Showing papers by "Michael D. Pierschbacher published in 1990"

Hydrophobic attachment site for adhesion peptides

Abstract: The invention provides a method of attaching peptides containing a RGD adhesion peptides, to a solid surface through a hydrophobic domain, and peptides so attached. The hydrophobic domain can contain either hydrophobic amino acids, such as leucine, valine, isoleucine or phenylalanine, or fatty acids, such as, for example, myristic acid, palmitic acid, arachidic acid or other fatty acids. Additionally, spacers, such as amino acids, between the hydrophobic domain and the biologically active domain can improve the presentation of the biologically active site. Specific peptides of the invention include GRGDSPASSKG4SRL6RNH2; GRGDSPASSKS3RL6RNH2; AND GRGDSPASSKSSKRL6RNH2. Coupled to a solid surface, such peptides can be used to detect the presence of a ligand complementary to the biologically active site.

Isolation and use of receptors binding to a peptide column

Abstract: A method of isolating cell surface receptors utilizing a short peptide sequence bound to an affinity column. Cell surface receptors which bind selectively to the short peptide and which are specific to various adhesion proteins may be isolated therewith from various cell preparations. These receptors, whose functional integrity has been maintained by the presence of the peptide ligand, are incorporated into liposomes and used to deliver specific compounds inside the liposomes to select tissues containing the specific adhesion proteins.

Agent containing a synthetic peptide for inhibiting cell movement

Abstract: PURPOSE: To prepare a pharmaceutical composition, comprising a synthetic peptide having a specific amino acid sequence as an active ingredient and useful for inhibiting the invasion of cells through an extracellular membrane. CONSTITUTION: This pharmaceutical composition comprises a synthetic peptide containing Arg-Gly-Asp, e.g. a synthetic peptide represented by the formula (R1 is one or more amino acids, other chemical molecular parts or H; X is Thr or other amino acids; R2 is one or more amino acids or OH, with the proviso that all of the R1 , X and R2 do not inhibit the membrane invasion inhibiting ability of the peptide and the peptide is not same as a natural peptide) as an active ingredient. The length of the peptide is restricted by the solubility thereof and the number of the amino acids in the peptide is preferably <30, especially preferably 5-8. The peptide can be stabilized by forming a conjugate with a saccharide polymer, preferably an organic polymer such as dextran.

Fibronectin Receptor Expression on Thymocytes

Abstract: Entrance of precursor T cells into the thymus and their subsequent exit into the circulation are prerequisite events for development of mature T-lymphocyte characteristics (1). Thymic epithelial cells may play an integral role in thymocyte differentiation, both through direct contact and by secretion of thymic hormones (2). Thus, positional and developmental cues for maturing thymocytes may come from neighboring cell surfaces (3) or from the extracellular matrix surrounding these cells. However, the full complement of molecules involved in this differentiation process has not been identified. The influence of cell adhesion on cell growth and differentiation is well established for many cell systems (4–10) yet the interaction of lymphocytes with adhesive extracellular matrix proteins, with a few exceptions, has been largely unexplored (11–16).