Variabilin, a novel RGD-containing antagonist of glycoprotein IIb-IIIa and platelet aggregation inhibitor from the hard tick Dermacentor variabilis
| Autor: | X, Wang, L B, Coons, D B, Taylor, S E, Stevens, T K, Gartner |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Dose-Response Relationship
Drug Molecular Sequence Data Proteins Platelet Glycoprotein GPIIb-IIIa Complex Mass Spectrometry Salivary Glands Molecular Weight Cell Adhesion Animals Humans Amino Acid Sequence Oligopeptides Sequence Analysis Chromatography High Pressure Liquid Platelet Aggregation Inhibitors Dermacentor |
| Zdroj: | The Journal of biological chemistry. 271(30) |
| ISSN: | 0021-9258 |
| Popis: | A novel inhibitor of human platelet aggregation, named variabilin, was isolated from salivary glands of the hard tick Dermacentor variabilis using a combination of gel filtration and high pressure liquid chromatography. Variabilin was a potent antagonist of the fibrinogen receptor glycoprotein IIb-IIIa (GPIIb-IIIa; alphaIIbbeta3) and the vitronectin receptor alphavbeta3. Amino acid sequence analysis by Edman degradation revealed that it has 47 residues, with a molecular weight of 4968.5. Like many other naturally occurring antagonists of GPIIb-IIIa, variabilin contains the RGD (Arg-Gly-Asp) motif. However, unlike the RGD-containing antagonists of GPIIb-IIIa, the RGD sequence of variabilin is not positioned in a loop bracketed by cysteine residues. It has little sequence homology to the other known naturally occurring antagonists of GPIIb-IIIa, including the disintegrins from snakes, decorsin and ornatin from leeches, and disagregin from soft ticks. Variabilin is the first RGD-containing antagonist isolated from ticks. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|