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Article ; Online: Identification of a common epitope in knottins and phospholipases D present in Loxosceles sp venom by a monoclonal antibody.

Alves-Mondini, Camila / Beltramino, Martina / Jiacomini, Isabella Gizzi / Karim-Silva, Sabrina / Dos Santos Antunes, Nicolle / de Moura, Juliana / Aubrey, Nicolas / Billiald, Philippe / Machado-de-Ávila, Ricardo Andrez / Alvarenga, Larissa M / Becker-Finco, Alessandra

International journal of biological macromolecules

2023 Volume 246, Page(s) 125588

Abstract: In the Americas and specially in Brazil, the Loxosceles intermedia, Loxosceles gaucho and Loxosceles laeta are the three most medically relevant brown spider species, and whose bites can lead to the condition known as loxoscelism. Here, we report the ... ...

Abstract	In the Americas and specially in Brazil, the Loxosceles intermedia, Loxosceles gaucho and Loxosceles laeta are the three most medically relevant brown spider species, and whose bites can lead to the condition known as loxoscelism. Here, we report the development of a tool capable of identifying a common epitope amongst Loxosceles sp. venom's toxins. A murine monoclonal antibody (LmAb12) and its recombinant fragments (scFv12P and diabody12P) have been produced and characterized. This antibody and its recombinant constructs were able to recognize proteins of Loxosceles spider venoms with specificity. The scFv12P variant was also able to detect low concentrations of Loxosceles venom in a competitive ELISA assay, displaying potential as a venom identification tool. The primary antigenic target of LmAb12 is a knottin, a venom neurotoxin, that has a shared identity of 100 % between the L. intermedia and L. gaucho species and high similarity to L. laeta. Furthermore, we observed LmAb12 was able to partially inhibit in vitro hemolysis, a cellular event typically induced by the Loxosceles sp. venoms. Such behavior might be due to LmAb12 cross-reactivity between the antigenic target of LmAb12 and the venom's dermonecrotic toxins, the PLDs, or even the existence of synergism between these two toxins.
MeSH term(s)	Animals ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antigens/chemistry ; Antivenins/chemistry ; Cross Reactions ; Cystine-Knot Miniproteins/chemistry ; Phospholipase D/chemistry ; Spider Venoms/chemistry ; Spiders/chemistry ; Epitopes/chemistry
Chemical Substances	Antibodies, Monoclonal ; Antigens ; Antivenins ; Cystine-Knot Miniproteins ; loxosceles venom ; Phospholipase D (EC 3.1.4.4) ; Spider Venoms ; Epitopes
Language	English
Publishing date	2023-07-01
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2023.125588
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Article ; Online: Identification of a common epitope in knottins and phospholipases D present in Loxosceles sp venom by a monoclonal antibody

Alves-Mondini, Camila / Beltramino, Martina / Jiacomini, Isabella Gizzi / Karim-Silva, Sabrina / dos Santos Antunes, Nicolle / de Moura, Juliana / Aubrey, Nicolas / Billiald, Philippe / Machado-de-Ávila, Ricardo Andrez / Alvarenga, Larissa M. / Becker-Finco, Alessandra

