Mass Spectrometry for Proteomics-Based Investigation

Woods, Alisa G.; Sokolowska, Izabela; Wetie, Armand G. Ngounou; Channaveerappa, Devika; Dupree, Emmalyn J.; Jayathirtha, Madhuri; Aslebagh, Roshanak; Wormwood, Kelly L.; Darie, Costel C.

doi:10.1007/978-3-030-15950-4_1

Cited by 24 publications

(38 citation statements)

References 180 publications

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“…Thus, we investigated the molecular changes in the atria caused by chronic OSA. Mass spectrometry has been used in analysis of a variety of compounds such as proteins (proteomics [14,23,24]), protein-protein interactions (interactomics [15,25]), post-translational modifications (translatomics [26]), or peptides (peptidomics [27]). In addition, comparative proteomics analysis of proteins from two or more conditions has been successfully used for unbiased interrogation of biological fluids or cellular lysates [23,[28][29][30][31][32][33] for identification of a protein signature characteristic to one condition (i.e.…”

Section: Dysregulated Atrial Proteins In Rats With Severe Apnoeamentioning

confidence: 99%

“…OSA severity is assessed by the apnoea-hypopnea index (AHI), or the average number of apnoeas (complete obstructions) or hypopneas (partial obstructions) per hour [2]. An estimated 20% of adults have mild OSA (AHI 5-15) and 7% of adults have moderate (AHI [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30] to severe (AHI > 30) OSA, with 85% of all patients remaining undiagnosed [1,2]. Obstructive apnoea causes transient hypoxia as well as decreased intrathoracic pressure because of enhanced breathing effort on the collapsed airway [2,3].…”

Section: Introductionmentioning

confidence: 99%

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Atrial electrophysiological and molecular remodelling induced by obstructive sleep apnoea

Channaveerappa

Lux

Wormwood

et al. 2017

J Cellular Molecular Medi

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Obstructive sleep apnoea (OSA) affects 9–24% of the adult population. OSA is associated with atrial disease, including atrial enlargement, fibrosis and arrhythmias. Despite the link between OSA and cardiac disease, the molecular changes in the heart which occur with OSA remain elusive. To study OSA‐induced cardiac changes, we utilized a recently developed rat model which closely recapitulates the characteristics of OSA. Male Sprague Dawley rats, aged 50–70 days, received surgically implanted tracheal balloons which were inflated to cause transient airway obstructions. Rats were given 60 apnoeas per hour of either 13 sec. (moderate apnoea) or 23 sec. (severe apnoea), 8 hrs per day for 2 weeks. Controls received implants, but no inflations were made. Pulse oximetry measurements were taken at regular intervals, and post‐apnoea ECGs were recorded. Rats had longer P wave durations and increased T wave amplitudes following chronic OSA. Proteomic analysis of the atrial tissue homogenates revealed that three of the nine enzymes in glycolysis, and two proteins related to oxidative phosphorylation, were down regulated in the severe apnoea group. Several sarcomeric and pro‐hypertrophic proteins were also up regulated with OSA. Chronic OSA causes proteins changes in the atria which suggest impairment of energy metabolism and enhancement of hypertrophy.

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Section: Dysregulated Atrial Proteins In Rats With Severe Apnoeamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Atrial electrophysiological and molecular remodelling induced by obstructive sleep apnoea

Channaveerappa

Lux

Wormwood

et al. 2017

J Cellular Molecular Medi

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“…The other type of workflow typically utilized in proteomic analysis first involves the digestion of proteins, which are then separated by liquid chromatography before identification with ESI mass spectrometry (Tomanek, 2011). The type of proteomic workflow determined for use in any given proteomic analysis depends on two parameters (Tomanek, 2011;Woods et al, 2014). The first parameter is the type of sample that is being used as the source of proteins (Tomanek, 2011).…”

Section: The Different Types Of Proteomic Workflowsmentioning

confidence: 99%

Section: Sample Preparationmentioning

confidence: 99%

“…Sample preparation, the first step in the proteomic workflow, is essentially the separation of proteins from other interfering macromolecular compounds such as nucleic acids and polysaccharides within a tissue (Tomanek, 2011;Woods et al, 2014). In other words, the aim of sample preparation is to convert the proteins within a tissue sample into a suitable physiochemical state for subsequent protein separation later on in the proteomic workflow (Shaw and Riederer, 2003;Woods et al, 2014). This means that the proteins need to be solubilized, disaggregated, denatured and reduced in order to completely disrupt intra-and intermolecular interactions and to ensure that each spot that is isolated truly represents only a single polypeptide (Shaw and Riederer, 2003;Görg et al, 2004).…”

