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Biochemical Markers in Ophthalmology
Published in Ching-Yu Cheng, Tien Yin Wong, Ophthalmic Epidemiology, 2022
Abdus Samad Ansari, Pirro G. Hysi
The term proteomics relates to the analysis of the entire protein complement of a cell, tissue, or organism under a specified set of defined conditions [138]. Proteomics is the process by which different proteins are studied to determine how they interact with each other and the role they play within an organism [139]. Proteomics has facilitated the reporting of an ever-increasing number of proteins and encompasses the investigation of proteomes from the overall level of protein activity, composition, and structure.
Role of Tandem Mass Spectrometry in Diagnosis and Management of Inborn Errors of Metabolism
Published in P. Mereena Luke, K. R. Dhanya, Didier Rouxel, Nandakumar Kalarikkal, Sabu Thomas, Advanced Studies in Experimental and Clinical Medicine, 2021
Kannan Vaidyanathan, Sandhya Gopalakrishnan
Historically, analysis for inborn errors of metabolism has been provided predominantly by research laboratories, each offering analyses only for disorders in line with their scientific interest. With the increasing attentiveness of genetics in medicine and nearly one thousand IEMs identified so far, Clinical Biochemical Genetics is now recognized as a laboratory discipline concerned with the estimation and diagnosis of patients and their families with inherited metabolic disease. Further, this discipline helps in monitoring of treatment and also differentiating heterozygous carriers from non-carriers by series of metabolite and enzymatic analysis. Proteomics is definitely the future of medical diagnosis. Developments in this field are occurring rapidly. Specifically in the field of IEM diagnosis and treatment, proteomics is going to play a dynamic role in future. Currently, TMS is widely used in all developed countries and many developing countries for NBS for IEM.
The Evolution of Anticancer Therapies
Published in David E. Thurston, Ilona Pysz, Chemistry and Pharmacology of Anticancer Drugs, 2021
Proteomics studies complement genomics in that they are designed to directly measure protein rather than mRNA production, thus countering some of the known criticisms of DNA array technologies (e.g., RNA splicing). Proteomics studies normally involve extraction of the entire population of proteins from a cell, followed by their separation using techniques such as two-dimensional electrophoresis followed by identification using mass spectrometry.
How can we use proteomics to learn more about platelets?
Published in Platelets, 2023
Ideally, before conducting a platelet proteomics experiment, researchers should have a specific plan in place for what they will ultimately do with the resulting dataset. It is important to have a clear, well-controlled, research question or goal in mind for proteomics experiments and not conduct experiments merely for the sake of using advanced technologies. Researchers planning to try out proteomics experiments should carefully consider the best- and worst-case scenarios of what their results may or may not provide. On a practical level, it is also important to note that proteomics projects will likely require several months or years of collaborative, open, team-style science before their presentation or publication to ensure that their efforts will not eventually be abandoned and can have the support of all players necessary for completion.
Proteomics in support of immunotherapy: contribution to model-based precision medicine
Published in Expert Review of Proteomics, 2022
Emmanuel Nony, Philippe Moingeon
Proteomics is being used across various therapeutic areas involving a dysregulation of the immune system such as cancer, allergy, infectious diseases and autoimmune and autoinflammatory diseases, for which modulating the patient’ immunity represents a valid option to alleviate symptoms. Irrespective of the disease area, the applications of proteomics share many commonalities. The latter encompass the characterization of the pathophysiology of the disease or of the causing agent (e.g. the antigen, allergen or infectious pathogen). Improving diagnostic, understanding disease heterogeneity and developing predictive and follow-up biomarkers to stratify patients in homogeneous subgroups are also very important applications. Another use of proteomics to support therapies involving the modulation of the patient’s immune system is represented by immunoproteomics, that is the detailed characterization of dysregulated immune responses causative of the disease or elicited during treatment. Proteomics is also highly valuable for quality testing of proteins used for diagnostic or therapeutic purposes. Altogether, these methods will play an important role in the future for implementing a precision medicine approach capitalizing on an unprecedented knowledge of both the disease and the immunotherapeutic drug to offer treatments better tailored to the patient’s needs and specificities.
Proteomic profiling of carbonic anhydrase CA3 in skeletal muscle
Published in Expert Review of Proteomics, 2021
Paul Dowling, Stephen Gargan, Margit Zweyer, Hemmen Sabir, Dieter Swandulla, Kay Ohlendieck
Protein identification from one-dimensional protein bands or two-dimensional gel spots is routinely performed by generating peptide mass fingerprints (PMFs) in combination with matrix-assisted laser-desorption-ionization time-of-flight (MALDI-ToF) mass spectrometry. The MALDI-ToF technique relies on peptide mass fingerprints for protein identification, whereas approaches such as electrospray ionization mass spectrometry (ESI-MS) provide peptide sequence information, which is especially powerful when analyzing complex samples or proteins of low abundance [28]. Liquid chromatography-mass spectrometry (LC-MS) can be employed with both labeling and label-free techniques for protein quantification experiments. Isobaric tags for relative and absolute quantitation (iTRAQ) and tandem mass tag (TMT) technologies are examples of a labeling approach that utilizes isobaric reagents to label amines of peptides and proteins. One type of proteome labeling begins with stable isotope amino acid(s) being included in cell growth media or rodent feed, referred to as SILAC (stable isotope labeling by amino acids in cell culture), while mammalian systems are referred to as SILAM (stable isotope labeling in mammals) [29]. High-throughput proteomics technologies are an important consideration when profiling large numbers of samples. One such high-throughput technology is an aptamer-based proteomics platform called SOMAscan that uses single-stranded oligonucleotides to bind specific proteins and simultaneously quantify hundreds of proteins in many types of protein extracts from cells or plasma [30].