The aggregated form of an AAMP derived peptide behaves as a heparin sensitive cell binding agent
✍ Scribed by Marie E. Beckner; Henry C. Krutzsch; Maria Tsokos; Douglas E. Moul; Lance A. Liotta
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 291 KB
- Volume
- 54
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
✦ Synopsis
Abstracts: A peptide termed P189, derived from the sequence of a newly discovered protein, AAMP (angio-assoto form biocompatible blood-contacting plastic surfaces ciated migratory cell protein), contains a motif that is on medical devices (extracorporeal and implantable).
predicted to bind heparin. It occurs near the amino termi-Some peptides mediate interactions with specific cell nal end of AAMP. Previous studies have shown that in surface receptors in the absence of serum (Dai and its solubilized form P189 (RRLRRMESESES) binds heparin and melanoma cells. The peptide is bipolar in that it con- . They may be used as agents for cell tains positive charges at its amino end and negative sorting, purging, or identification by strongly binding charges at its carboxyl end. It forms strongly aggregated specific cell surface molecules.
particles that require exposure to 50% DMSO and 100ЊC Peptide P189, derived from AAMP (angio-associated for solubilization to occur. Now heparin and cell binding migratory cell protein), contains a predicted heparin (heparin sensitive) are also demonstrated for the peptide in its particulate form. Cell binding/clustering to the pepbinding region that is near AAMP's amino terminal tide particles is strong and resists exposure to various end. Previous studies of synthetic P189 showed that its reagents (sugars and inhibitors of glycolysis and protein soluble form, when covalently linked to plastic plates synthesis) except heparin. Tumor cell migration is parvia 2-nM linker arms, binds heparin strongly with a tially inhibited by the presence of the peptide. On electron dissociation constant (K d ) of 14 pmol. It also mediates photomicrographs the peptide is seen in close apposition to cell membranes. Heparin sensitivity of the cell binding heparin-sensitive cell binding through its arginine (R)
indicates that cell surface glycosaminoglycans are inrich motif, RRXRRX. Variants that also contain this volved. The aggregated peptide binds heparin in a saturamotif bind cells in a comparable manner. Thus, heparin ble manner with a dissociation constant, K d , of 306 pmol.
binding is most likely charge dependent (ionic) for the Cell binding/clustering studies using peptide variants of soluble form of P189. In previous studies the peptides P189, which have substitutions in either the charged and/ or nonpolar residues, show that the specific sequence of were maintained in a specific orientation by linking them P189 optimizes heparin-sensitive cell aggregation. © 1997 to plastic plates at their carboxyl ends. The RRXRRX