Effects of hydrocortisone on binding of IgG or C3b-coated erythrocytes to human monocytes and polymorphonuclear leucocytes

Tolone, G.; Bonasera, L.; Sajeva, R

doi:10.1111/j.2042-7158.1979.tb13588.x

Cited by 16 publications

(3 citation statements)

References 5 publications

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“…A number of studies have shown glucocorticoid inhibition of the expression or availability of Fc receptors in human peripheral blood neutrophils or in a human promyelocytic cell line (158,159). In addition, several steroids including cortisol inhibit monocyte receptor activity for both IgG and C3b in a dose-response fashion (160,161). Phospholipid changes after adrenalectomy are reported to influence adrenaline-induced lipolysis (162).…”

Section: Corticosteroid Effects Upon Receptor Activitymentioning

confidence: 97%

Corticosteroid-Induced Changes in Phospholipid Membranes as Mediators of Their Action*

Nelson

1980

Endocrine Reviews

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T HIS SHORT review will describe mechanisms by which corticosteroid modification of cellular phospholipids and particularly the phospholipid-structure of a variety of membranes can produce some of the effects of the corticosteroids. In addition to these effects, many studies have demonstrated effects of other hormones to alter specific phospholipids, phospholipases, or for phospholipase action on cells to mimic hormone action. All actions of the corticosteroids are not thought to be produced by these lipid alterations, but such changes are capable of producing widespread effects on receptor activity, RNA and protein synthesis, enzymatic activity, and transport through membranes. The availability of new data indicating that phospholipids are altered considerably by corticosteroids in a number of tissues makes a review of this subject of interest at this time.Corticosteroids are secreted in response to a variety of "stresses" that represent alterations in the cellular environment that might result in death or injury to the exposed cells if proper adaptation did not occur. Thus, these hormones are increased in response to anoxia, very low or very high temperature, or hypoglycemia. Through mechanisms that have not been clearly understood the cell is protected by the increased hormones against potentially harmful alterations in its environment. Unicellular organisms, which lack a sophisticated endocrine system for response to stresses, undergo modifications in cellular membranes in response to stress. A decrease in the temperature at which the organism is grown would produce a decrease in the fluidity of the membrane with resulting marked effects upon membrane-bound enzymatic activities. Similarly, increased temperature would result in increased fluidity of the lipid membrane and similar alterations in its function. In order

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Section: Corticosteroid Effects Upon Receptor Activitymentioning

confidence: 97%

Corticosteroid-Induced Changes in Phospholipid Membranes as Mediators of Their Action*

Nelson

1980

Endocrine Reviews

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“…In vivo studies of immune hemolytic anemia suggested corticosteroid treatment in some way altered the interaction between the target erythrocytes and receptors on the surface of the effector reticuloendothelial cell (41)(42)(43). Other in vitro and in vivo studies have also implicated an impairment of binding of C3b and IgG to their respective receptors on monocyte/ macrophages (20,21), and more recently neutrophils (22,23), to be one effect of supraphysiologic concentrations (0.05-1.0 mg/ml) of corticosteroids. Recently, using the HL-60 human progranulocytic cell line, it has been demonstrated that 200 The mechanism by which peptide binding is altered by corticosteroids was further elucidated by examining the kinetics of interaction of the peptide with its receptor using living whole granulocytes.…”

Section: Discussionmentioning

confidence: 99%

“…Because corticosteroids have been reported to alter surface receptors in some immune adherence assays (20)(21)(22)(23), we postulated altered receptor function as a possible mechanism of high-dose corticosteroid effect on granulocyte responses to activated complement components. This hypothesis has been studied using the synthetic chemotaxin N-formyl-methionine-leucinephenylalanine (FMLP) as a probe to study the effect of corticosteroids on PMN receptor function.…”

Section: Introductionmentioning

confidence: 99%

Corticosteroids block binding of chemotactic peptide to its receptor on granulocytes and cause disaggregation of granulocyte aggregates in vitro.

Skubitz¹,

Craddock²,

Hammerschmidt³

et al. 1981

J. Clin. Invest.

117

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A B S T R A C T Inhibition of complement-mediated granulocyte aggregation has recently been proposed as a mechanism of action of high-dose corticosteroids in shock states. Postulating that such inhibition might be effected through alteration of receptor function, we examined the effect of methylprednisolone (MP), hydrocortisone (HC), and dexamethasone (DEX) on the extent and kinetics of binding of the synthetic chemotaxin f-methionine-leucine-phenylalanine (FMLP) to its specific receptor on the granulocyte surface. Dose

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o‐Chlorobenzaldehyde 89‐98‐5

2004

Sax's Dangerous Properties of Industrial Materials

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Effects of hydrocortisone on binding of IgG or C3b-coated erythrocytes to human monocytes and polymorphonuclear leucocytes

Cited by 16 publications

References 5 publications

Corticosteroid-Induced Changes in Phospholipid Membranes as Mediators of Their Action*

Corticosteroid-Induced Changes in Phospholipid Membranes as Mediators of Their Action*

Corticosteroids block binding of chemotactic peptide to its receptor on granulocytes and cause disaggregation of granulocyte aggregates in vitro.

o‐Chlorobenzaldehyde 89‐98‐5

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