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Related Experiment Videos

Species-specific aggregation factor in sponges. Sialyltransferase associated with aggregation factor.

W E Müller, J Arendes, B Kurelec

    The Journal of Biological Chemistry
    |June 10, 1977
    PubMed
    Summary

    Sialyltransferase in sponges enhances cell aggregation by adding sialic acid to receptors. This enzyme, purified from Geodia cydonium, is crucial for cell communication and adhesion.

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    Area of Science:

    • Biochemistry
    • Marine Biology
    • Cell Biology

    Background:

    • Cell-cell adhesion and communication are vital processes in multicellular organisms.
    • Sialic acids play a significant role in cell surface interactions and recognition.
    • Sponge aggregation provides a model system to study fundamental cell adhesion mechanisms.

    Purpose of the Study:

    • To investigate the role and characteristics of sialyltransferase in the sponge Geodia cydonium.
    • To purify and characterize the enzyme responsible for sialic acid transfer in sponge cell aggregation.
    • To understand the mechanism by which sialylation influences cell aggregation potency.

    Main Methods:

    • Studied sialyltransferase activity in both intact cellular and isolated enzyme systems.

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  • Purified the sialyltransferase using a multi-step chromatographic procedure (Sepharose 4B, CM-cellulose, Sephadex G-100).
  • Determined enzyme kinetics, molecular weight, pH optimum, and requirements for activity.

    • Main Results:

    • Desialylated sponge cells exhibited reduced aggregation compared to controls.
    • Enzymatic sialylation of desialylated cells occurred during aggregation, mediated by an aggregation factor associated with a high molecular weight particle.
    • The purified sialyltransferase (52,000 MW) catalyzes sialic acid transfer from CMP-sialic acid to the aggregation receptor, with optimal activity at pH 7.75 and requiring 200 mM NaCl.

    Conclusions:

    • Sialyltransferase is essential for restoring aggregation potency in desialylated sponge cells.
    • The enzyme is linked to an aggregation factor and acts on specific cell surface receptors.
    • This study elucidates the biochemical properties and functional significance of sialyltransferase in sponge cell aggregation.