Fc-mediated binding of IgG to vimentin-type intermediate filaments in vascular endothelial cells.

Hansson, Göran K.; Starkebaum, Gordon; Benditt, Earl P.; Schwartz, Stephen M.

doi:10.1073/pnas.81.10.3103

Cited by 38 publications

(14 citation statements)

References 32 publications

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“…Centriole staining was not observed, when preabsorbed anti-tektins were used. Hansson et al (27) (data not shown) similar to those described for uncleaved anti-tektins.…”

Section: Resultssupporting

confidence: 61%

Evidence for tektins in centrioles and axonemal microtubules.

Walter

Linck

1988

Proc. Natl. Acad. Sci. U.S.A.

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Affinity purified, polyclonal antibodies were prepared against three tektins (tektins A, B, and C) isolated from sea urchin sperm axonemal microtubules. These antibodies (anti-tektins) were used to localize tektins in axonemes, basal bodies, and centrioles. By immunofluorescence microscopy it could be demonstrated that in sperm tails from Lytechinus pictus all three anti-tektins stain all nine axonemal doublet microtubules and A-tubule extensions along their entire length. In addition to staining doublet microtubules, anti-tektin C weakly labeled the central-pair microtubules in sperm tails from Patiria miniata. The anti-tektin staining revealed also a clear cross-reaction with basal bodies of sea urchin sperm and with centrioles of cells from hamsters, humans, and pigs. These data provide evidence of tektin or tektin-like proteins in basal bodies and centrioles and suggest that centriole microtubules are constructed according to the same principles as flagellar microtubules.Centrioles are important cell organelles in nearly all animal cells and in some plant cells (1, 2). Aside from the clear presence of tubulin in centriolar microtubules (3, 4), their molecular composition is poorly understood. Several antibodies have been reported to cross-react with centriole components (4-7), but the nature and function of these components in relation to the microtubules have not been determined. Perhaps the most basic function of the centriole, in the capacity of a basal body, is to act as a template for the assembly of ciliary and flagellar axonemes (1, 2, 8-10). In particular, the A-and B-subfibers of centriolar triplet microtubules are templates for the assembly of the A-and Bsubfibers of ciliary and flagellar doublet microtubules. Because of the relationship between axonemes and centrioles, we have been investigating whether centrioles might share proteins with doublet microtubules, about which considerably more is known. In related investigations we have found that doublet microtubules from sea urchin sperm flagella can be extracted free of tubulin, leaving filaments, 2-6 nm in diameter, that are composed predominantly of a set of proteins named tektins (11-13). Three distinct, but related, tektins with relative molecular masses between 46 kDa and 57 kDa have so far been characterized. The tektins are different from tubulin yet strikingly similar to intermediate filament proteins in terms of their solubility properties, molecular masses, amino acid composition, fibrous substructure, high a-helical content, and immunological determinants (11-16). Cross-reactivities with polyclonal antibodies to a mixture of tektins indicate the presence of homologous proteins in echinoderm embryonic cilia and molluscan gill cilia (17). Chemical fractionation and immuno electron microscopy studies further suggest that tektins are components of the A-subfibers of doublet microtubules (12, 18), but it has not been determined whether all three tektins are present in each of the flagellar microtubules.We have prepared and characteri...

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“…Centriole staining was not observed, when preabsorbed anti-tektins were used. Hansson et al (27) (data not shown) similar to those described for uncleaved anti-tektins.…”

Section: Resultssupporting

confidence: 61%

Evidence for tektins in centrioles and axonemal microtubules.

Walter

Linck

1988

Proc. Natl. Acad. Sci. U.S.A.

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“…Furthermore, our current findings represent a plausible explanation for our previous demonstration of increased expression of PAI-1 on the surface of endothelium exposed to bacterial endotoxin and other inflammatory mediators in vitro (57) and in vivo (34). Vimentin also may modulate inflammatory responses and atherosclerosis (58) through its interactions with plasma proteins such as complement (59,60), IgG (61,62), and fibrinogen (62). Cytokeratin-type intermediate filaments that are also exposed on the surface of various cells interact with various hemostasis factors including kininogen (63,64), plasminogen (65), and thrombin⅐antithrombin⅐Vn complexes (66).…”

Section: Table I Pai-1 Activity and Antigen In Thrombin-activated Plamentioning

confidence: 54%

Vimentin Exposed on Activated Platelets and Platelet Microparticles Localizes Vitronectin and Plasminogen Activator Inhibitor Complexes on Their Surface

Podor¹,

Singh²,

Chindemi³

et al. 2002

Journal of Biological Chemistry

115

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Type 1 plasminogen activator inhibitor (PAI-1), the primary inhibitor of tissue-type plasminogen activator (t-PA), is found in plasma and platelets. PAI-1 circulates in complex with vitronectin (Vn), an interaction that stabilizes PAI-1 in its active conform. In this study, we examined the binding of platelet-derived Vn and PAI-1 to the surface of isolated platelets. Flow cytometry indicate that, like P-selectin, PAI-1, and Vn are found on the surface of thrombin-or calcium ionophore-activated platelets and platelet microparticles. The binding of PAI-1 to the activated platelet surface is Vn-dependent. Vn mediates the binding of PAI-1 to platelet surfaces through a high affinity (K d of 80 nM) binding interaction with the NH 2 terminus of vimentin, and this Vn-binding domain is expressed on the surface of activated platelets and platelet microparticles. Immunological and functional assays indicate that only ؊5% of the total PAI-1 in platelet releasates is functionally active, and it co-precipitates with Vn, and the vimentin-enriched cytoskeleton fraction of activated platelet debris. The remaining platelet PAI-1 is inactive, and does not associate with the cytoskeletal debris of activated platelets. Confocal microscopic analysis of platelet-rich plasma clots confirm the co-localization of PAI-1 with Vn and vimentin on the surface of activated platelets, and platelet microparticles. These findings suggest that platelet vimentin may regulate fibrinolysis in plasma and thrombi by binding platelet-derived Vn⅐PAI-1 complexes.

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“…Endothelial cell damage has been reported to result from circulating pathologic autoantibodies against EC [6,7]. Passive accumulation of normal IgG has been found only in irreversibly damaged EC [8].…”

Section: Introductionmentioning

confidence: 99%

Binding and internalization of human IgG by living cultured endothelial cells

Ronda

Gatti

Orlandini

et al. 1997

Clinical and Experimental Immunology

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SUMMARYInteractions between circulating IgG and endothelial cells (EC) in humans have been described only in conditions associated with pathologic immunoglobulins and/or activated or damaged EC. In this study we provide evidence that normal human IgG includes one/some antibody species that bind to and are internalized by living EC in culture. This novel function of EC and natural autoantibodies is of potential importance for the understanding of physiologic interactions between vessels and the immune system and for the clarification of pathogenesis of vasculitis and mechanisms of action of pooled IgG used in the therapy of such conditions.

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Fc-mediated binding of IgG to vimentin-type intermediate filaments in vascular endothelial cells.

Abstract: Prior

Cited by 38 publications

References 32 publications

Evidence for tektins in centrioles and axonemal microtubules.

Evidence for tektins in centrioles and axonemal microtubules.

Vimentin Exposed on Activated Platelets and Platelet Microparticles Localizes Vitronectin and Plasminogen Activator Inhibitor Complexes on Their Surface

Binding and internalization of human IgG by living cultured endothelial cells

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