PMID- 10512730
OWN - NLM
STAT- MEDLINE
DCOM- 19991123
LR  - 20131121
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 263
IP  - 3
DP  - 1999 Oct 5
TI  - Sulfation of iodothyronines by recombinant human liver steroid sulfotransferases.
PG  - 632-9
AB  - Sulfation is an important pathway in the metabolism of thyroid hormones. Sulfated
      iodothyronines are elevated in nonthyroidal illnesses and in the normal human
      fetal circulation. We assayed and characterized COS-1 cell expressed recombinant 
      human liver dehydroepiandrosterone sulfotransferase (DHEA ST or SULT2A1) and
      estrogen sulfotransferase (EST or SULT1E1) activities for the first time with
      triiodothyronine (T(3)) as the substrate. Several biochemical properties that
      included apparent K(m) values, thermal stabilities, and responses to the
      inhibitors 2, 6-dichloro-4-nitrophenol and NaCl were tested. SULT2A1, a member of
      the hydroxysteroid sulfotransferase family, used 3,3'-T(2) more readily than T(3)
      and 3,5-T(2) as substrates, but had the lowest apparent K(m) value for T(3) of
      any reported human SULT. SULT1E1, a member of the phenol sulfotransferase family,
      used 3,3'-T(2) and rT(3) more readily than T(3), and also displayed the greatest 
      specificity for T(4) among human SULTs. SULT2A1 may contribute more to
      iodothyronine sulfation than previously suspected. Potential roles of both
      steroid sulfotransferases in the enhanced sulfation of nonthyroidal illnesses and
      fetal development invite further investigation.
CI  - Copyright 1999 Academic Press.
FAU - Li, X
AU  - Li X
AD  - Creighton University School of Medicine, Omaha, Nebraska 68105, USA.
FAU - Anderson, R J
AU  - Anderson RJ
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (Recombinant Proteins)
RN  - 0 (Thyronines)
RN  - EC 2.8.2.- (Sulfotransferases)
RN  - EC 2.8.2.- (dehydroepiandrosterone sulfotransferase)
RN  - EC 2.8.2.1 (Arylsulfotransferase)
RN  - EC 2.8.2.4 (estrone sulfotransferase)
RN  - Q51BO43MG4 (Thyroxine)
SB  - IM
MH  - Animals
MH  - Arylsulfotransferase/metabolism
MH  - COS Cells
MH  - Humans
MH  - Kinetics
MH  - Recombinant Proteins/*metabolism
MH  - Substrate Specificity
MH  - Sulfotransferases/*metabolism
MH  - Thermodynamics
MH  - Thyronines/*metabolism
MH  - Thyroxine/metabolism
MH  - Transfection
EDAT- 1999/10/08 00:00
MHDA- 1999/10/08 00:01
CRDT- 1999/10/08 00:00
PHST- 1999/10/08 00:00 [pubmed]
PHST- 1999/10/08 00:01 [medline]
PHST- 1999/10/08 00:00 [entrez]
AID - 10.1006/bbrc.1999.1419 [doi]
AID - S0006-291X(99)91419-5 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Oct 5;263(3):632-9. doi: 10.1006/bbrc.1999.1419.