Allergen Sensitization and Perennial Asthma

Platts-Mills, Thomas A.E.; Squillace, Susan Pollart

doi:10.1159/000237514

Cited by 20 publications

(23 citation statements)

References 22 publications

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“…Hemolytic Assays-Results using both X13.2 and X52.1 with RE at the lysis target (29,30) were in sharp contrast to those observed with purified complement components. X13.2 was seen to be a strong inhibitor of complement-mediated hemolysis.…”

Section: Effects Of Monoclonal Antibodies On Fh/factor I-mediated Clementioning

confidence: 77%

Mechanistic Studies of the Effects of Anti-factor H Antibodies on Complement-mediated Lysis

Corey¹,

Kinders²,

Poduje³

et al. 2000

Journal of Biological Chemistry

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We have recently reported that complement factor H, a negative regulator of complement-mediated cytotoxicity, is produced and secreted by most bladder cancers. This observation was exploited in the development of the BTA stat™ and BTA TRAK™ diagnostic assays, both of which make use of two factor H-specific monoclonal antibodies in sandwich format. Here we show that both antibodies exert interesting effects on the biochemistry of complement activation in in vitro systems. Antibody X13.2 competes with C3b for association with factor H and strongly inhibits factor H/factor I-mediated cleavage of C3b, thereby evidently inactivating a negative regulator of complement; yet, the antibody strongly inhibits complement-mediated lysis as well. Conversely, antibody X52.1, which does not compete with C3b and has no effect on solution-phase cleavage of C3b, is capable of enhancing complement-mediated lysis of various cell types, including cancer cells, by over 10-fold. Our observations indicate that it is possible to deconvolute the biochemical roles of factor H in complement by means of appropriate inhibitors, a finding with potentially valuable implications for both basic research and cancer therapy.

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Section: Effects Of Monoclonal Antibodies On Fh/factor I-mediated Clementioning

confidence: 77%

Mechanistic Studies of the Effects of Anti-factor H Antibodies on Complement-mediated Lysis

Corey¹,

Kinders²,

Poduje³

et al. 2000

Journal of Biological Chemistry

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“…Erythrocyte Lysis Assays-To test for the alternative pathway of complement activation using rabbit erythrocytes and human serum (19), rabbit erythrocytes in Alsever's solution (Spring Valley Labs, Woodbine, MD) were washed five times with 10 vol of 150 mM NaCl, 10 mM HEPES, pH 7.4 (HEPES saline), followed by centrifugation for 2 s at 10,000 ϫ g. Reaction medium, in a 96-well plate, contained 0.4% packed erythrocytes in 40 l of 6.25 mM EGTA, 2.5 mM MgCl 2 , 20 mM HEPES, pH 7.4, and 150 mM NaCl. Additionally, 5 l of the test sample or HEPES saline control was added.…”

Section: Methodsmentioning

confidence: 99%

Purification, Cloning, and Expression of a Novel Salivary Anticomplement Protein from the Tick, Ixodes scapularis

Valenzuela¹,

Charlab²,

Mather³

et al. 2000

Journal of Biological Chemistry

224

219

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The alternative pathway of complement is an important defense against pathogens and in tick rejection reactions. The tick Ixodes scapularis is able to feed repeatedly on its natural host and has a salivary anticomplement activity that presumably facilitates feeding. In this study, we purified and then obtained the aminoterminal sequence of the I. scapularis salivary anticomplement (Isac). We found a full-length clone coding for Isac by random screening of a salivary gland cDNA library. Expressing Isac cDNA in COS cells reproduced the activity found in tick saliva, namely, inhibition of rabbit erythrocyte lysis by human serum in the presence of Mg 2؉ and EGTA, inhibition of C3b binding to agarose in the presence of Mg 2؉ and EGTA, and acceleration of factor Bb uncoupling from the C3 convertase generated by the alternative pathway. Recombinant Isac had no effect on the recalcification time of human platelet-poor plasma or in the classical complement pathway, indicating that it is a specific inhibitor similar to the regulators of complement activation of the alternative pathway such as factor H. Isac, however, has no similarity to any protein in the GenBank TM data base, indicating that it is a novel and relatively small (18.5 kDa) anticomplement molecule.

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“…The other two binding sites have not yet been well characterized. Results obtained by using either several anti-fH mAbs (38) or deletion mutants lacking [5][6][7][8][9][10] SCR domains (39) showed that there is more than one binding site on fH for C3b. One of the two new sites was localized to and the other was suggested to lie within .…”

Section: Introductionmentioning

confidence: 99%

Each of the Three Binding Sites on Complement Factor H Interacts with a Distinct Site on C3b

Jokiranta¹,

Hellwage²,

Koistinen³

et al. 2000

Journal of Biological Chemistry

196

157

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Allergen Sensitization and Perennial Asthma

Cited by 20 publications

References 22 publications

Mechanistic Studies of the Effects of Anti-factor H Antibodies on Complement-mediated Lysis

Mechanistic Studies of the Effects of Anti-factor H Antibodies on Complement-mediated Lysis

Purification, Cloning, and Expression of a Novel Salivary Anticomplement Protein from the Tick, Ixodes scapularis

Each of the Three Binding Sites on Complement Factor H Interacts with a Distinct Site on C3b

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