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Human Serum ₂HS-Glycoprotein Modulates in Vitro Bone Resorption^*

Departments of Biochemistry (G.C.C., W.G., G.D.O., R.F.T., M.L., K.S., R.B.N.), Oral Biology, (W.S.L.), and Periodontology (R.B.N.), Boston University School of Medicine and Henry M. Goldman School of Graduate Dentistry, Boston University Medical Center Boston, Massachusettes 02118
Kantonsspital (W.B.) Aarau, Switzerland

Address requests for reprints to: Dr. Richard B. Nimberg, Department of Biochemistry, Boston University Medical Center, 80 East Concord Street, Boston, Massachusetts 02118.

We previously isolated a family of bone-resorbing proteins from human cancer ascites fluid and established that the three purified bone-resorbing proteins were chemically and immunochemically related to each other and to -₂HS glycoprotein (₂HS). After this finding we purified the normal human serum counterpart of these ascites proteins and studied its effects on bone resorption.

The bone-resorbing properties of normal human serum ₂HS were examined in vitro over a wide dose range. This normal human serum glycoprotein had a biphasic effect on ⁴⁵Ca²⁺ release from bone. More specifically, this protein stimulated bone resorption at the lower concentrations tested, with a maximum effect [treated over control ratio of 2.5 ± 0.30 (±SE); P < 0.01] at 40 µg/mL. In contrast, at doses above 40 µg/raL, a sharp decline in calcium mobilization occurred, with a return to baseline occuring above 80 µg/mL. These results suggest that serum ₂HS may participate in the regulation of bone metabolism in vivo.

^* This work was supported by USPHS Grant CA-22062 awarded by the NCI, DHHS, and a grant from the NIH (GM-10374).

Received June 12, 1987.

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