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Alkaline phosphatase binds to collagen; a hypothesis on the mechanism of extravesicular mineralization in epiphyseal cartilage

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Summary

Affinity chromatography on Sepharose 4B-collagen gels was used to test the affinity of alkaline phosphatase for collagen. Results indicate that 1) alkaline phosphatase of preosseous cartilage binds to collagen probably by electrostatic interactions, 2) this interaction is inhibited by proteoglycan subunits. These results suggest that, in vivo, the formation of a collagen-alkaline phosphatase complex may be a step of the process leading to cartilage calcification.

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Authors and Affiliations

  1. Istituto di Chimica Biologica, Università di Trieste, Via A. Valerio 32, I-34127, Trieste, Italy

    F. Vittur, N. Stagni, L. Moro & B. de Bernard

Authors
  1. F. Vittur
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  2. N. Stagni
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  3. L. Moro
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  4. B. de Bernard
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Additional information

This investigation was supported by research grants of C.N.R. (C.T. 82.02437.04), of Ministero della Pubblica Istruzione and of the University of Trieste.

To whom correspondence and reprint requests should be addressed.

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Vittur, F., Stagni, N., Moro, L. et al. Alkaline phosphatase binds to collagen; a hypothesis on the mechanism of extravesicular mineralization in epiphyseal cartilage. Experientia 40, 836–837 (1984). https://doi.org/10.1007/BF01951980

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  • DOI: https://doi.org/10.1007/BF01951980

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