The Hidden side of SERPINB1/Leukocyte Elastase Inhibitor

Abstract : SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS . It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases.
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Seminars in Cell and Developmental Biology, Elsevier, 2017, 62, pp.178-186. 〈10.1016/j.semcdb.2016.07.010〉
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Soumis le : mercredi 27 juillet 2016 - 08:49:58
Dernière modification le : mercredi 21 mars 2018 - 18:57:52

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Alicia Torriglia, Elisabeth Martin, Imene Jaadane. The Hidden side of SERPINB1/Leukocyte Elastase Inhibitor. Seminars in Cell and Developmental Biology, Elsevier, 2017, 62, pp.178-186. 〈10.1016/j.semcdb.2016.07.010〉. 〈inserm-01349216〉

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