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J Biol Chem, Vol. 273, Issue 16, 9886-9893, April 17, 1998
From the Department of Biochemistry, Michigan State University,
East Lansing, Michigan 48824 and the Prostaglandin endoperoxide H synthases-1 and -2 (PGHS-1 and -2) are the major targets of nonsteroidal anti-inflammatory
drugs like aspirin and ibuprofen. These enzymes catalyze the committed step in the formation of prostanoids from arachidonic acid. Although PGHS-1 and -2 are similar biochemically, a number of studies suggest that PGHS-1 and PGHS-2 function independently to form prostanoids that
subserve different cellular functions. We have hypothesized that these
isozymes may reside, at least in part, in different subcellular
compartments and that their compartmentation may affect their access to
arachidonic acid and serve to separate the functions of the enzymes. To
obtain high resolution data on the subcellular locations of PGHS-1 and
-2, we employed immunoelectron microscopy with multiple antibodies
specific to each isozyme. Both PGHS-1 and -2 were found on the lumenal
surfaces of the endoplasmic reticulum (ER) and nuclear envelope of
human monocytes, murine NIH 3T3 cells, and human umbilical vein
endothelial cells. Within the nuclear envelope, PGHS-1 and -2 were
present on both the inner and outer nuclear membranes and in similar
proportions. Western blotting data showed a similar distribution of
PGHS-1 and -2 in subcellular fractions, and product analysis using
isozyme-specific inhibitors suggested that both enzymes generate the
same products in NIH 3T3 cells. Thus, we are unable to attribute the
independent functioning of PGHS-1 and PGHS-2 to differences in their
subcellular locations. Instead, the independent operation of these
isozymes may be attributable to subtle kinetic differences
(e.g. negative allosteric regulation of PGHS-1 at low
concentrations of arachidonate (500-1000 nM)). A further
conclusion of importance from a cell biological perspective is that
membrane proteins such as PGHS-1 and -2, which are located on the
lumenal surface of the ER, are able to diffuse freely among the ER and
the inner and outer membranes of the nuclear envelope.
Subcellular Localization of Prostaglandin Endoperoxide H
Synthases-1 and -2 by Immunoelectron Microscopy
,, and Department of
Biochemical and Molecular Pathology, Merck Research Laboratories,
Rahway, New Jersey 07065
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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M. Murakami, T. Kambe, S. Shimbara, and I. Kudo Functional Coupling Between Various Phospholipase A2s and Cyclooxygenases in Immediate and Delayed Prostanoid Biosynthetic Pathways J. Biol. Chem., January 29, 1999; 274(5): 3103 - 3115. [Abstract] [Full Text] [PDF]
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K. Tada, M. Murakami, T. Kambe, and I. Kudo Induction of Cyclooxygenase-2 by Secretory Phospholipases A2 in Nerve Growth Factor-Stimulated Rat Serosal Mast Cells Is Facilitated by Interaction with Fibroblasts and Mediated by a Mechanism Independent of Their Enzymatic Functions J. Immunol., November 1, 1998; 161(9): 5008 - 5015. [Abstract] [Full Text] [PDF]
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H. Sakamoto, H. Imai, and Y. Nakagawa Involvement of Phospholipid Hydroperoxide Glutathione Peroxidase in the Modulation of Prostaglandin D2 Synthesis J. Biol. Chem., December 15, 2000; 275(51): 40028 - 40035. [Abstract] [Full Text] [PDF]
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T. Tanioka, Y. Nakatani, N. Semmyo, M. Murakami, and I. Kudo Molecular Identification of Cytosolic Prostaglandin E2 Synthase That Is Functionally Coupled with Cyclooxygenase-1 in Immediate Prostaglandin E2 Biosynthesis J. Biol. Chem., October 13, 2000; 275(42): 32775 - 32782. [Abstract] [Full Text] [PDF]
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M. Murakami, R. S. Koduri, A. Enomoto, S. Shimbara, M. Seki, K. Yoshihara, A. Singer, E. Valentin, F. Ghomashchi, G. Lambeau, et al. Distinct Arachidonate-releasing Functions of Mammalian Secreted Phospholipase A2s in Human Embryonic Kidney 293 and Rat Mastocytoma RBL-2H3 Cells through Heparan Sulfate Shuttling and External Plasma Membrane Mechanisms J. Biol. Chem., March 23, 2001; 276(13): 10083 - 10096. [Abstract] [Full Text] [PDF]
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R. Koljak, I. Jarving, R. Kurg, W. E. Boeglin, K. Varvas, K. Valmsen, M. Ustav, A. R. Brash, and N. Samel The Basis of Prostaglandin Synthesis in Coral. MOLECULAR CLONING AND EXPRESSION OF A CYCLOOXYGENASE FROM THE ARCTIC SOFT CORAL GERSEMIA FRUTICOSA J. Biol. Chem., March 2, 2001; 276(10): 7033 - 7040. [Abstract] [Full Text] [PDF]
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N. Ueno, M. Murakami, T. Tanioka, K. Fujimori, T. Tanabe, Y. Urade, and I. Kudo Coupling between Cyclooxygenase, Terminal Prostanoid Synthase, and Phospholipase A2 J. Biol. Chem., September 7, 2001; 276(37): 34918 - 34927. [Abstract] [Full Text] [PDF]
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C. Bandeira-Melo, M. Phoofolo, and P. F. Weller Extranuclear Lipid Bodies, Elicited by CCR3-mediated Signaling Pathways, Are the Sites of Chemokine-enhanced Leukotriene C4 Production in Eosinophils and Basophils J. Biol. Chem., June 15, 2001; 276(25): 22779 - 22787. [Abstract] [Full Text] [PDF]
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J.-Y. Liou, W.-G. Deng, D. W. Gilroy, S.-K. Shyue, and K. K. Wu Colocalization and Interaction of Cyclooxygenase-2 with Caveolin-1 in Human Fibroblasts J. Biol. Chem., September 7, 2001; 276(37): 34975 - 34982. [Abstract] [Full Text] [PDF]
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T. Yang, Y. Huang, L. E. Heasley, T. Berl, J. B. Schnermann, and J. P. Briggs MAPK Mediation of Hypertonicity-stimulated Cyclooxygenase-2 Expression in Renal Medullary Collecting Duct Cells J. Biol. Chem., July 21, 2000; 275(30): 23281 - 23286. [Abstract] [Full Text] [PDF]
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F. Gobeil Jr, I. Dumont, A. M. Marrache, A. Vazquez-Tello, S. G. Bernier, D. Abran, X. Hou, M. H. Beauchamp, C. Quiniou, A. Bouayad, et al. Regulation of eNOS Expression in Brain Endothelial Cells by Perinuclear EP3 Receptors Circ. Res., April 5, 2002; 90(6): 682 - 689. [Abstract] [Full Text] [PDF]
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