International Journal of Biological Macromolecules. 2023 Aug., v. 246 p.125588-

2023

Abstract	In the Americas and specially in Brazil, the Loxosceles intermedia, Loxosceles gaucho and Loxosceles laeta are the three most medically relevant brown spider species, and whose bites can lead to the condition known as loxoscelism. Here, we report the development of a tool capable of identifying a common epitope amongst Loxosceles sp. venom's toxins. A murine monoclonal antibody (LmAb12) and its recombinant fragments (scFv12P and diabody12P) have been produced and characterized. This antibody and its recombinant constructs were able to recognize proteins of Loxosceles spider venoms with specificity. The scFv12P variant was also able to detect low concentrations of Loxosceles venom in a competitive ELISA assay, displaying potential as a venom identification tool. The primary antigenic target of LmAb12 is a knottin, a venom neurotoxin, that has a shared identity of 100 % between the L. intermedia and L. gaucho species and high similarity to L. laeta. Furthermore, we observed LmAb12 was able to partially inhibit in vitro hemolysis, a cellular event typically induced by the Loxosceles sp. venoms. Such behavior might be due to LmAb12 cross-reactivity between the antigenic target of LmAb12 and the venom's dermonecrotic toxins, the PLDs, or even the existence of synergism between these two toxins.
Keywords	Loxosceles ; cross reaction ; epitopes ; hemolysis ; mice ; monoclonal antibodies ; neurotoxins ; phospholipases ; spiders ; synergism ; venoms ; Brazil ; Recombinant fragments ; Knottins ; Cross-reactivity ; Phospholipases D
Language	English
Dates of publication	2023-08
Publishing place	Elsevier B.V.
Document type	Article ; Online
ZDB-ID	282732-3
ISSN	1879-0003 ; 0141-8130
ISSN (online)	1879-0003
ISSN	0141-8130
DOI	10.1016/j.ijbiomac.2023.125588
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Article ; Online: Loxoscelism: Advances and Challenges in the Design of Antibody Fragments with Therapeutic Potential.

Karim-Silva, Sabrina / Becker-Finco, Alessandra / Jiacomini, Isabella Gizzi / Boursin, Fanny / Leroy, Arnaud / Noiray, Magali / de Moura, Juliana / Aubrey, Nicolas / Billiald, Philippe / Alvarenga, Larissa M

Toxins

2020 Volume 12, Issue 4

Abstract: Envenoming due ... ...

Abstract	Envenoming due to
MeSH term(s)	Animals ; Antibodies, Monoclonal/administration & dosage ; Antibodies, Monoclonal/immunology ; Antigens/immunology ; Antivenins/administration & dosage ; Antivenins/immunology ; Erythrocytes/drug effects ; Hemolysis/drug effects ; Humans ; Models, Molecular ; Neutralization Tests ; Single-Chain Antibodies/administration & dosage ; Single-Chain Antibodies/immunology ; Spider Bites/therapy ; Spider Venoms/adverse effects ; Spider Venoms/immunology ; Spiders/immunology
Chemical Substances	Antibodies, Monoclonal ; Antigens ; Antivenins ; Single-Chain Antibodies ; Spider Venoms
Language	English
Publishing date	2020-04-16
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2518395-3
ISSN	2072-6651 ; 2072-6651
ISSN (online)	2072-6651
ISSN	2072-6651
DOI	10.3390/toxins12040256
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Article ; Online: Acanthamoeba

Weber-Lima, Michele Martha / Prado-Costa, Bianca / Becker-Finco, Alessandra / Costa, Adriana Oliveira / Billilad, Philippe / Furst, Cinthia / de Moura, Juliana Ferreira / Alvarenga, Larissa Magalhães

Parasitology

2020 Volume 147, Issue 14, Page(s) 1678–1688

Abstract: Free-living amoeba of the genus Acanthamoeba are ubiquitous protozoa involved in opportunistic and non-opportunistic infection in humans, such as granulomatous amoebic encephalitis and amoebic keratitis. Both infections have challenging characteristics ... ...

