title: [Effect of serine proteinases on the intracellular dynamics of membrane lipids and aggregation of human thrombocytes].
abstract: Room temperature tryptophan phosphorescence (RTTP) of human platelets in suspension was studied. The spectral and kinetic parameters of RTTP of thrombocytes were determined. By using the RTTP, the effect of serine proteases: thrombin, trypsin, and alpha-chymotrypsin at low concentrations (0-50 micrograms/ml) on the slow internal dynamics of membrane proteins was studied. It was shown that short-term incubation of platelets with proteases induces changes in the internal dynamics of membrane proteins in situ, and the magnitude of this effect correlates well with the extent of platelet aggregation. The functional role of the changes in the internal dynamics of membrane proteins and their relationship with intracellular signal transduction were discussed.
authors.affiliation: Institute of Photobiology, National Academy of Sciences of Belarus, Akademicheskaya ul. 27, Minsk, 220072 Belarus.
authors.forename: V M
authors.initials: VM
authors.lastname: Mazhul'
authors.forename: T S
authors.initials: TS
authors.lastname: Chernovets
authors.forename: E M
authors.initials: EM
authors.lastname: Zaĭtseva
authors.forename: D G
authors.initials: DG
authors.lastname: Shcherbin
mesh_terms: D001792:Blood Platelets / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism; D002918:Chymotrypsin / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D006801:Humans; D066298:In Vitro Techniques; D049449:Luminescence; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D010974:Platelet Aggregation / Q000187:drug effects*; D012697:Serine Endopeptidases / Q000494:pharmacology*; D013917:Thrombin / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology; D014364:Tryptophan / Q000737:chemistry
chemical_list: D008565:Membrane Proteins; D014364:Tryptophan; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C117608:alpha-chymotrypsin; D014357:Trypsin; D013917:Thrombin