Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus

Magellan Guewo-Fokeng; Eugene Sobngwi; Barbara Atogho-Tiedeu; Jean-Claude Mbanya; Wilfred Mbacham

doi:doi:10.11648/j.bmb.20210602.11

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Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus

Magellan Guewo-Fokeng, Eugene Sobngwi, Barbara Atogho-Tiedeu, Jean-Claude Mbanya, Wilfred Mbacham

Published in Biochemistry and Molecular Biology (Volume 6, Issue 2)

Received: 4 March 2021 Accepted: 22 March 2021 Published: 8 May 2021

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Abstract

The use of heat therapy to treat diseases was very common in Africa. To date, the number of people using this form of therapy is very much on the decrease. Data on the molecular action mechanisms of how it might induce beneficial effects remain unknown. The aim of the present study was to make a contribution towards understanding the putative implication of Heat Shock Protein 70 (HSP70) in the pathophysiology of Type 2 Diabetes Mellitus (T2DM) and the hypothetical benefits of heat therapy through the establishment of a network of protein-protein interactions between Krüppel Like Factor 14 (KLF14), Transcription Factor 7 Like 2 (TCF7L2), Peroxisome Proliferator-Activated Receptor Gamma (PPARG) and HSP70 (HSPA4). Data were generated by the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) software version 10.0. This was used to identify the known and predicted protein-protein interactions (including direct or physical and indirect or functional associations) in the KLF14, TCF7L2, PPARG and HSP70 protein networks. With the active prediction methods (Gene Fusion, Neighborhood, Co-occurrence, Co-expression, Experiments, Databases and Text Mining) as interaction sources, Medium Confidence (0.400) and maximum number of interactions were used to show no more than 50 at the first shell and none at the second shell parameters. Fifty (50) proteins were identified to interact with these four proteins, namely KLF14, TCF7L2, PPARG and HSP70, resulting in a network diagram with 54 nodes (gene/proteins) and 485 edges, representing protein-protein associations. The network showed that HSP70 strongly interacts with other heat shock proteins like HSP90. The HSPBP, a cytoplasmic co-chaperone 1, inhibits HSPA1A chaperone activity by changing the conformation of its ATP-binding domain, thus interfering with this function. Based on the data generated by this in silico study, the potential beneficial effects of heat therapy on T2DM could probably be coordinated by the HSP70 protein-protein interactions involved in cell life and in the susceptibility to T2DM.

Published in	Biochemistry and Molecular Biology (Volume 6, Issue 2)
DOI	10.11648/j.bmb.20210602.11
Page(s)	19-24
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Heat Therapy, Type 2 Diabetes Mellitus, Protein-Protein Interactions

References

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APA Style

Magellan Guewo-Fokeng, Eugene Sobngwi, Barbara Atogho-Tiedeu, Jean-Claude Mbanya, Wilfred Mbacham. (2021). Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus. Biochemistry and Molecular Biology, 6(2), 19-24. https://doi.org/10.11648/j.bmb.20210602.11

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ACS Style

Magellan Guewo-Fokeng; Eugene Sobngwi; Barbara Atogho-Tiedeu; Jean-Claude Mbanya; Wilfred Mbacham. Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus. Biochem. Mol. Biol. 2021, 6(2), 19-24. doi: 10.11648/j.bmb.20210602.11

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AMA Style

Magellan Guewo-Fokeng, Eugene Sobngwi, Barbara Atogho-Tiedeu, Jean-Claude Mbanya, Wilfred Mbacham. Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus. Biochem Mol Biol. 2021;6(2):19-24. doi: 10.11648/j.bmb.20210602.11

