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Research Article Free access | 10.1172/JCI106396

The interaction of monosodium urate with connective tissue components

Warren A. Katz and Maxwell Schubert

Department of Medicine, Albert Einstein Medical Center, Moss Rehabilitation Hospital, Korman Research Building, Philadelphia, Pennsylvania 19141

Department of Physical Medicine, Albert Einstein Medical Center, Moss Rehabilitation Hospital, Korman Research Building, Philadelphia, Pennsylvania 19141

Department of Medicine, New York University Medical Center, New York, New York 10021

Find articles by Katz, W. in: PubMed | Google Scholar

Department of Medicine, Albert Einstein Medical Center, Moss Rehabilitation Hospital, Korman Research Building, Philadelphia, Pennsylvania 19141

Department of Physical Medicine, Albert Einstein Medical Center, Moss Rehabilitation Hospital, Korman Research Building, Philadelphia, Pennsylvania 19141

Department of Medicine, New York University Medical Center, New York, New York 10021

Find articles by Schubert, M. in: PubMed | Google Scholar

Published October 1, 1970 - More info

Published in Volume 49, Issue 10 on October 1, 1970
J Clin Invest. 1970;49(10):1783–1789. https://doi.org/10.1172/JCI106396.
© 1970 The American Society for Clinical Investigation
Published October 1, 1970 - Version history
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Abstract

Monosodium urate deposits almost exclusively in the connective tissues of patients with gout. Acetone dried homogenates of bovine nasal cartilage, but not of other tissues, markedly enhances the solubility of urate in buffers having molarities and hydrogen ion concentrations similar to that of most body fluids. The components of cartilage responsible for this effect are the proteinpolysaccharides, compounds of protein and chondroitin sulfate, called PPL. A progressive increase in PPL concentration results in a corresponding increase in urate solubility. If, on the other hand, unbound chondroitin sulfate or PPL digested by trypsin is used, then no significant augmentation of urate solubility occurs indicating that the integrity of the molecule is essential. One subfraction of PPL, PPL5, causes an even more exaggerated response while another, PPL3, causes a lesser one. These proteinpolysaccharide macro-molecules also inhibit the crystallization of urate from a supersaturated medium. The mechanism of the solubilizing phenomenon is not known. It is suggested that some type of physical or chemical binding is responsible. When, as a result of normal or accelerated connective tissue turnover, PPL is enzymatically destroyed, urate crystals then precipitate from the saturated tissue fluids.

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