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3. John H. Johnson

Author

Hubbard, Arnette R., Stoute, Ronald Jr., Wells, Terry W., Borens, Alva, and Taylor, Karen

Subjects
Ethnic, cultural, racial issues/studies, General interest
Abstract

The critical importance of Mr. John H. Johnson's contributions to the world is undeniable and 'beyond category' ('Celebrating The Life And Legacy of John H. Johnson,' Nov. 2005). In thousands [...]

Published
2005

5. Identification of a novel dihydrolipoyl dehydrogenase-binding protein in the pyruvate dehydrogenase complex of the anaerobic parasitic nematode, Ascaris suum.

Author

Klingbeil, M M, Walker, D J, Arnette, R, Sidawy, E, Hayton, K, Komuniecki, P R, and Komuniecki, R

Abstract

A novel dihydrolipoyl dehydrogenase-binding protein (E3BP) which lacks an amino-terminal lipoyl domain, p45, has been identified in the pyruvate dehydrogenase complex (PDC) of the adult parasitic nematode, Ascaris suum. Sequence at the amino terminus of p45 exhibited significant similarity with internal E3-binding domains of dihydrolipoyl transacetylase (E2) and E3BP. Dissociation and resolution of a pyruvate dehydrogenase-depleted adult A. suum PDC in guanidine hydrochloride resulted in two E3-depleted E2 core preparations which were either enriched or substantially depleted of p45. Following reconstitution, the p45-enriched E2 core exhibited enhanced E3 binding, whereas, the p45-depleted E2 core exhibited dramatically reduced E3 binding. Reconstitution of either the bovine kidney or A. suum PDCs with the A. suum E3 suggested that the ascarid E3 was more sensitive to NADH inhibition when bound to the bovine kidney core. The expression of p45 was developmentally regulated and p45 was most abundant in anaerobic muscle. In contrast, E3s isolated from anaerobic muscle or aerobic second-stage larvae were identical. These results suggest that during the transition to anaerobic metabolism, E3 remains unchanged, but it appears that a novel E3BP, p45, is expressed which may help to maintain the activity of the PDC in the face of the elevated intramitochondrial NADH/NAD+ ratios associated with anaerobiosis.

Published
1996

6. Racism as a public health issue in environmental health disparities and environmental justice: working toward solutions.

Author

Beard S, Freeman K, Velasco ML, Boyd W, Chamberlain T, Latoni A, Lasko D, Lunn RM, O'Fallon L, Packenham J, Smarr MM, Arnette R, Cavalier-Keck C, Keck J, Muhammad N, Wilson O, Wilson B, Wilson A, and Dixon D

Subjects
Humans, Environmental Justice, Public Health, Environmental Exposure, Environmental Health, Racism
Abstract

Background: Environmental health research in the US has shown that racial and ethnic minorities and members of low-socioeconomic groups, are disproportionately burdened by harmful environmental exposures, in their homes, workplace, and neighborhood environments that impact their overall health and well-being. Systemic racism is a fundamental cause of these disproportionate exposures and associated health effects. To invigorate and inform current efforts on environmental justice and to raise awareness of environmental racism, the National Institute of Environmental Health Sciences (NIEHS) hosted a workshop where community leaders, academic researchers, and NIEHS staff shared perspectives and discussed ways to inform future work to address health disparities., Objectives: To share best practices learned and experienced in partnerships between academic researchers and communities that are addressing environmental racism across the US; and to outline critical needs and future actions for NIEHS, other federal agencies, and anyone who is interested in conducting or funding research that addresses environmental racism and advances health equity for all communities., Discussion: Through this workshop with community leaders and researchers funded by NIEHS, we learned that partnerships between academics and communities hold great promise for addressing environmental racism; however, there are still profound obstacles. To overcome these barriers, translation of research into plain language and health-protective interventions is needed. Structural changes are also needed in current funding mechanisms and training programs across federal agencies. We also learned the importance of leveraging advances in technology to develop creative solutions that can protect public health., (© 2024. This is a U.S. Government work and not under copyright protection in the US; foreign copyright protection may apply.)

Published
2024
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7. Role of dihydrolipoyl dehydrogenase (E3) and a novel E3-binding protein in the NADH sensitivity of the pyruvate dehydrogenase complex from anaerobic mitochondria of the parasitic nematode, Ascaris suum.

Author

Harmych S, Arnette R, and Komuniecki R

Subjects
Amino Acid Sequence, Anaerobiosis, Animals, Ascaris suum drug effects, Ascaris suum metabolism, Cloning, Molecular, Helminth Proteins physiology, Mitochondria drug effects, Mitochondria metabolism, Molecular Sequence Data, Mutation, Oxidation-Reduction, Peptides isolation & purification, Pyruvate Dehydrogenase Complex isolation & purification, Recombinant Proteins analysis, Recombinant Proteins isolation & purification, Recombinant Proteins metabolism, Sequence Homology, Amino Acid, Structural Homology, Protein, Swine, Ascaris suum enzymology, Dihydrolipoamide Dehydrogenase physiology, Mitochondria enzymology, NAD pharmacology, Peptides physiology, Pyruvate Dehydrogenase Complex metabolism, Pyruvate Dehydrogenase Complex physiology
Abstract

The pyruvate dehydrogenase complex (PDC) plays changing roles during the aerobic-anaerobic transition in the life cycle of the parasitic nematode, Ascaris suum. However, the dihydrolipoyl dehydrogenase (E3) subunit appears to be identical in all stages, despite the fact that the PDC is less sensitive to NADH inhibition in anaerobic muscle. Therefore, we have cloned cDNAs encoding E3 and a novel anaerobic-specific E3-binding protein (E3BP) that lacks the terminal lipoyl domain found in E3BPs from yeast and mammals, and functionally expressed E3 and E3 mutants designed to have decreased dimer stability on the assumption that the binding of E3 to an anaerobic-specific E3BP might stabilize the E3 dimer interface and decrease E3 sensitivity to NADH inhibition. As predicted, the mutants exhibited decreased thermal stability, increased sensitivity to NADH and the binding of E3(Y18F) to the E3-depleted core of the pig heart PDC increased E3 activity and decreased E3 sensitivity to NADH inhibition. However, although the free A. suum E3 was less sensitive to NADH inhibition than the pig heart E3, both E3s were significantly more sensitive to NADH inhibition when assayed with dihydrolipoamide than their corresponding PDCs assayed with pyruvate. More importantly, the binding of rE3 to its core complex had little effect on its apparent K(m) for NAD(+), K(i) for NADH inhibition, or the NADH/NAD(+) ratio yielding 50% inhibition. These data suggest that although binding to the core stabilizes the E3 dimer interface, it does not play a significant role in reducing the sensitivity of the A. suum PDC to NADH inhibition during anaerobiosis.

Published
2002
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