Endogenous inhibitor of prostaglandin synthetase

Saeed, Sheikh A.; McDonald-Gibson, Wendy J.; Cuthbert, Josephine; Copas, Julia L.; Schneider, C; Gardiner, P.J.; Butt, Naeem M.; Collier, H. O. J.

doi:10.1038/270032a0

Cited by 147 publications

(43 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Most of these effects seem to be mediated by the induction or repression of enzymes. The release of anti-phospholipase proteins from leucocytes (and probably other cells) is one way in which the steroids can exert their antiinflammatory action; it is not the only way, neither is it the only way in which they could affect the prostaglandin system (Saeed, McDonald-Gibson, Cuthbert, Copas, Schneider, Gardiner, Butt & Collier, 1977;Moore & Hoult, 1980;Araki, Peck, Lefer & Smith, 1981). Nevertheless it is a mechanism which could account for many hitherto unexplained features of steroid action, and which therefore deserves careful scrutiny.…”

Section: Discussionmentioning

confidence: 99%

Glucocorticoids Induce the Formation and Release of Anti‐inflammatory and Anti‐phospholipase Proteins Into the Peritoneal Cavity of the Rat

Blackwell¹,

Carnuccio

Rosa

et al. 1982

British J Pharmacology

204

View full text Add to dashboard Cite

1 Dexamethasone and hydrocortisone induce the release of anti-phospholipase proteins into the peritoneal cavities of rats. 2 Adrenocorticotrophic hormone (ACTH) also releases these proteins in normal but not in adrenalectomized rats. 3 Peritoneal lavage proteins were separated by ion-exchange and size exclusion chromatography. The anti-phospholipase activity occurred in four separate fractions with the major component having an apparent mol.wt. of 40 k. 4 Column fractions containing these anti-phospholipase proteins had anti-inflammatory effects in the rat carrageenin pleurisy model whereas other fractions were inactive. 5 The proteins appear to be identical to macrocortin and lipomodulin, the 'second messengers' of glucocorticoid hormone action on the arachidonate system.

show abstract

Section: Discussionmentioning

confidence: 99%

Glucocorticoids Induce the Formation and Release of Anti‐inflammatory and Anti‐phospholipase Proteins Into the Peritoneal Cavity of the Rat

Blackwell¹,

Carnuccio

Rosa

et al. 1982

British J Pharmacology

204

View full text Add to dashboard Cite

show abstract

“…37,38 A more speculative possibility is that haptoglobin acts as a regulatory factor in the feedback control of fever as a result of its inhibitory effect on prostaglandin synthetase. [39][40][41] The heterogeneity in the responses of IL-6-induced haptoglobin, fibrinogen, and albumin expression to heat shock indicates that the mechanism of thermal interaction with the acute-phase response is downstream of the point at which the IL-6 signal-transduction pathway diverges. Induction of acutephase proteins by IL-6 occurs at the transcriptional level, 1,21,42 requires posttranslational modification of transcription factors, 43 and may require de novo protein synthesis in some species.…”

Section: Discussionmentioning

confidence: 99%

Interaction between heat shock and interleukin 6 stimulation in the acute-phase response of human hepatoma (HepG2) cells

1998

View full text Add to dashboard Cite

Two characteristic elements of the acute-phase response are an altered pattern of circulating hepatic proteins and fever. Whereas a fever-induced heat shock response could affect expression of acute-phase proteins in the liver, the effects of a modest temperature increase on protein secretion in interleukin-6 (IL-6)-stimulated HepG2 cells were investigated. The response of HepG2 cells to IL-6 stimulation was significantly affected by heat treatment at 40ЊC. Albumin secretion rates, which were reduced by a factor of 2 in response to either heat shock or IL-6 stimulation alone, were down-regulated by a factor of 4 when IL-6 was administered simultaneously with a continuous 40ЊC heat shock. IL-6-induced fibrinogen up-regulation was significantly reduced by heat treatment (P F .01), and secretion rates were indistinguishable from control levels after 2 days (P G .10). Unexpectedly, heat shock at 40ЊC induced a fivefold up-regulation of haptoglobin production in the absence of IL-6. Simultaneous heat shock and IL-6 stimulation caused a synergistic enhancement of haptoglobin expression, with secretion rates increasing up to 30-fold compared with unstimulated control cells. For all three proteins, the interaction between temperature and IL-6 concentration was statistically significant (P F .001). Heat treatment resulted in significant alterations of both the kinetics and sensitivity of IL-6-induced protein synthesis, suggesting a major modification of the mechanism of acute-phase protein regulation at 40ЊC. In summary, the data show that heat shock can significantly modulate the pattern of acute-phase protein expression and that fever may be an important regulatory factor in the acute-phase response. (HEPATOLOGY 1998;28:994-1004.)The acute-phase response, a collective term referring to the constellation of host defense mechanisms induced in response to inflammation, infection, trauma, and certain malignancies, is characterized by drastic metabolic changes in the liver and is often accompanied by fever in the host. Indeed, the same cytokines that mediate the inflammatory processes are also endogenous pyrogens.

show abstract

“…Furthermore, inhibition of COX and LOX by plasma lipoproteins points to an important regulatory link in the body's defense system [11]. Our previous work shows that AA metabolism and human platelet aggregation is inhibited by human plasma, serum and other body fluids that this action of plasma is related to human hemoglobin and haptoglobin [15,16]. In the present study we found that plasma from different mammalian species is capable of inhibiting the cyclooxygenation and lipoxygenation of AA.…”

Section: Resultsmentioning

confidence: 47%

Anti-Inflammatory and Antiplatelet Activities of Plasma Are Conserved Across Twelve Mammalian Species

et al. 2014

View full text Add to dashboard Cite

Human plasma inhibits arachidonic acid metabolism and platelet aggregation. This helps human form a haemostatic control system that prevents the progress of certain aggregatory or inflammatory reactions. Whether this property of plasma is unique to human or extends to other species is not well known. It is speculated that this protective ability of plasma remains evolutionarily conserved in different mammals. In order to confirm this, the effect of plasma from 12 different mammalian species was investigated for its inhibitory potential against arachidonic acid metabolism and platelet aggregation. Metabolism of arachidonic acid by cyclooxygenase and lipoxygenase pathways was studies using radio-immuno assay and thin layer chromatography while platelet aggregation in the plasma of various mammals was monitored following turbedmetric method in a dual OPEN ACCESSMolecules 2014, 19 11386 channel aggregometer. Results indicate that inhibition of AA metabolism and platelet aggregation is a common feature of plasma obtained from different mammalian species, although there exists large interspecies variation. This shows that besides human, other mammals also possess general protective mechanisms against various aggregatory and inflammatory conditions and this anti-inflammatory property of the plasma is evolutionarily conserved in mammalian species. The most likely candidates responsible for these properties of plasma include haptoglobin, albumin and lipoproteins.

show abstract

Endogenous inhibitor of prostaglandin synthetase

Cited by 147 publications

References 15 publications

Glucocorticoids Induce the Formation and Release of Anti‐inflammatory and Anti‐phospholipase Proteins Into the Peritoneal Cavity of the Rat

Glucocorticoids Induce the Formation and Release of Anti‐inflammatory and Anti‐phospholipase Proteins Into the Peritoneal Cavity of the Rat

Interaction between heat shock and interleukin 6 stimulation in the acute-phase response of human hepatoma (HepG2) cells

Anti-Inflammatory and Antiplatelet Activities of Plasma Are Conserved Across Twelve Mammalian Species

Contact Info

Product

Resources

About