Murine epidermal growth factor peptide (33-42) binds to a YIGSR-specific laminin receptor on both tumor and endothelial cells.

Abstract

A laminin-antagonist peptide, comprising amino acids 33-42 of murine epidermal growth factor (mEGF-(33-42)), interacts with a breast cancer- and endothelial cell-associated receptor, which is specific for the laminin B1 chain sequence, CDPGYIGSR-NH2 (Lam.B1-(925-933)), and is immunologically similar to a previously described 67-kDa laminin receptor. In whole cell receptor assays, mEGF-(33-42), Lam. B1-(925-933), and laminin all have IC50 values for displacement of 125I-laminin in the range 1-5 nM. Cell attachment to solid-phase laminin is also blocked by all three ligands, but in contrast to the receptor assays, mEGF-(33-42) or Lam.B1-(925-933), while equipotent with each other, were less effective than laminin. The concentrations of the peptides required to produce half-maximal inhibition of attachment were in the range 230-390 nM, but those for laminin were 1000-fold lower, in the range 0.2-0.3 nM. Like laminin, solid-phase mEGF-(33-42) supports cell attachment, and this ability is blocked by anti-67-kDa receptor antibodies. Modeling studies suggest that both peptides present a tyrosyl and an arginyl residue on the same face of a right-handed helical fold with elliptical cross-section.

• Authors: J Nelson, W N Scott, W E Allen, D J Wilson, P Harriott, N V McFerran, B Walker
• Journal: The Journal of biological chemistry (J Biol Chem) Vol. 271 Issue 42 Pg. 26179-86 (Oct 18 1996) ISSN: 0021-9258 [Print] United States
• PMID: 8824265 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Oligopeptides
• Peptide Fragments
• Receptors, Laminin
• epidermal growth factor (33-42)
• tyrosyl-isoleucyl-glycyl-seryl-arginine
• Epidermal Growth Factor
• Neurokinin B
• neuromedin B

Topics

• Amino Acid Sequence
• Animals
• Binding Sites
• Breast Neoplasms (metabolism)
• Cattle
• Cell Adhesion (drug effects)
• Cell Line
• Chick Embryo
• Endothelium, Vascular (metabolism)
• Epidermal Growth Factor (metabolism)
• Female
• Humans
• Mice
• Models, Molecular
• Molecular Sequence Data
• Neurokinin B (analogs & derivatives, metabolism)
• Oligopeptides (metabolism)
• Peptide Fragments (metabolism)
• Receptors, Laminin (metabolism)
• Tumor Cells, Cultured