William E. Cotham

University of South Carolina

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Michael D. Walla

University of South Carolina

Terry F. Bidleman

Umeå University

Gerardo G. Piroli

University of South Carolina

Norma Frizzell

University of South Carolina

Jonathan W. C. Brock

University of South Carolina

Richard McCain

University of South Carolina

Jennifer M. Ames

Northumbria University

Reilly T. Enos

University of South Carolina

John Baynes

University of South Carolina

Holland H. Smith

University of South Carolina

Cooperative Institutions

University of South Carolina

Winthrop University

Medical University of South Carolina

University of Georgia

University of South Carolina Sumter

Georgia Southern University

Universidad de Oviedo

University of Tennessee Health Science Center

NOAA National Ocean Service

Columbia University

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GSK‐3β Phosphorylation of Cytoplasmic Dynein Reduces Ndel1 Binding to Intermediate Chains and Alters Dynein Motility

Traffic (2015)

Feng Gao Sachin Hebbar Xu Gao Michael P. Alexander Jai P. Pandey

Glycogen synthase kinase 3 (GSK-3) has been linked to regulation of kinesin-dependent axonal transport in squid and flies, and to indirect regulation of cytoplasmic dynein. We have now found evidence for direct regulation of dynein by mammalian GSK-3β in both neurons and non-neuronal cells. GSK-3β coprecipitates with and phosphorylates mammalian dynein. Phosphorylation of dynein intermediate chain (IC) reduces its interaction with Ndel1, a protein that contributes to dynein force generation. Two conserved residues, S87/T88 in IC-1B and S88/T89 in IC-2C, have been identified as GSK-3 targets by both mass spectrometry and site-directed mutagenesis. These sites are within an Ndel1-binding domain, and mutation of both sites alters the interaction of IC's with Ndel1. Dynein motility is stimulated by (i) pharmacological and genetic inhibition of GSK-3β, (ii) an insulin-sensitizing agent (rosiglitazone) and (iii) manipulating an insulin response pathway that leads to GSK-3β inactivation. Thus, our study connects a well-characterized insulin-signaling pathway directly to dynein stimulation via GSK-3 inhibition.

Dynactin

Dynein ATPase

Kinesin

10.1111/tra.12304

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Citations (53)

Preferential Sorption of Non- and Mono-ortho-polychlorinated Biphenyls to Urban Aerosols

Environmental Science & Technology (1995)

Renee L. Falconer Terry F. Bidleman William E. Cotham

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTPreferential Sorption of Non- and Mono-ortho-polychlorinated Biphenyls to Urban AerosolsRenee L. Falconer, Terry F. Bidleman, and William E. CothamCite this: Environ. Sci. Technol. 1995, 29, 6, 1666–1673Publication Date (Print):June 1, 1995Publication History Published online1 May 2002Published inissue 1 June 1995https://pubs.acs.org/doi/10.1021/es00006a034https://doi.org/10.1021/es00006a034research-articleACS PublicationsRequest reuse permissionsArticle Views151Altmetric-Citations49LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

10.1021/es00006a034

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Citations (52)

Augmenting Skeletal Muscle Estrogen Does not Prevent or Rescue Obesity-linked Metabolic Impairments in Female Mice

Endocrinology (2022)

Ahmed Al-Adhami Christian Unger Marion C Hope William E. Cotham Kandy T. Velázquez

Abstract Aims We developed a novel mouse model with increased skeletal muscle estrogen content via inducible, skeletal-muscle–specific aromatase overexpression (SkM-Arom↑). We proposed to examine the effect that increased skeletal muscle estrogen both in gonadally intact and ovariectomized (OVX) female mice has on preventing or rescuing high-fat diet (HFD)-induced obesity. Methods In the prevention experiment, gonadally intact and OVX SkM-Arom↑ mice and littermate controls were fed a low-fat diet (LFD) or HFD for 13 weeks. SkM-Arom↑ was induced at the initiation of dietary treatment. In the intervention experiment, gonadally intact and OVX SkM-Arom↑ mice and littermate controls were fed an HFD for 14 weeks before induction of SkM-Arom↑ for 6 weeks. Glucose tolerance, insulin action, adipose tissue inflammation, and body composition were assessed. Liquid chromatography–mass spectrometry was used to determine circulating and skeletal muscle steroid content. Results SkM-Arom↑ significantly increased skeletal muscle 17β-estradiol (E2) and estrone (E1) in both experiments. Interestingly, this resulted in leakage of estrogens into circulation, producing a physiologically relevant E2 concentration. Consequently, bone mineral density (BMD) was enhanced and adipose tissue inflammation was reduced in the prevention experiment only. However, no benefits were seen with respect to changes in adiposity or metabolic outcomes. Conclusion We show that increasing skeletal muscle estrogen content does not provide a metabolic benefit in gonadally intact and OVX female mice in the setting of obesity. However, a chronic physiological concentration of circulating E2 can improve BMD and reduce adipose tissue inflammation independently of a metabolic benefit or changes in adiposity.

