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PMID: 17170110 Published · ppublish English Journal Article

CD44-dependent intracellular and extracellular catabolism of hyaluronic acid by hyaluronidase-1 and -2.

The Journal of biological chemistry ·Vol. 282 ·No. 8 ·2007-02-23 ·Pages 5597-607

Harada H, Takahashi M

Abstract

Hyaluronic acid (HA) is a high molecular weight glycosaminoglycan involved in a wide variety of cellular functions. However, its turnover in living cells remains largely unknown. In this study, CD44, a receptor for HA, and hyaluronidase-1, -2, and -3 (Hyal-1, -2 and -3) were stably expressed in HEK 293 cells and the mechanism of HA catabolism was systematically investigated using fluorescein-labeled HA. CD44 was essential for HA degradation by both endogenous and exogenously expressed hyaluronidases. Hyal-1 was not able to cleave HA in living cells in the absence of CD44. Intracellular HA degradation was predominantly mediated by Hyal-1 after incorporation of HA by CD44. Although Hyal-1 was active only in intracellular space in vivo, a certain amount of the enzyme was secreted to extracellular space. This extracellular Hyal-1 was found to be incorporated by cells and such uptake of Hyal-1 was, in part, involved in the intracellular degradation of HA. Hyal-2 was involved in the extracellular degradation of HA. Hyal-2 activity was also dependent on the expression of CD44 in both living cells and enzyme assays. Immunofluorescent microscopy demonstrated that both Hyal-2 and CD44 are present on the cell surface. Without CD44 expression, Hyal-2 existed in a granular pattern, and did not show hyaluronidase activity, suggesting that localization change could contribute to Hyal-2 function. A convenient and quantitative enzyme assay was established for the measurement of Hyal-2 activity. Hyal-2 activity was detected in the membrane fraction of cells co-expressing Hyal-2 and CD44. The pH optimum for Hyal-2 was 6.0-7.0. The membrane fraction of cells expressing Hyal-2 alone did not show hyaluronidase activity. Hyal-3 did not show any hyaluronidase activity in our experimental conditions. Based on these findings, Hyal-1 and -2 contribute to intracellular and extracellular catabolism of HA, respectively, in a CD44-dependent manner, and their HA degradation occurs independently from one another.

MeSH Terms
Animals Antigens, Neoplasm/genetics,metabolism Cell Line Cell Membrane/enzymology Gene Expression Regulation, Enzymologic/physiology Histone Acetyltransferases/genetics,metabolism Humans Hyaluronan Receptors/genetics,metabolism Hyaluronic Acid/metabolism Hyaluronoglucosaminidase Hydrogen-Ion Concentration beta-N-Acetylhexosaminidases/genetics,metabolism
Chemicals
Antigens, Neoplasm Hyaluronan Receptors Hyaluronic Acid Histone Acetyltransferases OGA protein, human Hyaluronoglucosaminidase beta-N-Acetylhexosaminidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Harada Hosami
Lead Discovery Research Laboratories, Sankyo Co., Ltd., 1-2-58 Hiromachi, Shinagawa-ku, Tokyo 140-8710, Japan. [email protected]
Takahashi Masaaki
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2007-02-23
Epub
2006-00-14
Pages
5597-607
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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