Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancements
Serine protease inhibitors (serpins) are the most numerous and widespread multifunctional protease inhibitor superfamily and are expressed by all eukaryotes. Serpin E2 (serpin peptidase inhibitor, clade E, member 2), a member of the serine protease inhibitor superfamily is a potent endogenous thromb...
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| Format: | Article |
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Frontiers Media S.A.
2024-02-01
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| Series: | Frontiers in Molecular Biosciences |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmolb.2024.1334931/full |
| _version_ | 1797294375675363328 |
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| author | Shutong Wu Shutong Wu Yuchao Yang Yuchao Yang Meiling Zhang Asmat Ullah Khan Jingxing Dai Jun Ouyang |
| author_facet | Shutong Wu Shutong Wu Yuchao Yang Yuchao Yang Meiling Zhang Asmat Ullah Khan Jingxing Dai Jun Ouyang |
| author_sort | Shutong Wu |
| collection | DOAJ |
| description | Serine protease inhibitors (serpins) are the most numerous and widespread multifunctional protease inhibitor superfamily and are expressed by all eukaryotes. Serpin E2 (serpin peptidase inhibitor, clade E, member 2), a member of the serine protease inhibitor superfamily is a potent endogenous thrombin inhibitor, mainly found in the extracellular matrix and platelets, and expressed in numerous organs and secreted by many cell types. The multiple functions of serpin E2 are mainly mediated through regulating urokinase-type plasminogen activator (uPA, also known as PLAU), tissue-type plasminogen activator (tPA, also known as PLAT), and matrix metalloproteinase activity, and include hemostasis, cell adhesion, and promotion of tumor metastasis. The importance serpin E2 is clear from its involvement in numerous physiological and pathological processes. In this review, we summarize the structural characteristics of the Serpin E2 gene and protein, as well as its roles physiology and disease. |
| first_indexed | 2024-03-07T21:30:21Z |
| format | Article |
| id | doaj.art-01a07f3a28e24b71894b14ef43ec6b2e |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-03-07T21:30:21Z |
| publishDate | 2024-02-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-01a07f3a28e24b71894b14ef43ec6b2e2024-02-26T16:59:08ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2024-02-011110.3389/fmolb.2024.13349311334931Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancementsShutong Wu0Shutong Wu1Yuchao Yang2Yuchao Yang3Meiling Zhang4Asmat Ullah Khan5Jingxing Dai6Jun Ouyang7Guangdong Provincial Key Laboratory of Digital Medicine and Biomechanics, Guangdong Engineering Research Center for Translation of Medical 3D Printing Application, National Virtual & Reality Experimental Education Center for Medical Morphology (Southern Medical University), National Key Discipline of Human Anatomy, School of Basic Medical Sciences, Southern Medical University, Guangzhou, ChinaXinjin Branch of Chengdu Municipal Public Security Bureau, Chengdu, ChinaGuangdong Provincial Key Laboratory of Digital Medicine and Biomechanics, Guangdong Engineering Research Center for Translation of Medical 3D Printing Application, National Virtual & Reality Experimental Education Center for Medical Morphology (Southern Medical University), National Key Discipline of Human Anatomy, School of Basic Medical Sciences, Southern Medical University, Guangzhou, ChinaYue Bei People’s Hospital Postdoctoral Innovation Practice Base, Southern Medical University, Guangzhou, ChinaChengdu Municipal Public Security Bureau Wenjiang Branch, Chengdu, ChinaGuangdong Provincial Key Laboratory of Digital Medicine and Biomechanics, Guangdong Engineering Research Center for Translation of Medical 3D Printing Application, National Virtual & Reality Experimental Education Center for Medical Morphology (Southern Medical University), National Key Discipline of Human Anatomy, School of Basic Medical Sciences, Southern Medical University, Guangzhou, ChinaGuangdong Provincial Key Laboratory of Digital Medicine and Biomechanics, Guangdong Engineering Research Center for Translation of Medical 3D Printing Application, National Virtual & Reality Experimental Education Center for Medical Morphology (Southern Medical University), National Key Discipline of Human Anatomy, School of Basic Medical Sciences, Southern Medical University, Guangzhou, ChinaGuangdong Provincial Key Laboratory of Digital Medicine and Biomechanics, Guangdong Engineering Research Center for Translation of Medical 3D Printing Application, National Virtual & Reality Experimental Education Center for Medical Morphology (Southern Medical University), National Key Discipline of Human Anatomy, School of Basic Medical Sciences, Southern Medical University, Guangzhou, ChinaSerine protease inhibitors (serpins) are the most numerous and widespread multifunctional protease inhibitor superfamily and are expressed by all eukaryotes. Serpin E2 (serpin peptidase inhibitor, clade E, member 2), a member of the serine protease inhibitor superfamily is a potent endogenous thrombin inhibitor, mainly found in the extracellular matrix and platelets, and expressed in numerous organs and secreted by many cell types. The multiple functions of serpin E2 are mainly mediated through regulating urokinase-type plasminogen activator (uPA, also known as PLAU), tissue-type plasminogen activator (tPA, also known as PLAT), and matrix metalloproteinase activity, and include hemostasis, cell adhesion, and promotion of tumor metastasis. The importance serpin E2 is clear from its involvement in numerous physiological and pathological processes. In this review, we summarize the structural characteristics of the Serpin E2 gene and protein, as well as its roles physiology and disease.https://www.frontiersin.org/articles/10.3389/fmolb.2024.1334931/fullconformational diseaseshemostasisosteoarthritispathologyphysiological processesreproductive |
| spellingShingle | Shutong Wu Shutong Wu Yuchao Yang Yuchao Yang Meiling Zhang Asmat Ullah Khan Jingxing Dai Jun Ouyang Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancements Frontiers in Molecular Biosciences conformational diseases hemostasis osteoarthritis pathology physiological processes reproductive |
| title | Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancements |
| title_full | Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancements |
| title_fullStr | Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancements |
| title_full_unstemmed | Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancements |
| title_short | Serpin peptidase inhibitor, clade E, member 2 in physiology and pathology: recent advancements |
| title_sort | serpin peptidase inhibitor clade e member 2 in physiology and pathology recent advancements |
| topic | conformational diseases hemostasis osteoarthritis pathology physiological processes reproductive |
| url | https://www.frontiersin.org/articles/10.3389/fmolb.2024.1334931/full |
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