Abstract:
:Prostacyclin synthase (PGIS) cDNA comprises 1500 nucleotides coding for a 500 amino acid protein. It is a heme protein with spectral characteristics of cytochrome p450 (CYP). It does not possess the typical CYP mono-oxygenase activity but catalyzes the rearrangement of prostaglandin H2 to form PGI2. Analysis of its structure-function by molecular modeling and site-directed mutagenesis reveals a long substrate channel lined by hydrophobic residues. Cys-441 has been identified as the proximal axial ligand of heme. Tyr-430 is nitrated by peroxynitrite which results in reduced PGIS catalytic activity, suggesting that Tyr-430 is located close to the heme pocket. PGIS is constitutively expressed and may be upregulated by cytokines, reproductive hormones, and growth factors. It is physically colocalized with cyclooxygenases and phospholipases, and functionally coupled with these enzymes. PGIS coupling with COX-2 has been shown to play an important role in vascular protection, embryo development and implantation, and cancer growth.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Wu KK,Liou JYdoi
10.1016/j.bbrc.2005.08.021subject
Has Abstractpub_date
2005-12-09 00:00:00pages
45-52issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(05)01710-9journal_volume
338pub_type
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