• actin-binding-proteins;
  • α-actinin;
  • green algae;
  • immunolocalization;
  • spectrin

Immunochemical detection of actin as well as spectrin-like proteins have been carried out in the green algae Micrasterias denticulata, Closterium lunula, and Euastrum oblongum. In these algae, actin is detected on Western blots at 43kDa with antibodies to actin from higher plant and animal origin. By use of antibodies to human and chicken erythrocyte spectrin a cross-reactivity with desmid proteins is found at about the molecular mass of 220kDa, where also human erythrocyte spectrin is detected. Additional bands are present at 120kDa and 70kDa, which are probably breakdown products. An antibody against chicken α-actinin, a small protein of the spectrin superfamily, recognizes bands at 90kDa, where it is expected, and 70kDa, probably the same breakdown product as mentioned for spectrin. Isoelectric focusing provides staining at pI4.6 with antibodies against spectrin. Immunogold labelling of spectrin and α-actinin antigens on high-pressure frozen, freeze-substituted Micrasterias denticulata cells with the same antibodies exhibits staining, especially at membranes of different populations of secretory vesicles, at dictyosomes, and the plasma membrane. However, no clear correlation to the growth pattern of the cell could be observed. Taken together, our results demonstrate the presence of spectrin-like proteins in desmid cells which are probably functional in exocytosis.