CEMIP ( HYBID , KIAA1199 ): structure, function and expression in health and disease
Sofia Spataroa b, Concetta Guerrac, Andrea Cavallic d, Jacopo Sgrignanic, Jonathan Paul Sleemane f g, Lina Poulainh i, Andreas Bolandh i, Léonardo Scapozzaa b, Solange Mollj k, Marco Prunottoa b✉
- aInstitute of Pharmaceutical Sciences of Western Switzerland University of Geneva Switzerland
- bInstitute of Pharmaceutical Sciences of Western Switzerland, University of Geneva, Switzerland
- cInstitute for Research in Biomedicine Università della Svizzera Italiana Bellinzona Switzerland
- dSwiss Institute of Bioinformatics Lausanne Switzerland
- eEuropean Center for Angioscience (ECAS), Medical Faculty Mannheim Heidelberg University Mannheim Germany
- fInstitute for Biological and Chemical Systems – Biological Information Processing (IBCS – BIP) Karlsruhe Institute for Technology (KIT) Germany
- gEuropean Center for Angioscience (ECAS), Medical Faculty Mannheim, Heidelberg University, Mannheim, Germany
- hDepartment of Molecular Biology University of Geneva Switzerland
- iDepartment of Molecular Biology, University of Geneva, Switzerland
- jDepartment of Pathology University Hospital of Geneva Switzerland
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Abstract
CEMIP (cell migration-inducing protein), also known as KIAA1199 or HYBID, is a protein involved in the depolymerisation of hyaluronic acid (HA), a major glycosaminoglycan component of the extracellular matrix. CEMIP was originally described in patients affected by nonsyndromic hearing loss and has subsequently been shown to play a key role in tumour initiation and progression, as well as arthritis, atherosclerosis and idiopathic pulmonary fibrosis. Despite the vast literature associating CEMIP with these diseases, its biology remains elusive. The present review article summarises all the major scientific evidence regarding its structure, function, role and expression, and attempts to cast light on a protein that modulates EMT, fibrosis and tissue inflammation, an unmet key aspect in several inflammatory disease conditions.
TL;DRAll the major scientific evidence regarding its structure, function, role and expression are summarized, and light is cast on a protein that modulates EMT, fibrosis and tissue inflammation, an unmet key aspect in several inflammatory disease conditions. (Semantic Scholar)