CD44-stimulated dendrite formation ('spreading') in activated B cells

Immunology. 1997 Jan;90(1):147-53. doi: 10.1046/j.1365-2567.1997.00126.x.


A rat monoclonal antibody (mAb) (NIM-R8), insolubilized by binding to plastic plates, induced a rapid and extensive formation of dendrite processes ('spreading') in B lymphocytes activated by anti-IgM and interleukin-4 (IL-4) or anti-CD38 and IL-4. In contrast, resting B cells were unable to spread similarly on the NIM-R8-coated plates. The NIM-R8 antibody recognized a 90,000 MW surface glycoprotein (gp90) present on both B and T lymphocytes. The expression of this molecule was greatly increased after polyclonal (lipopolysaccharide, anti-IgM plus IL-4 or concanavalin A) activation. The NIM-R8 mAb with or without IL-2 or IL-4 was unable to induce proliferation of splenic lymphocytes. Following the demonstration that the NIM-R8 mAb recognizes the murine equivalent of human CD44, the induction of spreading of activated B lymphocytes was studied using a panel of mAb recognizing different epitopes of murine CD44. All of these different mAb induced similar spreading of activated B cells. The ligand-inducible spreading of activated B lymphocytes may be an important mechanism for providing an increased cell-surface area for cell-cell or cell-matrix interactions, and thus may be an important factor controlling the response of activated lymphocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology
  • B-Lymphocytes / cytology
  • B-Lymphocytes / immunology*
  • Cell Size / immunology
  • Dendrites / immunology*
  • Epitopes / immunology
  • Hyaluronan Receptors / immunology*
  • Lymphocyte Activation / immunology*
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / immunology
  • Mice
  • Mice, Inbred BALB C
  • Molecular Weight
  • T-Lymphocytes / immunology


  • Antibodies, Monoclonal
  • Epitopes
  • Hyaluronan Receptors
  • Membrane Glycoproteins