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9 záznamů v PubMed Filtry

Článek

Relative efficiencies of peptidylarginine deiminase 2 and 4 in generating target sites for anti-citrullinated protein antibodies in fibrinogen, alpha-enolase and histone H3

Damgaard, Dres
Autor Damgaard, Dres ORCID Institute for Inflammation Research, Center for Rheumatology and Spine Diseases, Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark Section for Periodontology, Microbiology and Community Dentistry, Department of Odontology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark
Bawadekar, Mandar
Autor Bawadekar, Mandar ORCID Department of Medicine, University of Wisconsin, Madison, Wisconsin, United States of America
Senolt, Ladislav
Autor Senolt, Ladislav Institute of Rheumatology and Department of Rheumatology, 1st Faculty of Medicine, Charles University, Prague, Czech Republic
Stensballe, Allan
Autor Stensballe, Allan ORCID Department of Health Science and Technology, Aalborg University, Aalborg, Denmark
Shelef, Miriam A
Autor Shelef, Miriam A Department of Medicine, University of Wisconsin, Madison, Wisconsin, United States of America William S. Middleton Memorial Veterans Hospital, Madison, Wisconsin, United States of America
Nielsen, Claus H
Autor Nielsen, Claus H Institute for Inflammation Research, Center for Rheumatology and Spine Diseases, Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark Section for Periodontology, Microbiology and Community Dentistry, Department of Odontology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark

PloS one. 2018 ; 13 (8) : e0203214. [epub] 20180830

PLoS One
ISSN 1932-6203
Zdroj

OBJECTIVE: Peptidylarginine deiminase 2 (PAD2) and PAD4 are expressed in the synovium of rheumatoid arthritis (RA) patients and catalyze citrullination of arginine residues in proteins targeted by anti-citrullinated protein antibodies (ACPAs). Little is known about the relative importance of PAD2 and PAD4 in generating citrullinated self-antigens. Here we investigate the ability of PAD2 and PAD4 to generate citrullinated targets for ACPAs in four human proteins. METHODS: Synovial fluid (SF) and plasma were collected from 42 RA patients. Human fibrinogen, human alpha-enolase (ENO1), human histone H3, and human serum albumin (HSA) were citrullinated in vitro by PAD2 or PAD4. The total degree of citrullination was determined using the anti-modified citrulline approach. Antibody binding to native and citrullinated proteins was measured by ELISA. RESULTS: ACPAs within pooled SF from multiple RA patients reacted equally well with, and cross-reacted with, PAD2- and PAD4-citrullinated fibrinogen. ACPAs from most individual patient SF and plasma samples bound equally well to PAD2- and PAD4-citrullinated fibrinogen or ENO1. When histone H3 was used as target, PAD4 was generally superior in generating epitopes recognized by ACPAs. No binding to citrullinated HSA was observed. CONCLUSION: In most patients, PAD2 and PAD4 are equally efficient in generating citrullinated target sites for ACPAs in fibrinogen and ENO1. The binding of autoantibodies to histone H3 was generally higher after citrullination with PAD4 than with PAD2. Citrullinated HSA is not a target for ACPAs.

Článek

Parasites & vectors. 2011 Jul 05 ; 4 () : 127. [epub] 20110705

Parasit Vectors
ISSN 1756-3305
Zdroj

BACKGROUND: Fibrinogen-related proteins with lectin activity are believed to be part of the tick innate immune system. Several fibrinogen-related proteins have been described and characterised mainly on the basis of their cDNA sequences while direct biochemical evidence is missing. One of them, the haemolymph lectin Dorin M from the tick Ornithodoros moubata was isolated and characterised in more depth. RESULTS: Several fibrinogen-related proteins were detected in the haemolymph of ixodid ticks Dermacentor marginatus, Rhipicephalus appendiculatus, R. pulchellus, and R. sanguineus. These proteins were recognised by sera directed against the tick lectin Dorin M and the haemagglutination activity of the ticks R. appendiculatus and D. marginatus. Cross-reactivity of the identified proteins with antibodies against the fibrinogen domain of the human ficolin was also shown. The carbohydrate-binding ability of tick haemolymph was confirmed by haemagglutination activity assays, and this activity was shown to be inhibited by neuraminic acid and sialylated glycoproteins as well as by N-acetylated hexosamines. The fibrinogen-related proteins were shown to be glycosylated and they were localised in salivary glands, midguts, and haemocytes of D. marginatus. Hemelipoglycoprotein was also recognised by sera directed against the fibrinogen-related proteins in all three Rhipicephalus species as well as in D. marginatus. However, this protein does not contain the fibrinogen domain and thus, the binding possibly results from the structure similarity between hemelipoglycoprotein and the fibrinogen domain. CONCLUSIONS: The presence of fibrinogen-related proteins was shown in the haemolymph of four tick species in high abundance. Reactivity of antibodies directed against ficolin or fibrinogen-related proteins with proteins which do not contain the fibrinogen domain points out the importance of sequence analysis of the identified proteins in further studies. Previously observed expression of fibrinogen-related proteins in haemocytes together with the results of this study suggest involvement of fibrinogen-related proteins in tick immunity processes. Thus, they have potential as targets for anti-tick vaccines and as antimicrobial proteins in pharmacology. Research on fibrinogen-related proteins could reveal further details of tick innate immunity processes.

