Post-translational modifications on the metal-sequestering protein calprotectin
Abstract Human calprotectin (CP, S100A8/S100A9 oligomer) is an abundant neutrophil protein that contributes to innate immunity by sequestering nutrient metal ions in the extracellular space. This process starves invading microbial pathogens of essential metal nutrients, which can inhibi...
| Main Authors: | , |
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| Other Authors: | |
| Format: | Article |
| Language: | English |
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Springer Netherlands
2023
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| Online Access: | https://hdl.handle.net/1721.1/148222 |
| _version_ | 1811080665262718976 |
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| author | Nolan, Elizabeth M. Peet, Janet J. Y. |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Nolan, Elizabeth M. Peet, Janet J. Y. |
| author_sort | Nolan, Elizabeth M. |
| collection | MIT |
| description | Abstract
Human calprotectin (CP, S100A8/S100A9 oligomer) is an abundant neutrophil protein that contributes to innate immunity by sequestering nutrient metal ions in the extracellular space. This process starves invading microbial pathogens of essential metal nutrients, which can inhibit growth and colonization. Over the past decade, fundamental and clinical studies have revealed that the S100A8 and S100A9 subunits of CP exhibit a variety of post-translational modifications (PTMs). This review summarizes PTMs on the CP subunits that have been detected and highlights two recent studies that evaluated the structural and functional consequences of methionine and cysteine oxidation on CP. Collectively, these investigations indicate that the molecular speciation of extracellular CP is complex and composed of multiple proteoforms. Moreover, PTMs may impact biological function and the lifetime of the protein. It is therefore important that post-translationally modified CP species receive consideration and integration into the current working model for how CP functions in nutritional immunity. |
| first_indexed | 2024-09-23T11:34:49Z |
| format | Article |
| id | mit-1721.1/148222 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T11:34:49Z |
| publishDate | 2023 |
| publisher | Springer Netherlands |
| record_format | dspace |
| spelling | mit-1721.1/1482222023-03-01T03:31:40Z Post-translational modifications on the metal-sequestering protein calprotectin Nolan, Elizabeth M. Peet, Janet J. Y. Massachusetts Institute of Technology. Department of Chemistry Abstract Human calprotectin (CP, S100A8/S100A9 oligomer) is an abundant neutrophil protein that contributes to innate immunity by sequestering nutrient metal ions in the extracellular space. This process starves invading microbial pathogens of essential metal nutrients, which can inhibit growth and colonization. Over the past decade, fundamental and clinical studies have revealed that the S100A8 and S100A9 subunits of CP exhibit a variety of post-translational modifications (PTMs). This review summarizes PTMs on the CP subunits that have been detected and highlights two recent studies that evaluated the structural and functional consequences of methionine and cysteine oxidation on CP. Collectively, these investigations indicate that the molecular speciation of extracellular CP is complex and composed of multiple proteoforms. Moreover, PTMs may impact biological function and the lifetime of the protein. It is therefore important that post-translationally modified CP species receive consideration and integration into the current working model for how CP functions in nutritional immunity. 2023-02-27T14:09:17Z 2023-02-27T14:09:17Z 2023-02-24 2023-02-26T04:14:53Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/148222 Nolan, Elizabeth M. and Peet, Janet J. Y. 2023. "Post-translational modifications on the metal-sequestering protein calprotectin." PUBLISHER_CC en https://doi.org/10.1007/s10534-023-00493-x Creative Commons Attribution https://creativecommons.org/licenses/by/4.0/ The Author(s) application/pdf Springer Netherlands Springer Netherlands |
| spellingShingle | Nolan, Elizabeth M. Peet, Janet J. Y. Post-translational modifications on the metal-sequestering protein calprotectin |
| title | Post-translational modifications on the metal-sequestering protein calprotectin |
| title_full | Post-translational modifications on the metal-sequestering protein calprotectin |
| title_fullStr | Post-translational modifications on the metal-sequestering protein calprotectin |
| title_full_unstemmed | Post-translational modifications on the metal-sequestering protein calprotectin |
| title_short | Post-translational modifications on the metal-sequestering protein calprotectin |
| title_sort | post translational modifications on the metal sequestering protein calprotectin |
| url | https://hdl.handle.net/1721.1/148222 |
| work_keys_str_mv | AT nolanelizabethm posttranslationalmodificationsonthemetalsequesteringproteincalprotectin AT peetjanetjy posttranslationalmodificationsonthemetalsequesteringproteincalprotectin |