[Thymosin alpha(1)--an endogenous modulator of alpha-thrombin recognition site].
Thymosin alpha 1-inhibited fibrinogen clotting activity of alpha-thrombin, but not amidolysis of H-D-Phe-Pip-Arg-pNA. Modulation of thrombin interaction with rat peritoneal mast cells (RPMC) by suppressors of additional recognition binding site (thymosin and heparin) was studied. Thrombin-induced pHi changes of RPMC were controlled with pH-sensitive fluorescent dye, BCECF. Thrombin caused a biphasic changes in pHi: rapid cell acidification (0.02) followed by slow alkalinization (0.06 above baseline for 18 min). Thymosin suppressed thrombin-induced pHi increase above resting level. Similar changes in pHi were observed after modification of additional recognition binding site by heparin. Beta/gamma-thrombin with disrupted additional binding site was shown to induce only a decrease of pHi. It is concluded that thymosin alpha 1 is endogenous modulator of alpha-thrombin activity.
Dugina
T N
TN
Strukova
S M
SM
Khlgatian
S V
SV
Ashmarin
I P
IP
D000818:Animals; D001665:Binding Sites; D005456:Fluorescent Dyes; D006493:Heparin / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008407:Mast Cells / Q000378:metabolism; D051381:Rats; D013053:Spectrophotometry; D013917:Thrombin / Q000378:metabolism / Q000502:physiology*; D000077596:Thymalfasin; D013947:Thymosin / Q000031:analogs & derivatives* / Q000502:physiology
D005456:Fluorescent Dyes; D013947:Thymosin; D006493:Heparin; D013917:Thrombin; D000077596:Thymalfasin
Timozin al'fa1--éndogennyĭ moduliator tsentra uznavaniia alfa-trombina.