MeSH
anatomické struktury zvířat chemie MeSH
Dermacentor chemie MeSH
fibrinogen imunologie MeSH
fikoliny MeSH
glykoproteiny imunologie metabolismus MeSH
hemaglutininy imunologie metabolismus MeSH
hmyzí proteiny imunologie metabolismus MeSH
lektiny imunologie metabolismus MeSH
lidé MeSH
metabolismus sacharidů MeSH
Ornithodoros chemie MeSH
protilátky imunologie MeSH
Rhipicephalus chemie MeSH
vazba proteinů MeSH
zkřížené reakce MeSH
zvířata MeSH
Check Tag
lidé MeSH
ženské pohlaví MeSH
zvířata MeSH
Publikační typ
časopisecké články MeSH
práce podpořená grantem MeSH
Názvy látek
fibrinogen MeSH
glykoproteiny MeSH
hemaglutininy MeSH
hmyzí proteiny MeSH
lektiny MeSH
protilátky MeSH

Článek

Průkaz hypoxie myokardu imunohistochemickým vysetrením
[Immunohistochemical detection of myocardial hypoxia]

Toupalík, P
Autor Toupalík, P Ustav soudního lékarství 3. LF UK, Praha

Soudni lekarstvi. 1997 May ; 42 (2) : 23-5.

Soud Lek
ISSN 0371-1854
Zdroj

Antibodies against myoglobin and fibrinogen were used for immunohistochemical investigation of myocardium in a group of 45 persons deceased of natural and violent cause. Suffocated persons showed a decrease or disappearing of myoglobin in 66% and disseminated positivity for fibrinogen in myocardial fibres in 70%. Deceased of violent cause without hypoxia had disseminated decrease or disappearing of myoglobin and simultaneous disseminated positive reaction for fibrinogen but in 14% of cases. Deceased persons with macroscopical heart infarction were used for control and had focal lack of myoglobin in 100%. Immunohistochemical investigation of myoglobin and fibrinogen can be used as a very sensitive prove of prolongated hypoxia or very intensive asphyxia when positive signs can occur after a very short period.

Článek

Comparison of several mouse and rat monoclonal antibodies against human fibrinogen

Hybridoma. 1996 Dec ; 15 (6) : 423-7.

ISSN 0272-457X
Zdroj

Six monoclonal antibodies raised against human fibrinogen have been characterized. Mouse monoclonal antibodies were targeted against sequential epitopes on the immunodominant D-domain of fibrinogen and they crossreacted with all molecules containing the D-domain [fibrin, fibrin(ogen)-degradation products]. Their behavior was not influenced by proteolytic degradation of fibrinogen with plasmin. Rat MoAbs were specific for the conformational epitopes on intact fibrinogen. Their reactivities were substantially lower with fibrin(ogen)-degradation products. Degradation of structures on intact fibrinogen was concomitant with the decay of rat MoAbs reactivity. Those structures were presumably on the C-terminal end of fibrinogen alpha chain and/or on the N-terminal end of fibrinogen beta chain.

Článek

Monoklonální protilátky proti fibrinogenu a fibrinu a proti jejich proteolytickým degradacním produktům
[Monoclonal antibodies against fibrinogen and fibrin and against their proteolytic degradation products]

Casopis lekaru ceskych. 1990 Oct 26 ; 129 (43) : 1349-51.

Cas Lek Cesk
ISSN 0008-7335
Zdroj

The level of fibrinogen (FDP) and fibrin (fDP) degradation products is one of the surprisingly few unequivocal indicators of the activity of the coagulation and fibrino (geno) lytic system. Today it is beyond doubt that, similarly as the FDP/fDP level is of unequivocal importance, traditional methods of their assessment are very equivocal. Fibrin and FDP/fDP are molecules derived from fibrinogen, which are formed from the latter as a result of a series of reactions during which structures are formed or are made available which are not present in the fibrinogen molecule. New antigenic determinants are formed, in relation to the original molecule so-called neoepitopes, neoantigens. The great predominance of monoclonal antibodies prepared in the meantime reacts with fibrinogen as well as with fibrin and their degradation products. By means of specific approaches and original methods it proved, however, possible to prepare some specific monoclonal antibodies which were successfully used in diagnostic tests in vitro; their use for detection of thrombi in vivo is tested as well as their use for an increasingly effective thrombolytic therapy after their conjugation with plasminogen activators. It may be expected that this problem will be intensely developed in the near future.