Case Studies and Enrichment References

Bhagavan, N.V.; Ha, Chung-Eun

doi:10.1016/b978-0-12-095461-2.00038-2

Essentials of Medical Biochemistry 2011

DOI: 10.1016/b978-0-12-095461-2.00038-2

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Case Studies and Enrichment References

N.V. Bhagavan¹,

Chung-Eun Ha²

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Cited by 4 publications

References 335 publications

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Multi‐Omics Reveals Impact of Cysteine Feed Concentration and Resulting Redox Imbalance on Cellular Energy Metabolism and Specific Productivity in CHO Cell Bioprocessing

Ali

Chen

Raju

et al. 2020

Biotechnology Journal

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Chinese hamster ovary (CHO) cells are currently the primary host cell lines used in biotherapeutic manufacturing of monoclonal antibodies (mAbs) and other biopharmaceuticals. Cellular energy metabolism and endoplasmic reticulum (ER) stress are known to greatly impact cell growth, viability, and specific productivity of a biotherapeutic; but the molecular mechanisms are not fully understood. The authors previously employed multi‐omics profiling to investigate the impact of a reduction in cysteine (Cys) feed concentration in a fed‐batch process and found that disruption of the redox balance led to a substantial decline in cell viability and titer. Here, the multi‐omics findings are expanded, and the impact redox imbalance has on ER stress, mitochondrial homeostasis, and lipid metabolism is explored. The reduced Cys feed activates the amino acid response (AAR), increases mitochondrial stress, and initiates gluconeogenesis. Multi‐omics analysis reveals that together, ER stress and AAR signaling shift the cellular energy metabolism to rely primarily on anaplerotic reactions, consuming amino acids and producing lactate, to maintain energy generation. Furthermore, the pathways are demonstrated in which this shift in metabolism leads to a substantial decline in specific productivity and altered mAb glycosylation. Through this work, meaningful bioprocess markers and targets for genetic engineering are identified.

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Multi‐Omics Reveals Impact of Cysteine Feed Concentration and Resulting Redox Imbalance on Cellular Energy Metabolism and Specific Productivity in CHO Cell Bioprocessing

Ali

Chen

Raju

et al. 2020

Biotechnology Journal

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High Strength and High Toughness Electrospun Multifibrillar Yarns with Highly Aligned Hierarchy Intended as Anisotropic Extracellular Matrix

Liao

Jérôme

Agarwal

et al. 2022

Macromolecular Bioscience

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Electrospun nanofibers can be effectively used as a surrogate for extracellular matrices (ECMs). However, in the context of cellular mechanobiology, their mechanical performances can be enhanced by using nanofibrous materials with a high level of structural organization. Herein, this work develops multifibrillar yarns with superior mechanical performance based on biocompatible polyacrylonitrile (PAN) as surrogate ECM. Nearly perfect aligned nanofibers along with the axis of the multifibrillar yarn are prepared. These highly aligned yarns exhibit high strength, high toughness, good stress relaxation behavior, and are robust enough for technical or medical applications. Further, this work analyzes the influence of the highly aligned-hierarchical topological structure of the material on cell proliferation and cell orientation using cells derived from epithelial and connective tissues. Compared to nonoriented electrospun multifibrillar yarns and flat films, the well-ordered topology in the electrospun PAN multifibrillar yarns triggers an improved proliferation of fibroblasts and epithelial cells. Fibroblasts acquire an elongated morphology analogous to their behavior in the natural ECM. Hence, this heterogeneous multifibrillar material can be used to restore or reproduce the ECM for tissue engineering applications, notably in the skeletal muscle and tendon.

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Investigation of mutations (L41F, F17M, N57E, Y99F_Y134W) effects on the TolAIII-UnaG fluorescence protein's unconjugated bilirubin (UC-BR) binding ability and thermal stability properties

Eczacioglu

Ulusu

Gökçe

et al. 2021

Preparative Biochemistry & Biotechnology

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The UnaG protein is a ligand (unconjugated bilirubin) dependent fluorescence protein isolated from Unagi freshwater eel larvae and expressed as fusion in heterologous expression systems. Bilirubin is a tetrapyrrole molecule mainly produced from heme catabolism by the destruction of erythrocytes in the body. Bilirubin can cause kernicterus, a serious condition associated with permanent neurological damage in neonates with the passage of brain tissue. Different methods have been developed for plasma bilirubin analysis and quantification. The use of UnaG fluorescence protein triggered by bilirubin has become a new approach in bilirubin studies. In this study, we aimed to investigate the biophysical characterization of ligand interactions with the proteins obtained as a result of mutations (UnaG Y99F_Y134W , UnaG N57E , UnaG L41F , and UnaG F17M ) on the amino acid sequence of TolAIII-UnaG protein. After the purity levels of the expressed proteins have been analyzed by SDS-PAGE, secondary structures and thermal melting temperatures of the proteins have been examined by circular dichroism spectroscopy. Then determination of excitation and emission points by fluorescence spectroscopy, titration studies have been performed with bilirubin, and dissociation constant was calculated. According to the biophysical characterization studies, UnaG L41F has the highest affinity and stability among the mutants.

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Case Studies and Enrichment References

Cited by 4 publications

References 335 publications

Multi‐Omics Reveals Impact of Cysteine Feed Concentration and Resulting Redox Imbalance on Cellular Energy Metabolism and Specific Productivity in CHO Cell Bioprocessing

Multi‐Omics Reveals Impact of Cysteine Feed Concentration and Resulting Redox Imbalance on Cellular Energy Metabolism and Specific Productivity in CHO Cell Bioprocessing

High Strength and High Toughness Electrospun Multifibrillar Yarns with Highly Aligned Hierarchy Intended as Anisotropic Extracellular Matrix

Investigation of mutations (L41F, F17M, N57E, Y99F_Y134W) effects on the TolAIII-UnaG fluorescence protein's unconjugated bilirubin (UC-BR) binding ability and thermal stability properties

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