Format

Send to

Choose Destination
Matrix Biol. 2018 Mar 27. pii: S0945-053X(17)30476-6. doi: 10.1016/j.matbio.2018.03.020. [Epub ahead of print]

TMEM2: A missing link in hyaluronan catabolism identified?

Author information

1
Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address: yyamaguchi@sbpdiscovery.org.
2
Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.

Abstract

Hyaluronan (HA) is a glycosaminoglycan (GAG) composed of repeating disaccharide units of glucuronic acid and N-acetylglucosamine. HA is an extremely long, unbranched polymer, which often exceeds 106 Da and sometimes reaches 107 Da. A feature that epitomizes HA is its rapid turnover; one-third of the total body HA is turned over daily. The current model of HA catabolism postulates that high-molecular weight HA in the extracellular space is first cleaved into smaller fragments by a hyaluronidase(s) that resides at the cell surface, followed by internalization of fragments and their degradation into monosaccharides in lysosomes. Over the last decade, considerable research has shown that the HYAL family of hyaluronidases plays significant roles in HA catabolism. Nonetheless, the identity of a hyaluronidase responsible for the initial step of HA cleavage on the cell surface remains elusive, as biochemical and enzymological properties of HYAL proteins are not entirely consistent with those expected of cell surface hyaluronidases. Recent identification of transmembrane 2 (TMEM2) as a cell surface protein that possesses potent hyaluronidase activity suggests that it may be the "missing" cell surface hyaluronidase, and that novel models of HA catabolism should include this protein.

PMID:
29601864
PMCID:
PMC6314907
[Available on 2019-09-27]
DOI:
10.1016/j.matbio.2018.03.020

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center