Modulation of the human monocyte binding site for monomeric immunoglobulin G by activated Hageman factor.

Chien, Paul; Pixley, Robin A.; Stumpo, L G; Colman, Robert W.; Schreiber, AD

doi:10.1172/jci113765

Cited by 35 publications

(17 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have previously observed that steroid hormones can influence human monocyte/macrophage Fcy receptor expression in vitro and in vivo (2,15,29,30). Furthermore, it appears that some Fcy receptors, e.g., human FcyR 1, are more responsive to such modulatory signals than are other macrophage Fcy receptors (2,28,30,31), similar to the relative preferential effect of glucocorticoids on guinea pig splenic macrophage Fc'yR2. However, the precise homology between the guinea pig and human macrophage Fcy receptors awaits the cloning of the guinea pig Fcy receptor genes.…”

Section: Resultsmentioning

confidence: 78%

In vivo glucocorticoid modulation of guinea pig splenic macrophage Fc gamma receptors.

Ruiz¹,

Gomez²,

King³

et al. 1991

J. Clin. Invest.

Self Cite

View full text Add to dashboard Cite

Although glucocorticoids are widely used in the treatment of immunohematologic disease, their relative efficacy is uncertain. We used an animal model, which has helped to elucidate the role of splenic macrophage Fc'y receptors in the clearance of IgG-coated cells, to investigate whether each Fc'y receptor is modulated by glucocorticoids to the same extent and to examine the relative potency of three commonly used glucocorticoids. Cortisol, prednisone, and dexamethasone all impaired the clearance ofIgG-coated erythrocytes. However, dexamethasone was more effective than either prednisone or cortisol (P < 0.001). Furthermore, splenic macrophages isolated from glucocorticoid-treated animals expressed impaired Fcy receptor function. This effect was greater in macrophages isolated from dexamethasone-treated animals, as compared to either cortisol-or prednisone-treated animals (P < 0.001). To assess the effect of glucocorticoids on the two types of guinea pig splenic macrophage Fc-y receptors, FcyR1,2 and FcyR2, specific immunoglobulin isotypes were used to measure macrophage binding of IgG-sensitized erythrocytes. Cortisol and prednisone primarily affected FcyR2, whereas dexamethasone inhibited the function of both guinea pig Fcy receptors. Furthermore, dexamethasone was more effective (P < 0.01) than either prednisone or cortisol in inhibiting the ability of both receptors to bind IgG-sensitized cells. Fluorescence-activated cell sorter analysis and fluorescence microscopy with monoclonal antibodies specific for each of these two receptors demonstrated that essentially all splenic macrophages expressed both receptors, and that these glucocorticoids decreased the level of each Fcy receptor protein expressed, rather than altering receptor mobility and clustering in the macrophage membrane. The effect on both Fcy receptors was greatest with dexamethasone and least with cortisol. These studies demonstrate the significant role of guinea pig splenic macrophage (J. Clin. Invest. 1991. 88:149-157.)

show abstract

Section: Resultsmentioning

confidence: 78%

In vivo glucocorticoid modulation of guinea pig splenic macrophage Fc gamma receptors.

Ruiz¹,

Gomez²,

King³

et al. 1991

J. Clin. Invest.

Self Cite

View full text Add to dashboard Cite

show abstract

“…In human plasma, FXII and FXIIa induce neutrophil aggregation (17) and plasma FXII is present on the surface of neutrophils (18). Zymogen FXII stimulates monocyte expression of FcγRII (19). In contrast to other components of the coagulation system, FXII has 2 EGF domains and the zymogen has mitogenic activity in smooth muscle and endothelial cells where FXII stimulates angiogenesis through urokinase plasminogen activator receptor (uPAR) (20)(21)(22).…”

Section: Introductionmentioning

confidence: 99%

Factor XII and uPAR upregulate neutrophil functions to influence wound healing

Stavrou

Fang

Bane

et al. 2018

Journal of Clinical Investigation

115

118

View full text Add to dashboard Cite

“…Several other domains, located at the N-terminal end, may have regulatory functions and comprise a leader peptide, a fibronectin-11 domain, a growth-factor-like domain, a fibronectin-I domain, a second growth-factor-like domain, a kringle domain and a proline-rich region which is unique to this protein. The functions of these domains have not been explored in relation to the multiple physiological roles of FXII and can only be assigned by analogy with similar domains of other serine proteases (Cool et al, 1985;Chien et al, 1988;Pixley et a]., 1987;Clarke et al, 1989). Their importance for the activation of the contact phase of blood coagulation is inferred from the inability of a fragment of FXII, comprising only the catalytic region and nine amino acids of the FXII heavy chain (the FXII fragment, also known as P-FXII), to bind to negative charges and to efficiently promote blood clotting (Kaplan and Silver ber g , 1 98 7).…”

mentioning

confidence: 99%

Control of human coagulation by recombinant serine proteases

Citarella

Aiuti

Porta

et al. 1992

European Journal of Biochemistry

View full text Add to dashboard Cite

The availability of engineered serine proteases allows one to study the activation, substrate specificity and regulation of human coagulation and fibrinolytic activities. Human coagulation factor XI1 is composed of the protease catalytic region at the C-terminus, a hinge proline-rich region and regulatory domains at the N-terminus. From cDNA clones coding for factor XII, two DNA molecules were constructed, one being full length and the other being deleted of exons coding for the regulatory domains. Engineered factor-XI1 cDNA species were inserted by a homologous recombination technique into vaccinia viruses. which were used to infect the human hepatoma cell line HepG2. Two recombinant proteins were prepared from the culture media and identified by their antigenic properties and electrophoretic mobilities. The recombinant protein of larger size was identified as the full-length factor XI1 of 80 kDa and its specific activities and activation patterns, determined both by the coagulation and the amidolytic assays, are very similar to these of native human factor XII. The recombinant protein of smaller size was identified as a 319-amino-acid-deleted factor-XI1 protein of 32 kDa, containing only the entire protease region and part of the proline-rich hmge. This protein was expected to be the 'minimal' portion of Factor XI1 able to sustain protease activity, but unable to recognize substrates and surfaces necessary to activate the contact phase of coagulation. However, this 'minimal' Factor-XI1 protein displays a marked protease activity and, although lacking five regulatory domains of factor XLI, is bound and activated by negative charges and promotes coagulation with high efficiency.Events relevant to cellular and extracellular processes are regulated by the sequential enzymatic activation of proteins. One example of this is protein kinase activity leading to the regulation of important functions in the cell cycle and differentiation. Cascades of serine protease activities bring into effect and regulate extracellular processes of great importance to vertebrate organisms, such as blood coagulation, fibrinolysis and inflammation. The multiple and composite functions of serine proteases may be ascribed to structural domains able to recognize activating surfaces, inhibitors, cofactors and other serine proteases. The present study is aimed at producing and characterizing recombinant (r) human factor XI1 (FXII) proteins in order to clarify the functional role of the different domains composing human FXII.

show abstract

Modulation of the human monocyte binding site for monomeric immunoglobulin G by activated Hageman factor.

Cited by 35 publications

References 21 publications

In vivo glucocorticoid modulation of guinea pig splenic macrophage Fc gamma receptors.

In vivo glucocorticoid modulation of guinea pig splenic macrophage Fc gamma receptors.

Factor XII and uPAR upregulate neutrophil functions to influence wound healing

Control of human coagulation by recombinant serine proteases

Contact Info

Product

Resources

About