Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.3.1.108 (TAT)
 2,389 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Activation of human normal serum with tetanus/antitetanus immune complexes (TAT-IC) resulted in increased binding of 125I-labeled interleukin-1 beta (IL-1 beta) to serum factors, as opposed to untreated serum. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by autoradiography showed labeling of two large molecular mass factors of an apparent molecular weight (Mr) of 200,000 and 400,000, respectively. These complexes could be dissociated by reduction. No complexes were formed when reducing compounds were added to serum-TAT-IC-125I-IL-1 beta mixtures. Complex formation was largely prevented by alkylating compounds. Molecular sieve chromatography of TAT-IC-activated serum confirmed that 125I-IL-1 beta became bound to high Mr serum proteins. Fractions containing high molecular 125I-IL-1 serum protein complexes partially retained IL-1-like activity since they induced proliferation of an IL-1-dependent murine T helper (D10G4) cell lineage. The 125I-IL-1 beta binding factors could be immunoprecipitated from TAT-IC-activated serum 125I-IL-1 beta solutions by antisera to alpha 2-macroglobulin (alpha 2M) or to the third complement component (C3). SDS-PAGE of the immunoprecipitates showed radioactive bands corresponding to the expected Mr resulting from complex formation between 125I-IL-1 beta and these two proteins. Treatment of purified plasma alpha 2M and C3 with trypsin or activation with methylamine, which causes cleavage of the internal thiol ester and the appearance of free thiol groups in these proteins, mediated binding of 125I-IL-1 beta to alpha 2M and C3b. The results suggest that cleavage of the internal thiol ester in C3 and alpha 2M makes these plasma proteins susceptible to binding of 125I-IL-1 beta and that free thiol groups do play a role in the formation of 125I-IL-1 beta plasma protein complexes. Activated C3 and alpha 2M may function as IL-1 beta carrier proteins in biologic fluids, in addition to their other physiologic roles.
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PMID:Binding of recombinant interleukin-1 beta to the third complement component and alpha 2-macroglobulin after activation of serum by immune complexes. 169 30

Copolymers composed of polar and nonpolar blocks, when blended with a base polymer in low concentrations, migrate to the base polymer surface during and after fabrication. Migration of these surface modifying additives (SMAs) dramatically changes the outermost surface molecular layers that comprise the region that determines biocompatibility. The blood compatibility of cardiopulmonary bypass and hemodialysis components have been improved by using SMA blended polymers or SMA coated surfaces. The particular SMAs used were a series of triblock copolymers with a general formulation of polycaprolactone-polydimethylsiloxane-polycaprolactone. X-ray fluorescence (XRF), fourier transform infrared (FTIR), refractive increments (RI), and gel permeation chromatography (GPC) were used to characterize the molecular weight of SMA and the bulk concentration of SMA after blending. Electron spectroscopy for chemical analysis (ESCA) proved that the surface of blended polymers was highly saturated with SMA. Results of in vitro experiments with human blood demonstrated that SMA blended polymers delay contact activation (kallikrein-like activity), reduce coagulation activity (thrombin-antithrombin [TAT] generation), and do not adversely affect complement activation (terminal complement complex [TCC] generation) or mononuclear cells activation (IL-1 beta production). Ex vivo canine AV shunt studies showed improvement of platelet compatibility of SMA blended polymers. Reduction of cellular and protein system activation by using components fabricated with SMA blood contacting surfaces can potentially result in reduced morbidity associated with extracorporeal circulation.
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PMID:Surface modifying additives for improved device-blood compatibility. 855 89