The hidden side of SERPINB1/Leukocyte Elastase Inhibitor

• Published in: Seminars in cell & developmental biology Vol. 62; pp. 178 - 186
• Main Authors: Torriglia, Alicia, Martin, Elisabeth, Jaadane, Imene
• Format: Journal Article
• Language: English
• Published: England Elsevier 01.02.2017; Academic Press
• Subjects: Animals; Apoptosis; Cellular Biology; Evolution, Molecular; Humans; Leukocyte Elastase - metabolism; Life Sciences; Phylogeny; Protease Inhibitors - metabolism; Serpins - metabolism; Murine neutrophil elastase inhibitor; Leukocyte elastase inhibitor; Inflammation; L-DNase II; Cell migration; Apoptosis; Serpin B1
• ISSN: 1084-9521; 1096-3634
• DOI: 10.1016/j.semcdb.2016.07.010

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.