Cell attachment peptide of C-reactive protein: critical amino acids and minimum length.
Human C-reactive protein (CRP) is an acute phase blood component that accumulates at sites of tissue damage and necrosis and is degraded by neutrophils to biologically active peptides. A dodecapeptide composed of amino acids 27-38 of CRP mediates cell attachment in vitro. This peptide was designated the cell-binding peptide (CB-Pep) of CRP. Characterization of the interaction between fibroblasts and modified synthetic peptides with sequential deletions from either the N-terminus or C-terminus revealed that the minimal sequence for cell attachment or inhibition of cell attachment to the CB-Pep was Phe-Thr-Val-Cys-Leu, which corresponds to residues 33-37 within each of the five 206 amino acid subunits of CRP. The pentapeptide by itself mediated cell attachment. Substitutions for each residue within the CB-Pep indicated that the critical residues for activity were Phe-33 and Thr-34. This cell-binding pentapeptide represents a recognition motif for cell adhesion not found in other proteins.
Mullenix
M C
MC
Department of Microbiology, Ohio State University, Columbus 43210.
Kaumaya
P T
PT
Mortensen
R F
RF
D000595:Amino Acid Sequence; D000818:Animals; D002097:C-Reactive Protein / Q000737:chemistry*; D002448:Cell Adhesion; D002460:Cell Line; D005347:Fibroblasts / Q000166:cytology; D005353:Fibronectins; D006801:Humans; D007668:Kidney; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D051381:Rats; D016415:Sequence Alignment; D013329:Structure-Activity Relationship
D005353:Fibronectins; D010446:Peptide Fragments; D002097:C-Reactive Protein