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J Biol Chem, Vol. 273, Issue 5, 2692-2697, January 30, 1998
V) Binding Protein
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From the This is the first report on peptidic inhibitors
of heme oxygenase. Such peptides were originally developed from the
immunomodulatory peptide 2702.75-84 which corresponds to amino acid
residues 75 to 84 of the SangStat Medical Corporation, Menlo Park,
California 94025 and § Department of Biochemistry,
Biophysics and Environmental Medicine, University of Rochester School
of Medicine, Rochester, New York 14642
1-helix of HLA-B2702
(2702.75-84) and has been shown to be immunosuppressive in
vitro and in vivo. In vitro, 2702.75-84 inhibited
cytotoxic T- and natural killer cell- mediated target cell lysis, and
in vivo peptide therapy resulted in prolongation of heart
and skin allograft survival in mice. The peptide was also shown to bind
to heat shock protein 70. However, D-enantiomers of
2702.75-84 and derivatives thereof, while still being
immunosuppressive, did not bind to heat shock protein 70. This study
was designed to identify proteins binding to peptide D2702.75-84(E 
V) (rvnlrialry) consisting of D-amino acids.
Compared with 2702.75-84 (RENLRIALRY), glutamic acid residue 76 (E) was replaced with valine (V). Affinity chromatography using
immobilized D2702.75-84(E V) and mouse and human cell extracts,
resulted in the isolation of heme oxygenase-1 (HO-1). Peptide
D2702.75-84 inhibited HO activity in vitro in a dose
dependent manner. Similar to what has been observed with other
inhibitors of HO, administration of peptide into mice resulted in an
up-regulation of HO-1 mRNA and protein, as well as enzyme activity
in liver, spleen and kidney. Other peptides derived from 2702.75-84
with similar immunomodulatory activity displayed similar effects. In
contrast, inactive derivatives of 2702.75-84 had no effect on HO
activity. Therefore, the immunosuppressive effects of the described
immunomodulatory peptides are similar to those of
cobalt-protoporphyrin, a known up-regulator of HO-1. Our results suggest that HO-1 modulation may be a novel mechanism of
immunomodulation.
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