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

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 journal › Article › peer-review

33 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 language	English
Pages (from-to)	1670-1675
Number of pages	6
Journal	Journal of Rheumatology
Volume	17
Issue number	12
Publication status	Published - 1990
Externally published	Yes

Keywords

Depolymerization
Hyaluronic acid
Hypochlorite
Myeloperoxidase
Rheumatoid arthritis
Synovial fluid

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@article{2ced676d5058471196a7a1021416ef4f,

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

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.",

keywords = "Depolymerization, Hyaluronic acid, Hypochlorite, Myeloperoxidase, Rheumatoid arthritis, Synovial fluid",

author = "Green, {S. P.} and Baker, {M. S.} and Lowther, {D. A.}",

year = "1990",

language = "English",

volume = "17",

pages = "1670--1675",

journal = "Journal of Rheumatology",

issn = "0315-162X",

publisher = "Journal of Rheumatology Publishing",

number = "12",

}

TY - JOUR

T1 - Depolymerization of synovial fluid hyaluronic acid (HA) by the complete myeloperoxidase (MPO) system may involve the formation of a HA-MPO ionic complex

AU - Green, S. P.

AU - Baker, M. S.

AU - Lowther, D. A.

PY - 1990

Y1 - 1990

N2 - 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.

AB - 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.

KW - Depolymerization

KW - Hyaluronic acid

KW - Hypochlorite

KW - Myeloperoxidase

KW - Rheumatoid arthritis

KW - Synovial fluid

UR - http://www.scopus.com/inward/record.url?scp=0025615119&partnerID=8YFLogxK

M3 - Article

C2 - 1964699

AN - SCOPUS:0025615119

SN - 0315-162X

VL - 17

SP - 1670

EP - 1675

JO - Journal of Rheumatology

JF - Journal of Rheumatology

IS - 12

ER -

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

Abstract

Keywords

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