10.1210/endocr/bqac146

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Citations (5)

Succination of Dihydrolipoyllysine Succinyltransferase by Fumarate Reduces α-Ketoglutarate Dehydrogenase Activity and Exacerbates Mitochondrial ATP Deficits in the Ndufs4 Knockout Model of Leigh Syndrome

Free Radical Biology and Medicine (2022)

Gerardo G. Piroli Richard McCain Allison M. Manuel Shoba Swaminathan Holland H. Smith

10.1016/j.freeradbiomed.2021.12.245

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Citations (0)

Rapid Extraction Method of Quantitating the Lachrymatory Factor of Onion Using Gas Chromatography

Journal of Agricultural and Food Chemistry (1996)

Norman E. Schmidt Leanne M. Santiago H. Donald Eason Kurtus A. Dafford Chris A. Grooms

A rapid extraction method has been developed for the quantitation of (Z,E)-propanethial S-oxide, the lachrymatory factor (LF), and other flavor chemicals in onion (Allium cepa) using gas chromatography. This method involves crushing the onion and extracting the resulting juice with a solution of methylene chloride and an internal standard. The resulting extract is concentrated and injected onto a gas chromatograph. This method is shown to be simple, fast, and reproducible. Results show that onion juice contains 1−22 μmol of the LF/mL. Keywords: Onion; Allium cepa; onion lachrymatory factor; gas chromatography

10.1021/jf950686s

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Identification of protein succination as a novel modification of tubulin

Biochemical Journal (2014)

Gerardo G. Piroli Allison M. Manuel Michael D. Walla Matthew J. Jepson Jonathan W. C. Brock

Protein succination is a stable post-translational modification that occurs when fumarate reacts with cysteine residues to generate 2SC [S-(2-succino)cysteine]. We demonstrate that both α- and β-tubulin are increasingly modified by succination in 3T3-L1 adipocytes and in the adipose tissue of db/db mice. Incubation of purified tubulin from porcine brain with fumarate (50 mM) or the pharmacological compound DMF (dimethylfumarate, 500 μM) inhibited polymerization up to 35% and 59% respectively. Using MS we identified Cys347α, Cys376α, Cys12β and Cys303β as sites of succination in porcine brain tubulin and the relative abundance of succination at these cysteine residues increased in association with fumarate concentration. The increase in succination after incubation with fumarate altered tubulin recognition by an anti-α-tubulin antibody. Succinated tubulin in adipocytes cultured in high glucose compared with normal glucose also had reduced reactivity with the anti-α-tubulin antibody; suggesting that succination may interfere with tubulin-protein interactions. DMF reacted rapidly with 11 of the 20 cysteine residues in the αβ-tubulin dimer, decreased the number of free thiols and inhibited the proliferation of 3T3-L1 fibroblasts. Our data suggest that inhibition of tubulin polymerization is an important undocumented mechanism of action of DMF. Taken together, our results demonstrate that succination is a novel post-translational modification of tubulin and suggest that extensive modification by fumarate, either physiologically or pharmacologically, may alter microtubule dynamics.

Mechanism of Action

10.1042/bj20131581

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Citations (42)

Quantification of the immunometabolite protein modifications S-2-succinocysteine and 2,3-dicarboxypropylcysteine

AJP Endocrinology and Metabolism (2024)

J. Hunter Cox Richard McCain E Tran Shoba Swaminathan Holland H. Smith

Itaconate and fumarate have roles as immunometabolites modulating the macrophage response to inflammation. Both immunometabolites chemically modify protein cysteine residues to modulate the immune response. Itaconate and fumarate levels change dynamically, whereas their stable protein modifications can be quantified by mass spectrometry. This method distinguishes itaconate and fumarate-derived protein modifications and will allow researchers to quantify their contributions in isolated cell types and tissues across a range of metabolic diseases.

10.1152/ajpendo.00354.2023

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Citations (1)

Degradation of malathion, endosulfan, and fenvalerate in seawater and seawater/sediment microcosms

Journal of Agricultural and Food Chemistry (1989)

William E. Cotham Terry F. Bidleman

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDegradation of malathion, endosulfan, and fenvalerate in seawater and seawater/sediment microcosmsWilliam E. Cotham Jr. and Terry F. BidlemanCite this: J. Agric. Food Chem. 1989, 37, 3, 824–828Publication Date (Print):May 1, 1989Publication History Published online1 May 2002Published inissue 1 May 1989https://pubs.acs.org/doi/10.1021/jf00087a055https://doi.org/10.1021/jf00087a055research-articleACS PublicationsRequest reuse permissionsArticle Views515Altmetric-Citations91LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

Fenvalerate

Endosulfan

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10.1021/jf00087a055

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Citations (112)

Proteomic Analysis of Arginine Adducts on Glyoxal-modified Ribonuclease

Molecular & Cellular Proteomics (2004)

William E. Cotham Thomas Metz P. Lee Ferguson Jonathan W. C. Brock Davinia J. S. Hinton

Glyoxal

Chemical modification

10.1074/mcp.m400002-mcp200

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Citations (50)

Electrospray ionization quadrupole time-of-flight mass spectrometry and quadrupole mass spectrometry for genotyping single nucleotide substitutions in intact polymerase chain reaction products in K-ras and p53

Rapid Communications in Mass Spectrometry (2002)

Warees T. Muhammad Karen F. Fox Alvin Fox William E. Cotham Michael D. Walla

Abstract Single nucleotide polymorphisms (SNPs) and mutations were genotyped for both homozygous and heterozygous PCR products of p53, a tumor suppressor gene, and K‐ras, an oncogene, using electrospray ionization (ESI) quadrupole time‐of‐flight (Q‐TOF) mass spectrometry (MS) and ESI‐quadrupole MS analysis. Mass accuracy was adequate for both instruments to detect genetic changes in homozygous PCR products, including the most difficult to distinguish (adenine [A] → thymine [T] transversion). However, for the detection of A → T shifts (9.0 Da difference) in heterozygous PCR products, the increased resolution of ESI‐Q‐TOFMS proved essential. Although, greater mass differences in heterozygotes (e.g. cytosine [C] ↔ T or guanine [G] ↔ A) can be discriminated using ESI‐quadrupole MS analysis. Copyright © 2002 John Wiley & Sons, Ltd.

10.1002/rcm.859

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Citations (11)