Thyroxine binding to members and non-members of the serine protease inhibitor family

被引:15
作者
Benvenga, S [1 ]
Lapa, D [1 ]
Trimarchi, F [1 ]
机构
[1] Univ Messina, Sch Med, Sect Endocrinol, Dept Clin & Expt Med & Pharmacol, Messina, Italy
关键词
T-4; lipoproteins; albumin; transthyretin; TBG; serine protease inhibitors (SERPINs); CBG; SHBG; alpha(1)-acid glycoprotein;
D O I
10.1007/BF03343958
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Partition of T-4 to plasma proteins is classically attributed only to TBGC approximate to70%), transthyretin (approximate to15%) and albumin (approximate to10%), based on zone electrophoresis. Since TBG migration spans the alpha1 and alpha2 regions, and since HDL, which have alpha1 migration, transport approximate to4% of circulating T-4, other alpha-globulins could bind T-4 and "contaminate" the TBG area. Hence, we determined the association of [I-125]T-4 to TBG and, for comparison, to transthyretin and albumin. Sera from 50 normolipidemic individuals were equilibrated with [I-125] T4 and analyzed by both zone electrophoresis and radioimmunoprecipitation with specific antisera. Transthyretin-T-4 or albumin-T-4 bindings as assessed by the two methods agreed, while TBG-T-4 did not, because other alpha-globulins carrying T-4 with low affinity co-migrated with TBG. Some, but not all, of these alpha-globulins belong to the same superfamily of TBG and also bind steroid hormones. (C) 2002, Editrice Kurtis.
引用
收藏
页码:32 / 38
页数:7
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