Abstract	Free-living amoeba of the genus Acanthamoeba are ubiquitous protozoa involved in opportunistic and non-opportunistic infection in humans, such as granulomatous amoebic encephalitis and amoebic keratitis. Both infections have challenging characteristics such as the formation of the resistant cysts in infected tissues, hampering the treatment and most usual diagnosis depending on time-consuming and/or low sensitivity techniques. The use of monoclonal antibodies presents itself as an opportunity for the development of more effective alternative diagnostic methods, as well as an important and useful tool in the search for new therapeutic targets. This study investigated the possibility of using a previously produced monoclonal antibody (mAb3), as a diagnostic tool for the detection of Acanthamoeba trophozoites by direct and indirect flow cytometry and immunofluorescence. Immunoprecipitation assay and mass spectrometry allowed the isolation of the antibody's target and suggested it is a transporter part of the CPA (cation: proton antiporter) superfamily. In vitro tests indicate an important role of this target in Acanthamoeba's encystment physiology. Our results support the importance of studying the role of CPA2 transporters in the context of acanthamoebiasis, as this may be a way to identify new therapeutic candidates.
MeSH term(s)	Acanthamoeba/genetics ; Acanthamoeba/immunology ; Amebiasis/diagnosis ; Amebiasis/parasitology ; Amino Acid Sequence ; Antibodies, Monoclonal ; Antibodies, Protozoan ; Flow Cytometry ; Fluorescent Antibody Technique ; Protein Structure, Secondary ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Sequence Alignment ; Sodium-Hydrogen Exchangers/chemistry ; Sodium-Hydrogen Exchangers/genetics ; Sodium-Hydrogen Exchangers/metabolism ; Trophozoites/genetics ; Trophozoites/immunology
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Protozoan ; Protozoan Proteins ; Sodium-Hydrogen Exchangers
Language	English
Publishing date	2020-09-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	207627-5
ISSN	1469-8161 ; 0031-1820
ISSN (online)	1469-8161
ISSN	0031-1820
DOI	10.1017/S0031182020001778
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Article ; Online: Biomolecular engineering of antidehydroepiandrosterone antibodies: a new perspective in cancer diagnosis and treatment using single-chain antibody variable fragment.

Fogaça, Rafaela L / Alvarenga, Larissa M / Woiski, Thiago D / Becker-Finco, Alessandra / Teixeira, Kadima N / Silva, Sabrina K / de Moraes, Rosana N / Noronha, Lúcia de / Noiray, Magali / de Figueiredo, Bonald C / Billiald, Philippe / Moura, Juliana de

Nanomedicine (London, England)

2019 Volume 14, Issue 6, Page(s) 689–705

Abstract: Aim: To develop a monoclonal antibody against dehydroepiandrosterone (DHEA) and miniaturize it, generating a single-chain antibody variable fragment (scFv) against DHEA as an adrenocortical carcinoma (ACC) marker.: Material & methods: DHEA conjugated ...

Abstract	Aim: To develop a monoclonal antibody against dehydroepiandrosterone (DHEA) and miniaturize it, generating a single-chain antibody variable fragment (scFv) against DHEA as an adrenocortical carcinoma (ACC) marker. Material & methods: DHEA conjugated to keyhole limpet hemocyanin was used as an immunogen to obtain anti-DHEA hybridomas. Variable fragments were cloned from hybridoma 5B7 total RNA, and used to detect DHEA in normal adrenal tissue and ACC cells. Results: IgM monoclonal antibody was highly specific, and the recombinant scFv preserved parental antibody characteristics, allowing tissue localization of DHEA. Conclusion: Undefined small lesions are challenges for clinicians and impact clinical adrenocortical tumor management. Generating an anti-DHEA scFv facilitates development of imaging tests for early diagnosis of pediatric ACC.
MeSH term(s)	Adrenal Cortex Neoplasms/diagnosis ; Adrenocortical Carcinoma/diagnosis ; Animals ; Biomarkers, Tumor/analysis ; Biomarkers, Tumor/metabolism ; Dehydroepiandrosterone/analysis ; Dehydroepiandrosterone/metabolism ; Gene Expression ; Humans ; Mice, Inbred BALB C ; Molecular Docking Simulation ; Protein Conformation ; Protein Engineering/methods ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Single-Chain Antibodies/genetics ; Single-Chain Antibodies/metabolism ; Zona Reticularis/metabolism
Chemical Substances	Biomarkers, Tumor ; Recombinant Proteins ; Single-Chain Antibodies ; Dehydroepiandrosterone (459AG36T1B)
Language	English
Publishing date	2019-01-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2277839-1
ISSN	1748-6963 ; 1743-5889
ISSN (online)	1748-6963
ISSN	1743-5889
DOI	10.2217/nnm-2018-0230
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Article: Acanthamoeba spp. monoclonal antibody against a CPA2 transporter: a promising molecular tool for acanthamoebiasis diagnosis and encystment study

