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C3 dysregulation due to factor H deficiency is mannan-binding lectin-associated serine proteases (MASP)-1 and MASP-3 independent in vivo.

Ruseva MM, Takahashi M, Fujita T, Pickering MC - Clin. Exp. Immunol. (2014)

Bottom Line: Mannan-binding lectin-associated serine proteases 1 and 3 (MASP-1, MASP-3) have been shown recently to contribute to alternative pathway activation by cleaving pro-factor D to its active form, factor D.Co-deficiency of FH and MASP-1/MASP-3 did not ameliorate either the plasma C3 activation or glomerular C3 accumulation in FH-deficient mice.Our data indicate that MASP-1 and MASP-3 are not essential for alternative pathway activation in complete FH deficiency.

View Article: PubMed Central - PubMed

Affiliation: Centre for Complement & Inflammation Research, Imperial College London, London, UK.

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Serum alternative pathway activity in Cfh–/–.mannan-binding lectin-associated serine proteases (MASP)-1/3–/– and MASP-1/3–/– mice. Rabbit erythrocytes were incubated with dilutions of serum from Cfh–/–.MASP-1/3–/– and MASP-1/3–/– and wild-type mice (n = 2 per group) and haemolytic activity was assessed by measuring release of haemoglobin in to the supernatant. Percentage lysis was plotted against serum concentration (expressed as percentage, logarithmic scale). Each symbol represents percentage lysis from an individual mouse and each point is an average of duplicate measurements. Data from one of two independent experiments with similar results are shown.
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fig05: Serum alternative pathway activity in Cfh–/–.mannan-binding lectin-associated serine proteases (MASP)-1/3–/– and MASP-1/3–/– mice. Rabbit erythrocytes were incubated with dilutions of serum from Cfh–/–.MASP-1/3–/– and MASP-1/3–/– and wild-type mice (n = 2 per group) and haemolytic activity was assessed by measuring release of haemoglobin in to the supernatant. Percentage lysis was plotted against serum concentration (expressed as percentage, logarithmic scale). Each symbol represents percentage lysis from an individual mouse and each point is an average of duplicate measurements. Data from one of two independent experiments with similar results are shown.

Mentions: Using a calcium-free rabbit erythrocyte haemolysis in-vitro assay, AP-mediated cell lysis was readily detectable with wild-type sera (Fig. 5). As expected, no lysis was demonstrable using sera from Cfh–/–.MASP-1/3–/– mice, as these sera are depleted of both C3 and C5 (Fig. 1). However, sera from MASP-1/3–/– mice, in contrast to previous reported in-vitro assays [13,17], did demonstrate lysis, although this was reduced in comparison with that of wild-type mice.


C3 dysregulation due to factor H deficiency is mannan-binding lectin-associated serine proteases (MASP)-1 and MASP-3 independent in vivo.

Ruseva MM, Takahashi M, Fujita T, Pickering MC - Clin. Exp. Immunol. (2014)

Serum alternative pathway activity in Cfh–/–.mannan-binding lectin-associated serine proteases (MASP)-1/3–/– and MASP-1/3–/– mice. Rabbit erythrocytes were incubated with dilutions of serum from Cfh–/–.MASP-1/3–/– and MASP-1/3–/– and wild-type mice (n = 2 per group) and haemolytic activity was assessed by measuring release of haemoglobin in to the supernatant. Percentage lysis was plotted against serum concentration (expressed as percentage, logarithmic scale). Each symbol represents percentage lysis from an individual mouse and each point is an average of duplicate measurements. Data from one of two independent experiments with similar results are shown.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3958157&req=5

fig05: Serum alternative pathway activity in Cfh–/–.mannan-binding lectin-associated serine proteases (MASP)-1/3–/– and MASP-1/3–/– mice. Rabbit erythrocytes were incubated with dilutions of serum from Cfh–/–.MASP-1/3–/– and MASP-1/3–/– and wild-type mice (n = 2 per group) and haemolytic activity was assessed by measuring release of haemoglobin in to the supernatant. Percentage lysis was plotted against serum concentration (expressed as percentage, logarithmic scale). Each symbol represents percentage lysis from an individual mouse and each point is an average of duplicate measurements. Data from one of two independent experiments with similar results are shown.
Mentions: Using a calcium-free rabbit erythrocyte haemolysis in-vitro assay, AP-mediated cell lysis was readily detectable with wild-type sera (Fig. 5). As expected, no lysis was demonstrable using sera from Cfh–/–.MASP-1/3–/– mice, as these sera are depleted of both C3 and C5 (Fig. 1). However, sera from MASP-1/3–/– mice, in contrast to previous reported in-vitro assays [13,17], did demonstrate lysis, although this was reduced in comparison with that of wild-type mice.

Bottom Line: Mannan-binding lectin-associated serine proteases 1 and 3 (MASP-1, MASP-3) have been shown recently to contribute to alternative pathway activation by cleaving pro-factor D to its active form, factor D.Co-deficiency of FH and MASP-1/MASP-3 did not ameliorate either the plasma C3 activation or glomerular C3 accumulation in FH-deficient mice.Our data indicate that MASP-1 and MASP-3 are not essential for alternative pathway activation in complete FH deficiency.

View Article: PubMed Central - PubMed

Affiliation: Centre for Complement & Inflammation Research, Imperial College London, London, UK.

Show MeSH
Related in: MedlinePlus