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N-terminal and central regions of the human CD44 extracellular domain participate in cell surface hyaluronan binding.

Publication ,  Journal Article
Liao, HX; Lee, DM; Levesque, MC; Haynes, BF
Published in: J Immunol
October 15, 1995

CD44 molecules are cell surface receptors for hyaluronan (HA). To define regions of the extracellular domain of CD44 that are important for HA binding, we have studied the ability of HA-blocking CD44 mAbs to bind to CD44 from a variety of sources. Five CD44 mAbs (5F12, BRIC235, 3F12, BU-75, and HP2/9) of 21 studied were identified that at least partially blocked FITC-labeled HA (HA-FITC) binding to the standard form of CD44 (CD44S) in CD44-transfected Jurkat cells. Analysis of reactivity of HA-blocking CD44 mAbs defined three distinct epitopes. Lack of reactivity of mAb 5F12 with a CD44 fusion protein (CD44-Rg) containing an N-terminal truncation of 20 amino acids (aa), as well as reactivity of mAb 5F12 with an N-terminal CD44 synthetic peptide (CD44-9A), demonstrated that the N-terminal proximal region of CD44 (aa 1 to 20) was involved in mAb 5F12 binding. A mutant cell line, CEM-NKR, derived from the T-ALL cell line, CEM, did not bind mAb 5F12 nor bind HA, whereas wild-type CEM did bind mAb 5F12 and HA. Sequence analysis of wild-type CEM and CEM-NKR CD44 cDNA demonstrated a G to A point mutation at position 575 in the CD44 cDNA of CEM-NKR, resulting in an arginine to histidine mutation at aa position 154. Taken together, our studies demonstrated that there are three epitopes to which HA-blocking mAbs bind in the extracellular domain of CD44, and that the CD44 N-terminal proximal and central regions are two regions in the extracellular domain of CD44 that may interact and either mediate or regulate HA binding to cell surface CD44.

Duke Scholars

Published In

J Immunol

ISSN

0022-1767

Publication Date

October 15, 1995

Volume

155

Issue

8

Start / End Page

3938 / 3945

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Transfection
  • Recombinant Fusion Proteins
  • Protein Binding
  • Papio
  • Molecular Sequence Data
  • Membrane Proteins
  • Leukemia, T-Cell
  • Immunology
  • Hyaluronic Acid
 

Citation

APA
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MLA
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Liao, H. X., Lee, D. M., Levesque, M. C., & Haynes, B. F. (1995). N-terminal and central regions of the human CD44 extracellular domain participate in cell surface hyaluronan binding. J Immunol, 155(8), 3938–3945.
Liao, H. X., D. M. Lee, M. C. Levesque, and B. F. Haynes. “N-terminal and central regions of the human CD44 extracellular domain participate in cell surface hyaluronan binding.J Immunol 155, no. 8 (October 15, 1995): 3938–45.
Liao HX, Lee DM, Levesque MC, Haynes BF. N-terminal and central regions of the human CD44 extracellular domain participate in cell surface hyaluronan binding. J Immunol. 1995 Oct 15;155(8):3938–45.
Liao, H. X., et al. “N-terminal and central regions of the human CD44 extracellular domain participate in cell surface hyaluronan binding.J Immunol, vol. 155, no. 8, Oct. 1995, pp. 3938–45.
Liao HX, Lee DM, Levesque MC, Haynes BF. N-terminal and central regions of the human CD44 extracellular domain participate in cell surface hyaluronan binding. J Immunol. 1995 Oct 15;155(8):3938–3945.

Published In

J Immunol

ISSN

0022-1767

Publication Date

October 15, 1995

Volume

155

Issue

8

Start / End Page

3938 / 3945

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Transfection
  • Recombinant Fusion Proteins
  • Protein Binding
  • Papio
  • Molecular Sequence Data
  • Membrane Proteins
  • Leukemia, T-Cell
  • Immunology
  • Hyaluronic Acid