Section: Sample Preparationmentioning

confidence: 99%

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The Proteomic Rresponses of Gill Tissue in Tidally and Subtidally-Acclimated Mussel Congeners (Mytilus trossulus and Mytilus galloprovincialis) to Acute Aerial-Emersion Hypoxia

Campbell¹

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Understanding species-specific physiological tolerances to environmental extremes is key in determining the factors that contribute to regulating species distribution. This understanding will aid in determining which species will manage to thrive in a changing global climate. According to the IPCC (2013) it is expected that, in the coming years, many different types of abiotic factors will change as a result of global climate change. The intertidal habitat is a model habitat for studying environmental extremes as it is located at the interface between the marine and terrestrial environments, making it one of the most stressful marine habitats. It is characterized by a 24 hr light: dark cycle and a 12.4 tidal ebb and flow that exposes animals inhabiting this habitat to a wide array of aerial-associated stressors such as changes in temperature, aerial exposure, low oxygen or hypoxic conditions and desiccation stress. Sessile organisms such as marine mussels of the genus Mytilus, are an ideal study species for studying physiological tolerance at the environmental extremes of the intertidal habitat. In particular, M. trossulus and M. galloprovincialis are an excellent study system for examining physiological tolerance at environmental extremes due to the recent change in biogeographic range of both species. M. galloprovincialis, a native of the Mediterranean, v has been taking over the coast of California and has been displacing the heat sensitive native M. trossulus. The effects of salinity stress and heat stress on the physiologies of these species have been investigated by Braby and Somero (2006a and 2006b), Tomanek and Zuzow (2010) and Tomanek et al. (2012). The results of these studies indicate that the invasive M. galloprovincialis is more heat tolerant but is sensitive to hyposalinity while the reverse is true for the native M. trossulus. The next logical environmental stress to study is low tide or aerial-emersion as both species can be found both tidally and subtidally. According to Grieshaber et al. (1994) and Müller et al. (2012) Mytilus edulis mussels have mechanisms for mitigating aerial-emersion hypoxia; however, very few studies have been performed using the study system of M. trossulus and M. galloprovincialis in regard to aerial-emersion hypoxia. This study aimed to observe the responses of both M. trossulus and M. galloprovincialis to aerial-emersion hypoxic stress or low tide. The study also looked to see if the recent habitat history (tidal or subtidal) can play a role in the response of the mussels to hypoxia. The results of the experiment indicate that the invasive M. galloprovincialis may be less sensitive to hypoxic stress when compared to the native M. trossulus. This difference in sensitivity may be due to the difference in mechanisms of energy metabolism proteins and proteostasis proteins used to mitigate the effects of hypoxic stress. Moreover, tidal acclimation appears to better prepare the mussels for subsequent aerial exposure in both species, possibly based upon the principles of stres...

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Proteomics analysis of human breast milk by two‐dimensional polyacrylamide gel electrophoresis (2D‐PAGE) coupled with mass spectrometry to assess breast cancer risk

et al. 2023

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Breast cancer (BC) is one of the most common cancers and one of the most common causes for cancer-related mortality. Discovery of protein biomarkers associated with cancer is considered important for early diagnosis and prediction of the cancer risk. Protein biomarkers could be investigated by large-scale protein investigation or proteomics, using mass spectrometry (MS)-based techniques. Our group applies MS-based proteomics to study the protein pattern in human breast milk from women with BC and controls and investigates the alterations and dysregulations of breast milk proteins in comparison pairs of BC versus control. These dysregulated proteins might be considered potential future biomarkers of BC. Identification of potential biomarkers in breast milk may benefit young women without BC, but who could collect the milk for future assessment of BC risk. Previously we identified several dysregulated proteins in different sets of human breast milk samples from BC patients and controls using gel-based protein separation coupled with MS. Here, we performed 2D-PAGE coupled with nano-liquid chromatography-tandem MS (nanoLC-MS/MS) in a small-scale study on a set of six human breast milk pairs (three BC samples vs. three controls) and we identified several dysregulated proteins that have potential roles in cancer progression and might be considered potential BC biomarkers in the future.

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Mass Spectrometry for Proteomics-Based Investigation

Cited by 24 publications

References 180 publications

Atrial electrophysiological and molecular remodelling induced by obstructive sleep apnoea

Atrial electrophysiological and molecular remodelling induced by obstructive sleep apnoea

The Proteomic Rresponses of Gill Tissue in Tidally and Subtidally-Acclimated Mussel Congeners (Mytilus trossulus and Mytilus galloprovincialis) to Acute Aerial-Emersion Hypoxia

Proteomics analysis of human breast milk by two‐dimensional polyacrylamide gel electrophoresis (2D‐PAGE) coupled with mass spectrometry to assess breast cancer risk

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