scholarly journals Chemical proteomics: a powerful tool for exploring protein lipidation

2013 ◽  
Vol 41 (1) ◽  
pp. 56-61 ◽  
Author(s):  
Elisabeth M. Storck ◽  
Remigiusz A. Serwa ◽  
Edward W. Tate
Keyword(s):  
Present Review ◽  
Chemical Proteomics ◽  
Post Translational Modifications ◽  
Health And Disease ◽  
Protein Lipidation ◽  
Protein Acylation ◽  
Identification And Quantification

The study of post-translational modifications such as protein lipidation is a non-trivial challenge of the post-genomic era. In recent years the field of chemical proteomics has greatly advanced our ability to identify and quantify protein lipidation. In the present review, we give a brief overview of the tools available to study protein acylation, prenylation and cholesterylation, and their application in the identification and quantification of protein lipidation in health and disease.

scholarly journals Emerging mass spectrometry-based proteomics methodologies for novel biomedical applications

2020 ◽  
Vol 48 (5) ◽  
pp. 1953-1966
Author(s):  
Lindsay K. Pino ◽  
Jacob Rose ◽  
Amy O'Broin ◽  
Samah Shah ◽  
Birgit Schilling
Keyword(s):  
Mass Spectrometry ◽  
Human Health ◽  
Protein Complexes ◽  
Protein Quantification ◽  
Intact Protein ◽  
Protein Signaling ◽  
Post Translational Modifications ◽  
Protein Protein Interaction ◽  
Health And Disease ◽  
Proteomics Research

Research into the basic biology of human health and disease, as well as translational human research and clinical applications, all benefit from the growing accessibility and versatility of mass spectrometry (MS)-based proteomics. Although once limited in throughput and sensitivity, proteomic studies have quickly grown in scope and scale over the last decade due to significant advances in instrumentation, computational approaches, and bio-sample preparation. Here, we review these latest developments in MS and highlight how these techniques are used to study the mechanisms, diagnosis, and treatment of human diseases. We first describe recent groundbreaking technological advancements for MS-based proteomics, including novel data acquisition techniques and protein quantification approaches. Next, we describe innovations that enable the unprecedented depth of coverage in protein signaling and spatiotemporal protein distributions, including studies of post-translational modifications, protein turnover, and single-cell proteomics. Finally, we explore new workflows to investigate protein complexes and structures, and we present new approaches for protein–protein interaction studies and intact protein or top-down MS. While these approaches are only recently incipient, we anticipate that their use in biomedical MS proteomics research will offer actionable discoveries for the improvement of human health.

scholarly journals Connexins: Synthesis, Post-Translational Modifications, and Trafficking in Health and Disease

2018 ◽  
Vol 19 (5) ◽  
pp. 1296 ◽  
Author(s):  
Trond Aasen ◽  
Scott Johnstone ◽  
Laia Vidal-Brime ◽  
K. Lynn ◽  
Michael Koval
Keyword(s):  
Post Translational Modifications ◽  
Health And Disease

scholarly journals Platelets in Healthy and Disease States: From Biomarkers Discovery to Drug Targets Identification by Proteomics

2020 ◽  
Vol 21 (12) ◽  
pp. 4541 ◽  
Author(s):  
Erica Gianazza ◽  
Maura Brioschi ◽  
Roberta Baetta ◽  
Alice Mallia ◽  
Cristina Banfi ◽  
...  
Keyword(s):  
Drug Targets ◽  
Disease Diagnosis ◽  
Post Translational Modifications ◽  
Disease States ◽  
Recent Advances ◽  
Health And Disease ◽  
Proteome Changes ◽  
Platelet Proteomics ◽  
The Impact ◽  
Platelet Functions