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@article{10.11648/j.bmb.20210602.11,
  author = {Magellan Guewo-Fokeng and Eugene Sobngwi and Barbara Atogho-Tiedeu and Jean-Claude Mbanya and Wilfred Mbacham},
  title = {Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus},
  journal = {Biochemistry and Molecular Biology},
  volume = {6},
  number = {2},
  pages = {19-24},
  doi = {10.11648/j.bmb.20210602.11},
  url = {https://doi.org/10.11648/j.bmb.20210602.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bmb.20210602.11},
  abstract = {The use of heat therapy to treat diseases was very common in Africa. To date, the number of people using this form of therapy is very much on the decrease. Data on the molecular action mechanisms of how it might induce beneficial effects remain unknown. The aim of the present study was to make a contribution towards understanding the putative implication of Heat Shock Protein 70 (HSP70) in the pathophysiology of Type 2 Diabetes Mellitus (T2DM) and the hypothetical benefits of heat therapy through the establishment of a network of protein-protein interactions between Krüppel Like Factor 14 (KLF14), Transcription Factor 7 Like 2 (TCF7L2), Peroxisome Proliferator-Activated Receptor Gamma (PPARG) and HSP70 (HSPA4). Data were generated by the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) software version 10.0. This was used to identify the known and predicted protein-protein interactions (including direct or physical and indirect or functional associations) in the KLF14, TCF7L2, PPARG and HSP70 protein networks. With the active prediction methods (Gene Fusion, Neighborhood, Co-occurrence, Co-expression, Experiments, Databases and Text Mining) as interaction sources, Medium Confidence (0.400) and maximum number of interactions were used to show no more than 50 at the first shell and none at the second shell parameters. Fifty (50) proteins were identified to interact with these four proteins, namely KLF14, TCF7L2, PPARG and HSP70, resulting in a network diagram with 54 nodes (gene/proteins) and 485 edges, representing protein-protein associations. The network showed that HSP70 strongly interacts with other heat shock proteins like HSP90. The HSPBP, a cytoplasmic co-chaperone 1, inhibits HSPA1A chaperone activity by changing the conformation of its ATP-binding domain, thus interfering with this function. Based on the data generated by this in silico study, the potential beneficial effects of heat therapy on T2DM could probably be coordinated by the HSP70 protein-protein interactions involved in cell life and in the susceptibility to T2DM.},
 year = {2021}
}

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TY  - JOUR
T1  - Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus
AU  - Magellan Guewo-Fokeng
AU  - Eugene Sobngwi
AU  - Barbara Atogho-Tiedeu
AU  - Jean-Claude Mbanya
AU  - Wilfred Mbacham
Y1  - 2021/05/08
PY  - 2021
N1  - https://doi.org/10.11648/j.bmb.20210602.11
DO  - 10.11648/j.bmb.20210602.11
T2  - Biochemistry and Molecular Biology
JF  - Biochemistry and Molecular Biology
JO  - Biochemistry and Molecular Biology
SP  - 19
EP  - 24
PB  - Science Publishing Group
SN  - 2575-5048
UR  - https://doi.org/10.11648/j.bmb.20210602.11
AB  - The use of heat therapy to treat diseases was very common in Africa. To date, the number of people using this form of therapy is very much on the decrease. Data on the molecular action mechanisms of how it might induce beneficial effects remain unknown. The aim of the present study was to make a contribution towards understanding the putative implication of Heat Shock Protein 70 (HSP70) in the pathophysiology of Type 2 Diabetes Mellitus (T2DM) and the hypothetical benefits of heat therapy through the establishment of a network of protein-protein interactions between Krüppel Like Factor 14 (KLF14), Transcription Factor 7 Like 2 (TCF7L2), Peroxisome Proliferator-Activated Receptor Gamma (PPARG) and HSP70 (HSPA4). Data were generated by the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) software version 10.0. This was used to identify the known and predicted protein-protein interactions (including direct or physical and indirect or functional associations) in the KLF14, TCF7L2, PPARG and HSP70 protein networks. With the active prediction methods (Gene Fusion, Neighborhood, Co-occurrence, Co-expression, Experiments, Databases and Text Mining) as interaction sources, Medium Confidence (0.400) and maximum number of interactions were used to show no more than 50 at the first shell and none at the second shell parameters. Fifty (50) proteins were identified to interact with these four proteins, namely KLF14, TCF7L2, PPARG and HSP70, resulting in a network diagram with 54 nodes (gene/proteins) and 485 edges, representing protein-protein associations. The network showed that HSP70 strongly interacts with other heat shock proteins like HSP90. The HSPBP, a cytoplasmic co-chaperone 1, inhibits HSPA1A chaperone activity by changing the conformation of its ATP-binding domain, thus interfering with this function. Based on the data generated by this in silico study, the potential beneficial effects of heat therapy on T2DM could probably be coordinated by the HSP70 protein-protein interactions involved in cell life and in the susceptibility to T2DM.
VL  - 6
IS  - 2
ER  -

