Related Experiment Videos

Physarum vitronectin-like protein: an Arg-Gly-Asp-dependent cell-spreading protein with a distinct NH2-terminal

K Miyazaki1, T Hamano, M Hayashi

  • 1Department of Biology, Ochanomizu University, Tokyo, Japan.

Experimental Cell Research
|March 1, 1992
PubMed

Insights

Researchers discovered a 70-kDa protein in slime mold Physarum polycephalum with cell-spreading activity. This Physarum vitronectin-like protein, though functionally similar to animal vitronectins, lacks sequence homology and is inhibited by Arg-Gly-Asp peptides.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Mycology

Background:

  • Vitronectin is a key extracellular matrix protein involved in cell adhesion and spreading.
  • The presence of vitronectin-like proteins in non-animal organisms is largely unexplored.

Purpose of the Study:

  • To isolate and characterize a protein from Physarum polycephalum that cross-reacts with anti-bovine vitronectin antibodies.
  • To investigate the functional properties and sequence homology of the isolated protein.

Main Methods:

  • Isolation of a 70-kDa protein from Physarum polycephalum using antibody cross-reactivity.
  • NH2-terminal amino acid sequencing.
  • Assessment of cell-spreading activity in vitro.
  • Inhibition assays using Arg-Gly-Asp (RGD)-containing peptides.

Main Results:

  • A 70-kDa protein, termed Physarum vitronectin-like protein, was successfully isolated.
  • The protein exhibited cell-spreading activity on substrates.
  • NH2-terminal sequencing revealed no homology with known animal vitronectins.
  • Cell-spreading activity was specifically inhibited by an RGD-containing peptide.

Conclusions:

  • Physarum polycephalum possesses a vitronectin-like protein with functional cell-spreading properties.
  • This protein represents a non-animal homologue of vitronectin, potentially utilizing similar RGD-dependent mechanisms for cell adhesion.

Related Concept Videos