Platelets are a heterogeneous small anucleate blood cell population with a central role both in physiological haemostasis and in pathological states, spanning from thrombosis to inflammation, and cancer. Recent advances in proteomic studies provided additional important information concerning the platelet biology and the response of platelets to several pathophysiological pathways. Platelets circulate systemically and can be easily isolated from human samples, making proteomic application very interesting for characterizing the complexity of platelet functions in health and disease as well as for identifying and quantifying potential platelet proteins as biomarkers and novel antiplatelet therapeutic targets. To date, the highly dynamic protein content of platelets has been studied in resting and activated platelets, and several subproteomes have been characterized including platelet-derived microparticles, platelet granules, platelet releasates, platelet membrane proteins, and specific platelet post-translational modifications. In this review, a critical overview is provided on principal platelet proteomic studies focused on platelet biology from signaling to granules content, platelet proteome changes in several diseases, and the impact of drugs on platelet functions. Moreover, recent advances in quantitative platelet proteomics are discussed, emphasizing the importance of targeted quantification methods for more precise, robust and accurate quantification of selected proteins, which might be used as biomarkers for disease diagnosis, prognosis and therapy, and their strong clinical impact in the near future.

scholarly journals Inherited and Sporadic Amyotrophic Lateral Sclerosis and Fronto-Temporal Lobar Degenerations arising from Pathological Condensates of Phase Separating Proteins

2019 ◽  
Vol 28 (R2) ◽  
pp. R187-R196 ◽  
Author(s):  
Michael Fernandopulle ◽  
GuoZhen Wang ◽  
Jonathon Nixon-Abell ◽  
Seema Qamar ◽  
Varun Balaji ◽  
...  
Keyword(s):  
Amyotrophic Lateral Sclerosis ◽  
Recent Work ◽  
Neurodegenerative Disorders ◽  
Low Complexity ◽  
Present Review ◽  
Sporadic Amyotrophic Lateral Sclerosis ◽  
Missense Mutations ◽  
Post Translational Modifications ◽  
Intrinsically Disordered ◽  
Lateral Sclerosis

Abstract Recent work on the biophysics of proteins with low complexity, intrinsically disordered domains that have the capacity to form biological condensates has profoundly altered the concepts about the pathogenesis of inherited and sporadic neurodegenerative disorders associated with pathological accumulation of these proteins. In the present review, we use the FUS, TDP-43 and A11 proteins as examples to illustrate how missense mutations and aberrant post-translational modifications of these proteins cause amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration (FTLD).

Deconvoluting the biology and druggability of protein lipidation using chemical proteomics

2021 ◽  
Vol 60 ◽  
pp. 97-112
Author(s):  
Ana Losada de la Lastra ◽  
Sarah Hassan ◽  
Edward W. Tate
Keyword(s):  
Chemical Proteomics ◽  
Protein Lipidation

Mucins: structure, function, and role in pulmonary diseases

1992 ◽  
Vol 263 (4) ◽  
pp. L413-L429 ◽  
Author(s):  
M. C. Rose
Keyword(s):  
Tandem Repeats ◽  
Variable Number ◽  
Cdna Clones ◽  
Detailed Knowledge ◽  
Nucleotide Sugar ◽  
Post Translational Modifications ◽  
Disease States ◽  
Health And Disease ◽  
Pathological Material ◽  
Oligosaccharide Structures

Mucins, major components of the extracellular mucus blanket that protect and lubricate mammalian epithelia, are high-molecular-mass glycoconjugates (154 to > or = 7,000 kDa) with hundreds of oligosaccharide chains in O-glycosidic linkages to a protein backbone. The apparent expression of more than one type of oligosaccharide core structure in mucins isolated from pathological material may reflect either inherent limitations in analysis, disease-related alterations in parameters affecting glycosylation and post-translational modifications (e.g., nucleotide-sugar concentrations, expression of specific glycosyltransferases, rates of transport through the endoplasmic reticulum and Golgi) or the activation of mucin protein genes that are more highly expressed in disease states with different glycosylation patterns. Recent studies have revealed the existence of a family of at least four human mucin proteins; MUC1, MUC2, MUC3, MUC4, each of which contains a variable number of tandem repeats that differ in sequence and size. Full-length sequences of cDNA clones encoding human mucin proteins are currently available only for MUC1 which, in contrast to most airway and intestinal mucins, is membrane associated and not secreted. Current information on mucin oligosaccharides and proteins is reviewed herein. More detailed knowledge of the protein and oligosaccharide structures of mucins will be important in identifying specific role(s) in health and disease, i.e., in the physiological functions of mucus.

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