allows for new interpretations and analyses for understanding the evolutionary, developmental and functional therapeutic potential in the setting of heart disease.

Dr. Chang Won Kho
Dr. Kiyotake Ishikawa
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Journal of Cardiovascular Development and Disease is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Heart disease
  • Heart failure
  • Protein–protein interaction
  • Post-translational modifications
  • Proteomics
  • Gene therapy

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:

Research

1605 KiB  
Article
Strategy for Identification of Phosphorylation Levels of Low Abundance Proteins in Vivo for Which Antibodies Are not Available
by Kozo Hayashi, Ryo Yamashita, Ritsuko Takami, Toshikatsu Matsui, Masamitsu Gotou, Tomoyuki Nishimoto and Hiroyuki Kobayashi
J. Cardiovasc. Dev. Dis. 2017, 4(4), 17; https://doi.org/10.3390/jcdd4040017 - 08 Oct 2017
Viewed by 4668
Abstract
Protein function is mainly modulated by dynamic reversible or irreversible post-translational modifications. Among them, the identification of protein phosphorylation sites and changes in phosphorylation levels in vivo are of considerable interest for a better understanding of the protein function. Thus, effective strategies for [...] Read more.
Protein function is mainly modulated by dynamic reversible or irreversible post-translational modifications. Among them, the identification of protein phosphorylation sites and changes in phosphorylation levels in vivo are of considerable interest for a better understanding of the protein function. Thus, effective strategies for the quantitative determination of phosphorylation degrees for low abundant proteins, for which antibodies are not available, are required in order to evaluate the functional regulation of proteins attributed to phosphorylation. In this study, we used the heart β1-adrenergic receptor (Adrb1) as a model protein and developed FLAG-Adrb1 knock-in mice, in which the FLAG tag was inserted at the N-terminus of Adrb1. The phosphorylation sites and levels of Adrb1 in the heart were elucidated by immuno-affinity purification followed by quantitative mass spectrometry analysis using ion intensity ratio of the phosphorylated peptide versus corresponding unphosphorylated peptide. The phosphorylation levels at Ser274 and Ser462 of Adrb1 were approximately 0.25 and 0.0023. This effective strategy should be useful for not only analyzing site-specific phosphorylation levels of target proteins, but also quantifying the expression levels of proteins of interest when appropriate antibodies are not available. Full article
(This article belongs to the Special Issue Proteomics and Protein Post-Translational Modification)
Show Figures

Graphical abstract

Back to TopTop