PubMed HealthSearch

PubMed · 6367714

[Inflammation, immunity, hypersensitivity].

Abstract

The conjugation between inflammation and hypersensitivity is analysed. In human pathology, these processes have been shown to be closely associated and to be in the cause-and-effect relationship, immunity being the connecting link between them: immune responses generated in inflammation for elimination of the injurious agent and reparation may, upon distortion of the inflammation kinetics, become responses of "sick immunity" or hypersensitivity responses leading to damage and immune inflammation. The problem of conjugation of inflammation and hypersensitivity with immunity covers a wide range of aspects of morphology, molecular biology, immunology, and genetics. The understanding of this conjugation will give an insight into immunopathology represented in all branches of the modern clinical science.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

V V Serov. 1983. [Inflammation, immunity, hypersensitivity].. https://pubmed.ncbi.nlm.nih.gov/6367714/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Superoxide dismutase protects Escherichia coli against killing by human serum.

To assess the role of superoxide dismutase in protecting Escherichia coli from killing by human serum and neutrophils, we constructed isogenic, smooth-lipopolysaccharide K-12 strains, either sod wild-type, delta sodA, or delta sodA delta sodB. The delta sodA delta sodB strain was killed by serum much more readily than either the wild-type or delta sodA strain. After allowing for this serum sensitivity difference, the delta sodA delta sodB strain also showed increased susceptibility to phagocytic killing by human neutrophils. These results indicate that superoxide dismutase protects E. coli from killing by serum (complement system) and by human neutrophils, possibly by a role in maintaining bacterial membrane structure.

Complement System Proteins

Dual function of human IgA antibodies: inhibition of phagocytosis in circulating neutrophils and enhancement of responses in IL-8-stimulated cells.

We have sought to elucidate the responses of human peripheral blood neutrophils to antigenic surfaces complexed with human specific IgA antibodies obtained either as myeloma proteins that recognize staphylococcal alpha-toxin, or from the serum of patients with subacute bacterial endocarditis due to Streptococcus mutans, or from colostrum. In contrast to IgG, IgA antibodies bound to antigen-coated fluorescent microspheres, and subsequently exposed to complement (or not), did not promote phagocytosis, as measured by flow cytometric enumeration of cell-associated microspheres. Instead, IgA antibodies interfered with complement-dependent phagocytosis mediated by IgG antibodies. These properties were shown by different forms of IgA antibodies, including serum and secretory IgA, as well as by monoclonal or polyclonal antibodies. Neutrophils did not respond to the production of superoxide to IgA antibodies complexed with antigen-coated microspheres or with antigen deposited on a solid surface and IgA antibodies suppressed IgG antibody- and complement-mediated superoxide release. However, neutrophils pretreated with interleukin-8 ingested IgA-opsonized microspheres and released superoxide when exposed to IgA antibody-antigen complexes. IgG antibody-antigen complexes did not stimulate increased superoxide release in interleukin-8-treated neutrophils. These findings were consistent with a selective increase in the surface expression of Fc alpha R by interleukin-8-treated neutrophils. We conclude that IgA antibodies interfere with the phagocytic activities of normal circulating human neutrophils and may promote these activities in inflammatory neutrophils activated by interleukin-8 in which Fc alpha R is up-regulated.

Complement System Proteins