Effects of plasma proteins on the adhesion, spreading, polarization in suspension, random motility and chemotaxis of neutrophil leukocytes on polycarbonate (Nuclepore) filtration membrane.

The effects on adhesion, spreading, polarization in suspension, random motility and chemotaxis to N-formyl-methionyl-leucyl-phenyl-alanine (FMLP) of neutrophil leukocytes on polycarbonate (Nuclepore) membrane in the Boyden chamber of purified serum albumin, gamma globulin and fibrinogen, as well as of the Hanks'-soluble components of Cohn fractions III (beta and gamma globulins) and IV (albumin, alpha globulins and transferrin) of plasma proteins were tested in comparison to the corresponding effects of dilute fresh heparinized plasma. Serum albumin, fibrinogen and fibronectin inhibited adhesion of neutrophils, so that the spreading, random motility and chemotaxis of these cells could not be assessed in the presence of these proteins alone. These plasma proteins induced little or no polarization of the cells in suspension. Of the remaining preparations, gamma globulin promoted adhesion and excessive spreading and caused corresponding reduction of random motility and chemotaxis to FMLP of these cells. This plasma protein, even in low concentration, induced marked polarization of neutrophils in suspension. Both Cohn fractions III and IV supported adhesion and permitted random motility and chemotaxis to FMLP approximating that which occurs in dilute plasma. These fractions induced moderate polarization of cells in suspension. Addition of serum albumin or fibronection to the preparations of gamma globulin, or Cohn fractions III or IV did not alter the adhesion, random motility or chemotaxis of the neutrophils in these preparations. These results suggest that alpha and beta globulins, as well as gamma globulins are factors in plasma affecting adhesiveness and polarization of neutrophils and which provide for optimal motility and chemotaxis of these cells on solid substrata.(ABSTRACT TRUNCATED AT 250 WORDS)