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In JoVE (1)
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Articles by Mohini Kulp in JoVE
Skeletal Muscle Kjønn Dimorphism fra Proteomikk
Kalina Dimova1, Lauren Ann Metskas2, Mohini Kulp3, Stylianos P. Scordilis4
1Center for Proteomics, Smith College, 2Department of Molecular Biophysics and Biochemistry, Yale University, 3Department of Chemistry, Smith College, 4Department of Biological Sciences and Center for Proteomics, Smith College
En rett-fram sett av metoder for å isolere og fastslå identiteten til de mest tallrike proteinene uttrykt i skjelettmuskulatur. Omtrent 800 flekker er avdekket, på en to-dimensjonal gel fra 10 mg muskler, og dette gjør det mulig for bestemmelse av kjønnsspesifikke protein uttrykk. Disse metodene vil gi tilsvarende resultater i de fleste vev.
Other articles by Mohini Kulp on PubMed
Domain Architecture of Protein-disulfide Isomerase Facilitates Its Dual Role As an Oxidase and an Isomerase in Ero1p-mediated Disulfide Formation
The Journal of Biological Chemistry. Jan, 2006 | Pubmed ID: 16368681
Native disulfide bond formation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and its homologs, which contain varying combinations of catalytically active and inactive thioredoxin domains. However, the specific contribution of PDI to the formation of new disulfides versus reduction/rearrangement of non-native disulfides is poorly understood. We analyzed the role of individual PDI domains in disulfide bond formation in a reaction driven by their natural oxidant, Ero1p. We found that Ero1p oxidizes the isolated PDI catalytic thioredoxin domains, A and A' at the same rate. In contrast, we found that in the context of full-length PDI, there is an asymmetry in the rate of oxidation of the two active sites. This asymmetry is the result of a dual effect: an enhanced rate of oxidation of the second catalytic (A') domain and the substrate-mediated inhibition of oxidation of the first catalytic (A) domain. The specific order of thioredoxin domains in PDI is important in establishing the asymmetry in the rate of oxidation of the two active sites thus allowing A and A', two thioredoxin domains that are similar in sequence and structure, to serve opposing functional roles as a disulfide isomerase and disulfide oxidase, respectively. These findings reveal how native disulfide folding is accomplished in the endoplasmic reticulum and provide a context for understanding the proliferation of PDI homologs with combinatorial arrangements of thioredoxin domains.
Cellular & Molecular Biology Letters. Sep, 2010 | Pubmed ID: 20563704
Skeletal muscle is a plastic tissue with known gender dimorphism, especially at the metabolic level. A proteomic comparison of male and female murine biceps brachii was undertaken, resolving an average of 600 protein spots of MW 15-150 kDa and pI 5-8. Twenty-six unique full-length proteins spanning 11 KOG groups demonstrated statistically significant (p<0.05) abundance differences between genders; the majority of these proteins have metabolic functions. Identified glycolytic enzymes demonstrated decreased abundance in females, while abundance differences in identified oxidative phosphorylation enzymes were specific to the proteins rather than to the functional group as a whole. Certain cytoskeletal and stress proteins showed specific expression differences, and all three phosphorylation states of creatine kinase showed significant decreased abundance in females. Expression differences were significant but many were subtle (< or = 2-fold), and known hormonally-regulated proteins were not identified. We conclude that while gender dimorphism is present in non-exercised murine skeletal muscle, the proteome comparison of male and female biceps brachii in exercise-naive mice indicates subtle differences rather than a large or obviously hormonal dimorphism.