PMID- 9712828
OWN - NLM
STAT- MEDLINE
DCOM- 19980924
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 273
IP  - 35
DP  - 1998 Aug 28
TI  - Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I).
PG  - 22173-6
AB  - Arsenic is a potent toxin and carcinogen. In prokaryotes, arsenic detoxification 
      is accomplished by chromosomal and plasmid-borne operon-encoded efflux systems. 
      We have previously reported the cloning of hASNA-I, a human homologue of arsA 
      encoding the ATPase component of the Escherichia coli arsenite transporter. 
      Purified glutathione S-transferase (GST)-hASNA-I fusion protein was biochemically 
      characterized, and its properties were compared with those of ArsA. The 
      GST-hASNA-I exhibited a basal level of ATPase activity of 18.5 +/- 8 nmol/min/mg 
      in the absence of arsenite. Arsenite produced a 1.6 +/- 0.1-fold stimulation of 
      activity (p = 0. 0044), which was related to an increase in Vmax; antimonite did 
      not stimulate activity. Two lines of evidence suggest that an oligomer is the 
      most likely native form of hASNA-I. First, lysates of human embryo kidney 293 
      cells overproducing recombinant hASNA-I produced a single monomeric 37-kDa band 
      on SDS-polyacrylamide gel electrophoresis (PAGE) and two distinct species when 
      analyzed using nondenaturing PAGE. Second, chemical cross-linking of the 63-kDa 
      GST-hASNA-I resulted in the formation of dimeric and tetrameric protein forms. 
      The results indicate that hASNA-I is a distinct human arsenite-stimulated ATPase 
      belonging to the same superfamily of ATPases represented by the E. coli ArsA 
      protein.
FAU - Kurdi-Haidar, B
AU  - Kurdi-Haidar B
AD  - Department of Medicine and the University of California, San Diego Cancer Center, 
      University of California, San Diego, La Jolla, California 92093-0058, USA. 
      bhaidar@ucsd.edu
FAU - Heath, D
AU  - Heath D
FAU - Aebi, S
AU  - Aebi S
FAU - Howell, S B
AU  - Howell SB
LA  - eng
GR  - CA69004/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Arsenites)
RN  - 0 (Cross-Linking Reagents)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 2.5.1.18 (Glutathione Transferase)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - N5509X556J (arsenite)
SB  - IM
MH  - Adenosine Triphosphatases/*metabolism
MH  - Adenosine Triphosphate/metabolism
MH  - Arsenites/*pharmacology
MH  - Blotting, Western
MH  - Cell Line
MH  - Cross-Linking Reagents
MH  - Enzyme Activation
MH  - Glutathione Transferase/chemistry
MH  - Humans
MH  - Protein Binding
MH  - Recombinant Fusion Proteins/chemistry/metabolism
EDAT- 1998/08/26 00:00
MHDA- 1998/08/26 00:01
CRDT- 1998/08/26 00:00
PHST- 1998/08/26 00:00 [pubmed]
PHST- 1998/08/26 00:01 [medline]
PHST- 1998/08/26 00:00 [entrez]
AID - S0021-9258(18)48705-4 [pii]
AID - 10.1074/jbc.273.35.22173 [doi]
PST - ppublish
SO  - J Biol Chem. 1998 Aug 28;273(35):22173-6. doi: 10.1074/jbc.273.35.22173.