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Author Information

Magellan Guewo-Fokeng

Department of Biochemistry, Faculty of Medicine and Biomedical Sciences, University of Yaounde I, Yaounde, Cameroon
Eugene Sobngwi

The Biotechnology Centre, University of Yaounde I, Nkolbisson, Yaounde, Cameroon
Barbara Atogho-Tiedeu

The Biotechnology Centre, University of Yaounde I, Nkolbisson, Yaounde, Cameroon
Jean-Claude Mbanya

The Biotechnology Centre, University of Yaounde I, Nkolbisson, Yaounde, Cameroon
Wilfred Mbacham

Department of Biochemistry, Faculty of Medicine and Biomedical Sciences, University of Yaounde I, Yaounde, Cameroon

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APA Style

Magellan Guewo-Fokeng, Eugene Sobngwi, Barbara Atogho-Tiedeu, Jean-Claude Mbanya, Wilfred Mbacham. (2021). Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus. Biochemistry and Molecular Biology, 6(2), 19-24. https://doi.org/10.11648/j.bmb.20210602.11

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ACS Style

Magellan Guewo-Fokeng; Eugene Sobngwi; Barbara Atogho-Tiedeu; Jean-Claude Mbanya; Wilfred Mbacham. Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus. Biochem. Mol. Biol. 2021, 6(2), 19-24. doi: 10.11648/j.bmb.20210602.11

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AMA Style

Magellan Guewo-Fokeng, Eugene Sobngwi, Barbara Atogho-Tiedeu, Jean-Claude Mbanya, Wilfred Mbacham. Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus. Biochem Mol Biol. 2021;6(2):19-24. doi: 10.11648/j.bmb.20210602.11

Copy | Download

@article{10.11648/j.bmb.20210602.11,
  author = {Magellan Guewo-Fokeng and Eugene Sobngwi and Barbara Atogho-Tiedeu and Jean-Claude Mbanya and Wilfred Mbacham},
  title = {Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus},
  journal = {Biochemistry and Molecular Biology},
  volume = {6},
  number = {2},
  pages = {19-24},
  doi = {10.11648/j.bmb.20210602.11},
  url = {https://doi.org/10.11648/j.bmb.20210602.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.bmb.20210602.11},
  abstract = {The use of heat therapy to treat diseases was very common in Africa. To date, the number of people using this form of therapy is very much on the decrease. Data on the molecular action mechanisms of how it might induce beneficial effects remain unknown. The aim of the present study was to make a contribution towards understanding the putative implication of Heat Shock Protein 70 (HSP70) in the pathophysiology of Type 2 Diabetes Mellitus (T2DM) and the hypothetical benefits of heat therapy through the establishment of a network of protein-protein interactions between Krüppel Like Factor 14 (KLF14), Transcription Factor 7 Like 2 (TCF7L2), Peroxisome Proliferator-Activated Receptor Gamma (PPARG) and HSP70 (HSPA4). Data were generated by the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) software version 10.0. This was used to identify the known and predicted protein-protein interactions (including direct or physical and indirect or functional associations) in the KLF14, TCF7L2, PPARG and HSP70 protein networks. With the active prediction methods (Gene Fusion, Neighborhood, Co-occurrence, Co-expression, Experiments, Databases and Text Mining) as interaction sources, Medium Confidence (0.400) and maximum number of interactions were used to show no more than 50 at the first shell and none at the second shell parameters. Fifty (50) proteins were identified to interact with these four proteins, namely KLF14, TCF7L2, PPARG and HSP70, resulting in a network diagram with 54 nodes (gene/proteins) and 485 edges, representing protein-protein associations. The network showed that HSP70 strongly interacts with other heat shock proteins like HSP90. The HSPBP, a cytoplasmic co-chaperone 1, inhibits HSPA1A chaperone activity by changing the conformation of its ATP-binding domain, thus interfering with this function. Based on the data generated by this in silico study, the potential beneficial effects of heat therapy on T2DM could probably be coordinated by the HSP70 protein-protein interactions involved in cell life and in the susceptibility to T2DM.},
 year = {2021}
}

