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Post-translational Modification of Transthyretin in Plasma

1998; Elsevier BV; Volume: 249; Issue: 1 Linguagem: Inglês

10.1006/bbrc.1998.9097

1090-2104

Hisayasu Terazaki, Yukio Ando, Ole B. Suhr, Per‐Ingvar Ohlsson, Konen Obayashi, Taro Yamashita, Shinichi Yoshimatsu, Moritaka Suga, Makoto Uchino, Masayuki Ando,

Blood Coagulation and Thrombosis Mechanisms

To determine the behavior of transthyretin (TTR) in blood circulation, TTR purified from normal subjects’ plasma was injected to rats, and blood and urine were collected time dependently. Although TTR in plasma was proven to be a predominantly cysteine (Cys) conjugated form by electrospray ionization mass spectrometry (ESI-MS) analysis, it was gradually converted into free, 32 Da (dihydroxylation), 80 Da (phosphorylation), and 306 Da (glutathionylation), increased forms in molecular weight of TTR. The plasma levels of TTR were decreased in a time-dependent manner with the half life of 72.4 min. No secretion of TTR into the urine was observed by ESI-MS. In conclusion, this method can be simply performed without loading a radioactive molecule to the targeted protein. It offers a possibility to determine natural protein behaviors in the blood stream.