PMID- 10514471
OWN - NLM
STAT- MEDLINE
DCOM- 19991119
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 42
DP  - 1999 Oct 15
TI  - Characterization of human and murine PMP20 peroxisomal proteins that exhibit
      antioxidant activity in vitro.
PG  - 29897-904
AB  - We have isolated the cDNAs encoding human and mouse homologues of a yeast
      protein, termed peroxisomal membrane protein 20 (PMP20). Comparison of the amino 
      acid sequences of human (HsPMP20) and mouse (MmPMP20) PMP20 proteins revealed a
      high degree of identity (93%), whereas resemblance to the yeast Candida boidinii 
      PMP20A and PMP20B (CbPMP20A and CbPMP20B) was less (30% identity). Both HsPMP20
      and MmPMP20 lack transmembrane regions, as do CbPMP20A and CbPMP20B. HsPMP20 mRNA
      expression was low in human fetal tissues, especially in the brain. In adult
      tissues, HsPMP20 mRNA was expressed in the majority of tissues tested. HsPMP20
      and MmPMP20 contained the C-terminal tripeptide sequence Ser-Gln-Leu (SQL), which
      is similar to the peroxisomal targeting signal 1 utilized for protein import into
      peroxisomes. HsPMP20 bound directly to the human peroxisomal targeting signal 1
      receptor, HsPEX5. Mutagenesis analysis showed that the C-terminal tripeptide
      sequence, SQL, of HsPMP20 is necessary for its binding to HsPEX5. Subcellular
      fractionation of HeLa cells, expressing epitope-tagged PMP20, revealed that
      HsPMP20 is localized in the cytoplasm and in a particulate fraction containing
      peroxisomes. Double-staining immunofluorescence studies showed colocalization of 
      HsPMP20 and thiolase, a bona fide peroxisomal protein. The amino acid sequence
      alignment of HsPMP20, MmPMP20, CbPMP20A, and CbPMP20B displayed high similarity
      to thiol-specific antioxidant proteins. HsPMP20 exerted an inhibitory effect on
      the inactivation of glutamine synthetase in the thiol metal-catalyzed oxidation
      system but not in the nonthiol metal-catalyzed oxidation system, suggesting that 
      HsPMP20 possesses thiol-specific antioxidant activity. In addition, HsPMP20
      removed hydrogen peroxide by its thiol-peroxidase activity. These results
      indicate that HsPMP20 is imported into the peroxisomal matrix via PEX5p and may
      work to protect peroxisomal proteins against oxidative stress. Because some
      portion of PMP20 might also be present in the cytosol, HsPMP20 may also have a
      protective effect in the cytoplasm.
FAU - Yamashita, H
AU  - Yamashita H
AD  - Division of Experimental Medicine, Beth Israel Deaconess Medical Center, Harvard 
      Medical School, Boston, Massachusetts 02215, USA.
FAU - Avraham, S
AU  - Avraham S
FAU - Jiang, S
AU  - Jiang S
FAU - London, R
AU  - London R
FAU - Van Veldhoven, P P
AU  - Van Veldhoven PP
FAU - Subramani, S
AU  - Subramani S
FAU - Rogers, R A
AU  - Rogers RA
FAU - Avraham, H
AU  - Avraham H
LA  - eng
SI  - GENBANK/AF124993
SI  - GENBANK/AF124994
GR  - CA76226/CA/NCI NIH HHS/United States
GR  - HL51456/HL/NHLBI NIH HHS/United States
GR  - HL55445/HL/NHLBI 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 (Antioxidants)
RN  - 0 (DNA, Complementary)
RN  - 0 (Membrane Proteins)
RN  - 0 (Peroxisome-Targeting Signal 1 Receptor)
RN  - 0 (Receptors, Cytoplasmic and Nuclear)
RN  - 0 (Sulfhydryl Compounds)
RN  - EC 1.11.1.- (Peroxidases)
RN  - EC 1.11.1.15 (PRDX5 protein, human)
RN  - EC 1.11.1.15 (Peroxiredoxins)
RN  - EC 1.11.1.15 (Prdx5 protein, mouse)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antioxidants/*metabolism
MH  - Base Sequence
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Humans
MH  - Membrane Proteins/*genetics/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - *Peroxidases
MH  - Peroxiredoxins
MH  - Peroxisome-Targeting Signal 1 Receptor
MH  - Peroxisomes/*metabolism
MH  - Protein Binding
MH  - Receptors, Cytoplasmic and Nuclear/metabolism
MH  - Saccharomyces cerevisiae/genetics
MH  - Sequence Homology, Amino Acid
MH  - Subcellular Fractions/metabolism
MH  - Sulfhydryl Compounds/metabolism
EDAT- 1999/10/09 00:00
MHDA- 1999/10/09 00:01
CRDT- 1999/10/09 00:00
PHST- 1999/10/09 00:00 [pubmed]
PHST- 1999/10/09 00:01 [medline]
PHST- 1999/10/09 00:00 [entrez]
AID - 10.1074/jbc.274.42.29897 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Oct 15;274(42):29897-904. doi: 10.1074/jbc.274.42.29897.