Parasitology. 2020 Dec., v. 147, no. 14

2020

Abstract	Free-living amoeba of the genus Acanthamoeba are ubiquitous protozoa involved in opportunistic and non-opportunistic infection in humans, such as granulomatous amoebic encephalitis and amoebic keratitis. Both infections have challenging characteristics such as the formation of the resistant cysts in infected tissues, hampering the treatment and most usual diagnosis depending on time-consuming and/or low sensitivity techniques. The use of monoclonal antibodies presents itself as an opportunity for the development of more effective alternative diagnostic methods, as well as an important and useful tool in the search for new therapeutic targets. This study investigated the possibility of using a previously produced monoclonal antibody (mAb3), as a diagnostic tool for the detection of Acanthamoeba trophozoites by direct and indirect flow cytometry and immunofluorescence. Immunoprecipitation assay and mass spectrometry allowed the isolation of the antibody's target and suggested it is a transporter part of the CPA (cation: proton antiporter) superfamily. In vitro tests indicate an important role of this target in Acanthamoeba's encystment physiology. Our results support the importance of studying the role of CPA2 transporters in the context of acanthamoebiasis, as this may be a way to identify new therapeutic candidates.
Keywords	Acanthamoeba ; antiporters ; cations ; diagnostic techniques ; encephalitis ; encystment ; flow cytometry ; fluorescent antibody technique ; keratitis ; mass spectrometry ; monoclonal antibodies ; parasitology ; precipitin tests ; therapeutics ; trophozoites
Language	English
Dates of publication	2020-12
Size	p. 1678-1688.
Publishing place	Cambridge University Press
Document type	Article
Note	NAL-light
ZDB-ID	207627-5
ISSN	1469-8161 ; 0031-1820
ISSN (online)	1469-8161
ISSN	0031-1820
DOI	10.1017/S0031182020001778
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Loxoscelism

Sabrina Karim-Silva / Alessandra Becker-Finco / Isabella Gizzi Jiacomini / Fanny Boursin / Arnaud Leroy / Magali Noiray / Juliana de Moura / Nicolas Aubrey / Philippe Billiald / Larissa M. Alvarenga

Toxins, Vol 12, Iss 256, p

Advances and Challenges in the Design of Antibody Fragments with Therapeutic Potential

2020 Volume 256

Abstract: Envenoming due to Loxosceles spider bites still remains a neglected disease of particular medical concern in the Americas. To date, there is no consensus for the treatment of envenomed patients, yet horse polyclonal antivenoms are usually infused to ... ...

Abstract	Envenoming due to Loxosceles spider bites still remains a neglected disease of particular medical concern in the Americas. To date, there is no consensus for the treatment of envenomed patients, yet horse polyclonal antivenoms are usually infused to patients with identified severe medical conditions. It is widely known that venom proteins in the 30–35 kDa range with sphingomyelinase D (SMasesD) activity, reproduce most of the toxic effects observed in loxoscelism. Hence, we believe that monoclonal antibody fragments targeting such toxins might pose an alternative safe and effective treatment. In the present study, starting from the monoclonal antibody LimAb7, previously shown to target SMasesD from the venom of L. intermedia and neutralize its dermonecrotic activity, we designed humanized antibody V-domains, then produced and purified as recombinant single-chain antibody fragments (scFvs). These molecules were characterized in terms of humanness, structural stability, antigen-binding activity, and venom-neutralizing potential. Throughout this process, we identified some blocking points that can impact the Abs antigen-binding activity and neutralizing capacity. In silico analysis of the antigen/antibody amino acid interactions also contributed to a better understanding of the antibody’s neutralization mechanism and led to reformatting the humanized antibody fragment which, ultimately, recovered the functional characteristics for efficient in vitro venom neutralization.
Keywords	venom ; antivenom ; neutralization ; loxosceles ; sphingomyelinase D ; humanization ; Medicine ; R
Subject code	570
Language	English
Publishing date	2020-04-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article: Generation and characterization of monoclonal antibody against Advanced Glycation End Products in chronic kidney disease.

