The Role of a Hemolytic System in Human Tissues in Some Hemolytic States

Stefanini, Mario; Xefteris, Electra; Moschides, Elly; Blumenthal, William S.

doi:10.1097/00000441-196109000-00005

Cited by 6 publications

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, IgG and complement could mediate autoimmune hemolytic anemia [39] . However, the mechanism through which the erythrocyte meets its destruction in normal conditions remains controversial [40] – [42] . The present findings that two IgG fractions possessed nonspecific hemolytic properties against erythrocytes might provide an alternative approach to induce hemolysis in normal conditions in human.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Novel Hemolytic Activity of Human IgG Fractions Arising from Diversity in Protein and Oligosaccharide Components

et al. 2014

View full text Add to dashboard Cite

Human IgG is a well-established multifunctional antigen specific immunoglobulin molecule of the adaptive immune system. However, an antigen nonspecific immunological function of human IgG has never been reported. In this study, human IgG was isolated using ammonium sulfate fractional precipitation and diethylaminoethanol (DEAE) cellulose 52 ion exchange chromatography, from which h-IgG and hs-IgG fractions were purified on the basis of their differential binding to rabbit anti-shrimp hemocyanin antibody (h) and rabbit anti-shrimp hemocyanin's small subunit antibody (hs), respectively. We found that h-IgG had a higher hemolytic activity than hs-IgG against erythrocytes from humans, rabbits, mice and chickens, whereas the control IgG showed negligible activity. h-IgG could interact directly with erythrocyte membranes, and this interaction was suppressed by high molecular weight osmoprotectants, showing that it may follow a colloid-osmotic mechanism. In comparative proteomics and glycomics studies, h-IgG and hs-IgG yielded 20 and 5 significantly altered protein spots, respectively, on a 2-D gel. The mean carbohydrate content of h-IgG and hs-IgG was approximately 3.6- and 2-fold higher than that of IgG, respectively, and the α-d-mannose/α-d-glucose content was in the order of h-IgG>hs-IgG>IgG. In this study, a novel antigen nonspecific immune property of human IgG was investigated, and the diversity in the protein constituents and glycosylation levels may have functional signficance.

show abstract

Section: Discussionmentioning

confidence: 99%