ReviewProceedings of the Japan Academy. Series B, Physical and biological sciences2025
New molecules indispensable for hyaluronan degradation, HYBID (CEMIP/KIAA1199) and TMEM2 (CEMIP2): Differential roles in physiological and pathological non-neoplastic conditions.
Review in Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Heterogeneity of Extracellular Vesicles and Non-Vesicular Nanoparticles in Glioblastoma.Journal of extracellular vesicles · 2025Article
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3 authors.
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Abstract
The biological activity of hyaluronan (HA), a major component of the extracellular matrix in vertebrate tissues, depends on its molecular weight, and thus its degradation is a critical process for HA biological functions. Here, we review the characteristics of newly discovered proteins essential for HA degradation, hyaluronan-binding protein involved in hyaluronan depolymerization (HYBID), also known as cell migration inducing hyaluronidase 1 (CEMIP) and KIAA1199, and transmembrane protein-2 (TMEM2; alias CEMIP2). Human and mouse forms of HYBID exert their HA-degrading activity in special microenvironments including recycling endosomes. Mouse TMEM2 functions as a cell-surface hyaluronidase for HA turnover in local tissues, lymph nodes, and the liver. In contrast, the role of human TMEM2 in HA degradation is the subject of much debate. HYBID expression is upregulated by proinflammatory factors such as histamine and interleukin-6 and downregulated by transforming growth factor-β. HYBID is involved in physiological HA turnover in human skin and joint tissues and plays an important role in their pathological destruction by accelerating HA degradation.
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