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

作者信息

Green S P, Baker M S, Lowther D A

机构信息

Department of Medicine, Melbourne University, John Curtin School of Medical Research, Australian National University, Canberra, ACT.

出版信息

J Rheumatol. 1990 Dec;17(12):1670-5.

PMID:1964699
Abstract

Gel filtration analysis (Sephacryl S-1000) indicated that the Mr of purified equine synovial cell culture 3H-hyaluronic acid (HA) (Mr greater than 1.67 x 10(7) Da) decreased in a concentration dependent manner after exposure to hypochlorite (OCl-). Both high (equine) and medium (human, Mr = 5.5 x 10(5) 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/Cl- system is discussed.

摘要

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