A synthetic peptide derived from the sequence of a type I collagen receptor inhibits type I collagen-mediated platelet aggregation.
نویسندگان
چکیده
A synthetic peptide-1, an 18 amino acid residue peptide derived from a hydrophilic domain of a cloned platelet type I collagen receptor, was used to study the role of the receptor on types I and III collagen-induced platelet aggregation and the release of ATP. The peptide inhibits the type I, but not the type III, collagen-induced platelet aggregation and the release of ATP in a dose-dependent manner. The [125I]peptide-1 specifically binds to type I collagen-coated microtiter wells in a dose-dependent manner (with Kd = 10 nM). The binding of [125I]peptide-1 can be inhibited by an excess of unlabeled peptide-1 suggesting that the binding is specific. The labeled peptide-1 does not bind to type III collagen-coated microtiter wells. Results from an enzyme-linked immunosorbent assay show that the peptide reacts with the poly- and monoclonal antibodies raised against the purified platelet type I collagen receptor (Mr 65 kD). The peptide also inhibits the adhesion of platelets on type I collagen matrix and rabbit aortic segments in a dose-dependent manner. These results suggest that the reactive site of the platelet receptor for type I collagen resides in this portion of the molecule.
منابع مشابه
Cloning, characterization, and functional studies of a nonintegrin platelet receptor for type I collagen.
A cDNA (1.6 kb) encoding a platelet protein receptor that binds type I collagen has been isolated from a human bone marrow cDNA library by using a degenerate oligonucleotide probe derived from the amino acid sequence of a CNBr fragment of the purified receptor. Computer search revealed that this cDNA represents the coding sequence of a unique protein. Using the prokaryotic expression system pKK...
متن کاملPromotion of human platelet adhesion and aggregation by a synthetic, triple-helical "mini-collagen".
Platelet activation and aggregation by fibrillar collagens are based on substrate primary, secondary, tertiary, and quaternary structure. Although several peptides incorporating sequences from the triple-helical domains of types I and III collagen inhibit collagen-mediated platelet aggregation, none independently promote platelet activation and aggregation. It is believed that the absence of th...
متن کاملA study of the kinds of placental collegens from Iranian women to determine the standard rate of placental collagen
Background: Alteration in polymorphism of tissue collagens has been reported in association with some genetic and metabolic disorders. These alterations can be estimated quantitatively by measuring alpha-chain monomers derived from the polymeric form of collagens following treatment with sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). We studied the rate of placental colla...
متن کاملCloning, characterization, and functional studies of a 47-kDa platelet receptor for type III collagen.
A 1.2-kb cDNA fragment encoding a platelet 47-kDa protein has been isolated from a human bone marrow cDNA library by using a degenerate oligonucleotide of the sequenced amino terminus of the purified platelet protein with a poly(dT)(12).(dG) by polymerase chain reaction. A computer search revealed that the cDNA represents the coding sequence of a protein with a fragmentary homology to several p...
متن کاملCEACAM1 negatively regulates platelet-collagen interactions and thrombus growth in vitro and in vivo.
Carcinoembryonic antigen cell adhesion molecule-1 (CEACAM1) is a surface glycoprotein expressed on various blood cells, epithelial cells, and vascular cells. CEACAM1 possesses adhesive and signaling properties mediated by its intrinsic immunoreceptor tyrosine-based inhibitory motifs that recruit SHP-1 protein-tyrosine phosphatase. In this study, we demonstrate that CEACAM1 is expressed on the s...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of clinical investigation
دوره 100 8 شماره
صفحات -
تاریخ انتشار 1997