scholarly journals Differential expression of prostaglandin-H synthase isoenzymes in normal and activated keratinocytes in vivo and in vitro

1995 ◽  
Vol 309 (1) ◽  
pp. 263-269 ◽  
Author(s):  
K Scholz ◽  
G Fürstenberger ◽  
K Müller-Decker ◽  
F Marks
Keyword(s):  
Gradient Centrifugation ◽  
Mouse Skin ◽  
Neonatal Mouse ◽  
Similar Distribution ◽  
Mouse Epidermis ◽  
Epidermal Hyperplasia ◽  
Prostaglandin H Synthase ◽  
Percoll Density Gradient Centrifugation ◽  
Prostaglandin H

Normal mouse epidermis constitutively expresses prostaglandin-H synthase 1 (PGHS-1) but no PGHS-2. Acute inflammation and epidermal hyperplasia, (hyperplastic transformation), as evoked in adult mouse skin in vivo by wounding or by the phorbol ester phorbol 12-myristate 13-acetate (PMA), resulted in a transient induction of PGHS-2 expression while PGHS-1 remained unchanged. Under conditions of a stationary epidermal hyperplasia, as in neonatal mouse epidermis, PGHS-1, but not PGHS-2, expression was observed. Induction of ‘balanced hyperproliferation’ by 4-O-methyl-phorbol 12-myristate 13-acetate (4-O-methyl-PMA) did not lead to PGHS-2 expression. When keratinocytes were isolated from neonatal mouse skin and separated by Percoll density-gradient centrifugation according to their stage of differentiation, PGHS-1 mRNA expression and protein were found to be highest in the differentiated cells compared with those from the proliferative compartment. A similar distribution of PGHS-1 mRNA was found in keratinocytes from adult mice, whereas PGHS-1 protein was equally distributed in all cell types. Contrary to the situation in intact epidermis, PGHS-2 mRNA but no protein was detected in all cell fractions. Established keratinocyte lines constitutively expressed both isoenzymes at different ratios. In the mouse line MSCP5 an almost exclusive expression of PGHS-2 was found, which was further enhanced by PMA treatment. These data indicate that the expression of PGHS-2 in mouse epidermis is specifically related to the emergency reaction of hyperplastic transformation.

Prostaglandin H synthase-2 isozyme induction as emergency response of epidermis in vivo

1995 ◽  
Vol 121 (S1) ◽  
pp. A18-A18
Author(s):  
K. Müller-Decker ◽  
K. Scholz ◽  
F. Marks ◽  
G. Fürstenberger
Keyword(s):  
Emergency Response ◽  
Prostaglandin H Synthase ◽  
Prostaglandin H

Localization of Prostaglandin-H Synthase-1 and -2 in Mouse Skin: Implications for Cutaneous Function

1998 ◽  
Vol 242 (1) ◽  
pp. 84-91 ◽  
Author(s):  
K. Müller-Decker ◽  
K. Scholz ◽  
G. Neufang ◽  
F. Marks ◽  
G. Fürstenberger
Keyword(s):  
Mouse Skin ◽  
Prostaglandin H Synthase ◽  
Prostaglandin H

scholarly journals Differences in myeloperoxidase activity from neutrophilic polymorphonuclear leukocytes of differing density: relationship to selective exocytosis of distinct forms of the enzyme

Blood ◽  
1983 ◽  
Vol 61 (6) ◽  
pp. 1116-1124
Author(s):  
SO Pember ◽  
JM Jr Kinkade
Keyword(s):  
Polymorphonuclear Leukocytes ◽  
Human Peripheral Blood ◽  
Gradient Centrifugation ◽  
Fold Increase ◽  
Myeloperoxidase Activity ◽  
Percoll Density Gradient Centrifugation ◽  
Density Relationship ◽  
Neutrophilic Polymorphonuclear Leukocytes

