JPB is an open access journal that aims to publish the advanced and latest research developments in the field of proteomics and bioinformatics.

Mass spectrometry has emerged as an important analytical tool for gaining a better understanding of mechanisms underlying Huntington's disease (HD), alongside the increased availability of cell and animal models of the disease. This review, published in the Journal of Huntington's Disease, brings together and recaps data from major published mass spectrometry studies undertaken in HD research over the last 20 years, identifying important changes that occur in HD. The authors encourage researchers to make greater use of these studies to accelerate the development of new treatments.

HD is a rare neurodegenerative disorder caused by the aberrant expression of mutant Huntingtin  protein containing an expanded polyglutamine tract. Mass spectrometry is a technique that has existed for over a century to measure the mass-to-charge ratio of ions, however, proteins in complex mixtures such as tissues were not commonly analyzed until more modern ionization methods became available.

The authors have explained mass spectrometry in terms understandable for most biologists. Although these studies have yielded copious, useful data, researchers in the HD field have been unaware of just how many such studies have been performed.

"There are several advantages of using mass spectrometry," explained Kimberly B. Kegel-Gleason, MassGeneral Institute for Neurodegenerative Disease, Department of Neurology, Massachusetts General Hospital, Charlestown, MA, USA. "First, it is objective—scientists don't need to have a preformed idea or candidate proteins in mind, which frees the experiment of our preconceptions and allows us to identify changes that we might not have thought of. Second, recent advances in the hardware have made it easier to detect many proteins, including those at very low levels in a mixed sample. Finally, expanded gene databases provided by whole genome sequencing now allow accurate 'annotation' or identification of the proteins of interest."

HTT is now known to have a wide variety of post translational modifications. In the early 2000s, mass spectrometry was used to identify Hap40 as part of protein complex with HTT. It was also used to investigate the difference in wild-type and HD proteomes. Following this study, several other investigators performed whole proteome studies in both human and mouse HD models. Many researchers have taken this a step further to investigate the HTT interactome  using mass spectrometry, and also examined HTT itself to identifying novel PTMs.

Notable among the studies reviewed are 15 proteome studies that sought to determine changes in expression levels and five Interactome studies that looked at changes in how HTT interacts with other proteins. These studies compared brain tissue from animal models and autopsy tissue from patients with HD compared to controls. Importantly, three studies used cerebral spinal fluid from controls and patients with HD in an effort to identify biomarkers for disease progression. They also highlight four studies that identified posttranslational modifications on the Huntingtin protein.

Journal of Proteomics and Bioinformatics announces papers for the upcoming issue. Interested can submit their manuscript through online portal.

Submit manuscript at https://www.longdom.org/proteomics-bioinformatics/submit-manuscript.htmlor send as an e-mail attachment to the Editorial Office at proteomics@escientificjournals.com

Media contact:

Eliza Grace

Managing Editor

Journal of Proteomics and Bioinformatics

Mail ID: proteomics@longdomjournal.org