Depolymerization of synovial fluid hyaluronic acid (HA) by the complete myeloperoxidase (MPO) system may involve the formation of a HA-MPO ionic complex

S. P. Green, M. S. Baker*, D. A. Lowther

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)

Abstract

Gel filtration analysis (Sephacryl S-1000) indicated that the M(r) of purified equine synovial cell culture 3H-hyaluronic acid (HA) (M(r) > 1.67 x 107 Da) decreased in a concentration dependent manner after exposure to hypochlorite (OCl-). Both high (equine) and medium (human, M(r) = 5.5 x 105 Da) molecular weight HA were cleaved by the complete myeloperoxidase system (MPO/H2O2/Cl-). Purified human neutrophil myeloperoxidase (MPO) bound tightly to HA-Sepharose and we suggest that this is due to a strong ionic interaction between HA and MPO. The formation of such a complex did not disturb MPO activity. The significance of these results in relation to our previous studies concerning the reduction in viscosity and potential cleavage of HA by the product of the MPO/H2O2/CI- system is discussed.

Original languageEnglish
Pages (from-to)1670-1675
Number of pages6
JournalJournal of Rheumatology
Volume17
Issue number12
Publication statusPublished - 1990
Externally publishedYes

Keywords

  • Depolymerization
  • Hyaluronic acid
  • Hypochlorite
  • Myeloperoxidase
  • Rheumatoid arthritis
  • Synovial fluid

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