TY - JOUR
T1 - Murine epidermal growth factor peptide (33-42) binds to a YIGSR-specific laminin receptor on both tumor and endothelial cells
AU - Nelson, John
AU - Scott, William N.
AU - Allen, William E.
AU - Wilson, David J.
AU - Harriott, Patrick
AU - McFerran, Neil V.
AU - Walker, Brian
PY - 1996
Y1 - 1996
N2 - A laminin-antagonist peptide, comprising amino acids 33-42 of murine epidermal growth factor (mEGF-(3342)), 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 I-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.
AB - A laminin-antagonist peptide, comprising amino acids 33-42 of murine epidermal growth factor (mEGF-(3342)), 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 I-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.
UR - http://www.scopus.com/inward/record.url?scp=0029955428&partnerID=8YFLogxK
U2 - 10.1074/jbc.271.42.26179
DO - 10.1074/jbc.271.42.26179
M3 - Article
C2 - 8824265
AN - SCOPUS:0029955428
SN - 0021-9258
VL - 271
SP - 26179
EP - 26186
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 42
ER -