Copy | Download

TY  - JOUR
T1  - Heat Shock Protein 70 (HSP70) Protein-Protein Interactions and a Putative Mechanism for the Potential Benefits of Heat Therapy for Type 2 Diabetes Mellitus
AU  - Magellan Guewo-Fokeng
AU  - Eugene Sobngwi
AU  - Barbara Atogho-Tiedeu
AU  - Jean-Claude Mbanya
AU  - Wilfred Mbacham
Y1  - 2021/05/08
PY  - 2021
N1  - https://doi.org/10.11648/j.bmb.20210602.11
DO  - 10.11648/j.bmb.20210602.11
T2  - Biochemistry and Molecular Biology
JF  - Biochemistry and Molecular Biology
JO  - Biochemistry and Molecular Biology
SP  - 19
EP  - 24
PB  - Science Publishing Group
SN  - 2575-5048
UR  - https://doi.org/10.11648/j.bmb.20210602.11
AB  - The use of heat therapy to treat diseases was very common in Africa. To date, the number of people using this form of therapy is very much on the decrease. Data on the molecular action mechanisms of how it might induce beneficial effects remain unknown. The aim of the present study was to make a contribution towards understanding the putative implication of Heat Shock Protein 70 (HSP70) in the pathophysiology of Type 2 Diabetes Mellitus (T2DM) and the hypothetical benefits of heat therapy through the establishment of a network of protein-protein interactions between Krüppel Like Factor 14 (KLF14), Transcription Factor 7 Like 2 (TCF7L2), Peroxisome Proliferator-Activated Receptor Gamma (PPARG) and HSP70 (HSPA4). Data were generated by the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) software version 10.0. This was used to identify the known and predicted protein-protein interactions (including direct or physical and indirect or functional associations) in the KLF14, TCF7L2, PPARG and HSP70 protein networks. With the active prediction methods (Gene Fusion, Neighborhood, Co-occurrence, Co-expression, Experiments, Databases and Text Mining) as interaction sources, Medium Confidence (0.400) and maximum number of interactions were used to show no more than 50 at the first shell and none at the second shell parameters. Fifty (50) proteins were identified to interact with these four proteins, namely KLF14, TCF7L2, PPARG and HSP70, resulting in a network diagram with 54 nodes (gene/proteins) and 485 edges, representing protein-protein associations. The network showed that HSP70 strongly interacts with other heat shock proteins like HSP90. The HSPBP, a cytoplasmic co-chaperone 1, inhibits HSPA1A chaperone activity by changing the conformation of its ATP-binding domain, thus interfering with this function. Based on the data generated by this in silico study, the potential beneficial effects of heat therapy on T2DM could probably be coordinated by the HSP70 protein-protein interactions involved in cell life and in the susceptibility to T2DM.
VL  - 6
IS  - 2
ER  -

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