Relationship between binding activity of 67Ga and low sulfated acid glycosaminoglycans

Abstract

The sulfate content of acid glycosaminoglycan (AGAG) extracted from granuloma which had been produced by turpentine oil was inversely proportional to the amount of 67Ga accumulation in the granuloma. Additionally, the lowest sulfation occurred in granuloma at a peak of inflammation when the uptake of 67Ga had reached a maximum. On the basis of electrophoretic pattern, sulfate content, and specific optical rotation, it was concluded that acid glycosaminoglycans obtained from granuloma are mainly composed of chondroitin sulfate-A, -B, and desulfated heparin, while heparan sulfate was a minor component. From in vitro assays, desulfated acid glycosaminoglycans, especially desulfated-heparin and desulfated-heparan sulfate, were found to have a high affinity to 67Ga. These results suggest that low- or de-sulfation of AGAG is related to the accumulation of 67Ga in inflammatory lesions such as granuloma. Moreover, these results suggest that 67Ga does not bind to glycosaminoglycans via sulfuric acid residues.