Elicited murine neutrophilic polymorphonuclear leukocytes (PMN) were fractionated by Percoll density gradient centrifugation into high density (HD) and intermediate density (ID) populations. As described in the accompanying article HD- and ID-PMN appear to represent “resting” and “activated” cell populations, respectively. Consistent with this possibility, histochemical and biochemical evidence suggested that ID- PMN were degranulated compared to HD-PMN. Myeloperoxidase (MPO) in the ID-PMN population showed increased sensitivity to inhibition by 3-amino- 1,2,4-triazole, and HD-PMN exhibited a 2–3-fold increase in chloride and iodide oxidation per unit of MPO activity compared to ID-PMN. When HD-PMN were induced to degranulate in vitro, the remaining cell- associated MPO displayed enzymatic properties characteristic of the activity associated with ID-PMN. The mechanism of this phenomenon was also investigated in vitro using purified human peripheral blood PMN and the synthetic chemotactic peptide N-formyl-methionyl-leucyl- phenylalanine. Differences in cell-associated MPO activity were shown to be related to selective exocytosis of enzymatically and chromatographically distinct forms of the enzyme. These data indicate that, in addition to the well known selective exocytosis of specific and azurophilic granules induced by various agents, selectivity may also occur at the level of enzymatically distinct forms of a particular granule enzyme. Moreover, our observations provide further evidence that density differences may be utilized to fractionate and study the generation of functionally distinct subpopulations of PMN that arise in vivo as well as in vitro following exposure to various stimuli.

Localization of prostaglandin H synthase type 2 protein and mRNA in term human fetal membranes and decidua

1996 ◽  
Vol 150 (3) ◽  
pp. 497-503 ◽  
Author(s):  
W Gibb ◽  
M Sun
Keyword(s):  
Epithelial Cells ◽  
Blood Vessels ◽  
Fetal Membranes ◽  
Similar Distribution ◽  
Prostaglandin H Synthase ◽  
Membrane Rupture ◽  
Chorion Laeve ◽  
Prostaglandin H ◽  
Amnion Epithelial Cells

Abstract Prostaglandin (PG) production by human fetal membranes (amnion and chorion laeve) may be important in the onset and progression of labour, cervical ripening and membrane rupture. Prostaglandin H synthase (PGHS) is a key enzyme in PG formation and has two isoforms, a constitutive form (PGHS-1) and an inducible form (PGHS-2). The present study examined the cellular distribution of the PGHS-2 enzyme and PGHS-2 mRNA in term human fetal membranes and decidua prior to and following labour, using immunohistochemistry and in situ hybridization with an 35S-labelled oligonucleotide probe. The PGHS-2 protein was found to be localized in amnion epithelial cells and chorion laeve trophoblast, but was absent or at low levels in the decidual stroma in most tissues, although cells surrounding some of the blood vessels in the decidua did express PGHS-2. In situ hybridization demonstrated that PGHS-2 mRNA had a similar distribution and was localized to amnion epithelial cells, cells in the amnion-chorion mesenchyme, chorion laeve trophoblast and, occasionally, to cells surrounding blood vessels in the decidua. Of particular note was the high mRNA expression in some cells and low expression in other cells, particularly in the chorion, and the low level of PGHS-2 mRNA in decidua. There was no observable difference in the cellular localization of PGHS-2 protein or PGHS-2 mRNA in tissues obtained prior to and following labour. The studies indicate that, at term, the inducible form of PGHS, PGHS-2, is expressed at a high level in fetal tissues in a number of different cell types rather than in the maternal decidua. Journal of Endocrinology (1996) 150, 497–503

scholarly journals The in Vivo Control of Prostaglandin H Synthase-2 Messenger Ribonucleic Acid Expression in the Human Amnion at Parturition

2002 ◽  
Vol 87 (6) ◽  
pp. 2816-2823 ◽  
Author(s):  
Renée F. Johnson ◽  
Carolyn M. Mitchell ◽  
Warwick B. Giles ◽  
William A. Walters ◽  
Tamas Zakar
Keyword(s):  
Ribonucleic Acid ◽  
Prostaglandin H Synthase ◽  
Human Amnion ◽  
Messenger Ribonucleic Acid ◽  
Prostaglandin H

DNA adducts formed by ring-oxidation of the carcinogen 2-naphthylamine with prostaglandin H synthase in vitro and in the dog urothelium in vivo

1985 ◽  
Vol 6 (9) ◽  
pp. 1379-1387 ◽  
Author(s):  
Y. Yamazoe ◽  
D.W. Miller ◽  
C.C. Weis ◽  
K.L. Dooley ◽  
T.V. Zenser ◽  
...  
Keyword(s):  
Dna Adducts ◽  
Prostaglandin H Synthase ◽  
Ring Oxidation ◽  
Prostaglandin H
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