CEMIP (HYBID, KIAA1199): structure, function and expression in health and disease

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 s...

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Bibliographic Details
Published in:The FEBS journal 2023-08, Vol.290 (16), p.3946-3962
Main Authors: Spataro, Sofia, Guerra, Concetta, Cavalli, Andrea, Sgrignani, Jacopo, Sleeman, Jonathan, Poulain, Lina, Boland, Andreas, Scapozza, Leonardo, Moll, Solange, Prunotto, Marco
Format: Article
Language:English
Subjects:
Arteriosclerosis
Atherosclerosis
Cell migration
CEMIP
Depolymerization
disease
ECM
EMT
Extracellular matrix
Fibrosis
Glycosaminoglycans
Hearing loss
Hyaluronic acid
Inflammatory diseases
Lung diseases
Proteins
Structure-function relationships
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Summary: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. Cell migration‐inducing protein, also called CEMIP, is a protein involved in the depolymerisation of hyaluronic acid (HA), a major component of the extracellular matrix (ECM). In this viewpoint, we discuss the main scientific evidence regarding CEMIP structure, function, role and expression, and we attempt to cast light on a protein that modulates the epithelial–mesenchymal transition (EMT), fibrosis and tissue inflammation, an unmet key aspect in several inflammatory disease conditions.
ISSN:1742-464X
1742-4658
DOI:10.1111/febs.16600