Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications
Cancer involves a series of diseases where cellular growth is not controlled. Cancer is a leading cause of death worldwide, and the burden of cancer incidence and mortality is rapidly growing, mainly in developing countries. Many drugs are currently used, from chemotherapeutic agents to immunotherap...
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MDPI AG
2023-08-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/28/16/6163 |
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| author | Sergio Enríquez-Flores Ignacio De la Mora-De la Mora Itzhel García-Torres Luis A. Flores-López Yoalli Martínez-Pérez Gabriel López-Velázquez |
| author_facet | Sergio Enríquez-Flores Ignacio De la Mora-De la Mora Itzhel García-Torres Luis A. Flores-López Yoalli Martínez-Pérez Gabriel López-Velázquez |
| author_sort | Sergio Enríquez-Flores |
| collection | DOAJ |
| description | Cancer involves a series of diseases where cellular growth is not controlled. Cancer is a leading cause of death worldwide, and the burden of cancer incidence and mortality is rapidly growing, mainly in developing countries. Many drugs are currently used, from chemotherapeutic agents to immunotherapy, among others, along with organ transplantation. Treatments can cause severe side effects, including remission and progression of the disease with serious consequences. Increased glycolytic activity is characteristic of cancer cells. Triosephosphate isomerase is essential for net ATP production in the glycolytic pathway. Notably, some post-translational events have been described that occur in human triosephosphate isomerase in which functional and structural alterations are provoked. This is considered a window of opportunity, given the differences that may exist between cancer cells and their counterpart in normal cells concerning the glycolytic enzymes. Here, we provide elements that bring out the potential of triosephosphate isomerase, under post-translational modifications, to be considered an efficacious target for treating cancer. |
| first_indexed | 2024-03-10T23:41:25Z |
| format | Article |
| id | doaj.art-594ffe6f4c8d4dd4914b5b7e377db877 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T23:41:25Z |
| publishDate | 2023-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-594ffe6f4c8d4dd4914b5b7e377db8772023-11-19T02:25:56ZengMDPI AGMolecules1420-30492023-08-012816616310.3390/molecules28166163Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational ModificationsSergio Enríquez-Flores0Ignacio De la Mora-De la Mora1Itzhel García-Torres2Luis A. Flores-López3Yoalli Martínez-Pérez4Gabriel López-Velázquez5Laboratorio de Biomoléculas y Salud Infantil, Instituto Nacional de Pediatría, Secretaría de Salud, Mexico City 04530, MexicoLaboratorio de Biomoléculas y Salud Infantil, Instituto Nacional de Pediatría, Secretaría de Salud, Mexico City 04530, MexicoLaboratorio de Biomoléculas y Salud Infantil, Instituto Nacional de Pediatría, Secretaría de Salud, Mexico City 04530, MexicoLaboratorio de Biomoléculas y Salud Infantil, CONAHCYT-Instituto Nacional de Pediatría, Mexico City 04530, MexicoInstituto Tecnológico y de Estudios Superiores de Monterrey, Mexico City 14380, MexicoLaboratorio de Biomoléculas y Salud Infantil, Instituto Nacional de Pediatría, Secretaría de Salud, Mexico City 04530, MexicoCancer involves a series of diseases where cellular growth is not controlled. Cancer is a leading cause of death worldwide, and the burden of cancer incidence and mortality is rapidly growing, mainly in developing countries. Many drugs are currently used, from chemotherapeutic agents to immunotherapy, among others, along with organ transplantation. Treatments can cause severe side effects, including remission and progression of the disease with serious consequences. Increased glycolytic activity is characteristic of cancer cells. Triosephosphate isomerase is essential for net ATP production in the glycolytic pathway. Notably, some post-translational events have been described that occur in human triosephosphate isomerase in which functional and structural alterations are provoked. This is considered a window of opportunity, given the differences that may exist between cancer cells and their counterpart in normal cells concerning the glycolytic enzymes. Here, we provide elements that bring out the potential of triosephosphate isomerase, under post-translational modifications, to be considered an efficacious target for treating cancer.https://www.mdpi.com/1420-3049/28/16/6163glycolysisdeamidationphosphorylationS-nitrosylationpost-translational modification |
| spellingShingle | Sergio Enríquez-Flores Ignacio De la Mora-De la Mora Itzhel García-Torres Luis A. Flores-López Yoalli Martínez-Pérez Gabriel López-Velázquez Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications Molecules glycolysis deamidation phosphorylation S-nitrosylation post-translational modification |
| title | Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications |
| title_full | Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications |
| title_fullStr | Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications |
| title_full_unstemmed | Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications |
| title_short | Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications |
| title_sort | human triosephosphate isomerase is a potential target in cancer due to commonly occurring post translational modifications |
| topic | glycolysis deamidation phosphorylation S-nitrosylation post-translational modification |
| url | https://www.mdpi.com/1420-3049/28/16/6163 |
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