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Two cell surface proteins bind the sponge Microciona prolifera aggregation factor.

J A Varner1, M M Burger, J F Kaufman

  • 1Biozentrum, University of Basel, Switzerland.

The Journal of Biological Chemistry
|June 15, 1988
PubMed
Summary
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Researchers identified two novel cell surface proteins in marine sponges that bind the aggregation factor (MAF). These proteins, 210-kDa and 68-kDa, are crucial for cell adhesion and may be early invertebrate analogs of vertebrate extracellular matrix proteins.

Area of Science:

  • Marine biology
  • Biochemistry
  • Cellular biology

Background:

  • The marine sponge Microciona prolifera utilizes a proteoglycan-like aggregation factor (MAF) for cell adhesion.
  • Understanding the molecular mechanisms of cell-cell recognition and adhesion in invertebrates is crucial for evolutionary biology.

Purpose of the Study:

  • To identify and characterize cell surface proteins that bind MAF in Microciona prolifera.
  • To elucidate the potential role of these proteins as physiological receptors for MAF and their relationship to known extracellular matrix proteins.

Main Methods:

  • Proteins binding iodinated MAF were identified using SDS-PAGE and Western blotting.
  • Cell surface localization was confirmed by protease sensitivity and immunoprecipitation.
  • Protein properties were assessed using Triton X-114 phase separation, liposome flotation, and affinity chromatography.

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  • High-resolution separation was achieved via FPLC Mono Q anion exchange chromatography.

    • Main Results:

    • Two MAF-binding proteins of 210-kDa and 68-kDa were identified on the cell surface.
    • These proteins are species-specific, protease-sensitive, and non-integral membrane proteins.
    • The 68-kDa protein is a glycoprotein, and both exhibit moderate affinity for MAF.
    • A third MAF-binding protein (95-kDa) was found in the extracellular matrix.

    Conclusions:

    • The 210-kDa and 68-kDa proteins are likely cell surface receptors for MAF in Microciona prolifera.
    • These proteins may represent early invertebrate counterparts to vertebrate extracellular matrix adhesion proteins like fibronectin or vitronectin.
    • The findings suggest a novel set of cell adhesion molecules involved in invertebrate tissue organization and development.