Finco, Alessandra Becker / Machado-de-Ávila, Ricardo Andrez / Maciel, Rayana / De Moura, Juliana / Billiald, Philippe / Stinghen, Andrea Emilia Marques / Alvarenga, Larissa M

Biochemistry and biophysics reports

2016 Volume 6, Page(s) 142–148

Abstract: Advanced Glycation End Products (AGEs) are toxins that are involved in structural and functional alterations of several organs and tissues, resulting in various pathologies. Several types of AGEs have been described but carboxymethyllysine (CML) is the ... ...

Abstract	Advanced Glycation End Products (AGEs) are toxins that are involved in structural and functional alterations of several organs and tissues, resulting in various pathologies. Several types of AGEs have been described but carboxymethyllysine (CML) is the major antigenic AGE compound. In this study, three different immunogenic carrier proteins (KLH, keyhole limpet hemocyanin; BSA, bovine serum albumin; and HSA, human serum albumin) were modified by glycation. The glycated molecules were used to produce epitope-specific monoclonal antibodies able to recognize the CML domain and to detect uremic toxins in the serum of patients with chronic kidney disease (CKD). A competitive ELISA was standardized in order to quantify CML in the sera of CKD patients. An increase in uremic toxins can compromise the clinical condition of these patients, thus, the detection and quantification of these toxins should contribute to a better management and understanding of this disease.
Language	English
Publishing date	2016-03-23
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2831046-9
ISSN	2405-5808
ISSN	2405-5808
DOI	10.1016/j.bbrep.2016.03.011
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Article ; Online: p-cresol but not p-cresyl sulfate stimulate MCP-1 production via NF-κB p65 in human vascular smooth muscle cells.

Maciel, Rayana Ariane Pereira / Rempel, Lisienny Campoli Tono / Bosquetti, Bruna / Finco, Alessandra Becker / Pecoits-Filho, Roberto / Souza, Wesley Mauricio de / Stinghen, Andréa Emilia Marques

Jornal brasileiro de nefrologia : 'orgao oficial de Sociedades Brasileira e Latino-Americana de Nefrologia

2016 Volume 38, Issue 2, Page(s) 153–160

Abstract: Introduction: p-cresol (PC) and p-cresyl sulfate (PCS) are responsible for many of the uremia clinical consequences, such as atherosclerosis in Chronic Kidney Disease (CKD) patients.: Objectives: We investigate the in vitro impact of PC and PCS on ... ...

Title translation	p-cresol mas não p-cresil sulfato estimulam a produção de MCP-1 via NF-κB p65 em células vasculares musculares lisas humanas.
Abstract	Introduction: p-cresol (PC) and p-cresyl sulfate (PCS) are responsible for many of the uremia clinical consequences, such as atherosclerosis in Chronic Kidney Disease (CKD) patients. Objectives: We investigate the in vitro impact of PC and PCS on monocyte chemoattractant protein-1 (MCP-1) expression via NF-kappa B (NF-κB) p65 in VSMC. Methods: PCS was synthesized by PC sulfatation. VSMC were extracted by enzymatic digestion of umbilical cord vein and characterized by immunofluorescence against α-actin antibody. The cells were treated with PC and PCS at their normal (n), uremic (u) and maximum uremic concentrations (m). Cell viability was assessed by MTT. MCP-1 expression was investigated by ELISA in cells supernatants after toxins treatment with or without the NF-κB p65 inhibitor. Results: There was no significant difference in cell viability after toxins treatment for all concentrations tested. There was a significant increase in MCP-1 expression in cells treated with PCu and PCm (p < 0.001) and PCSn, PCSu and PCSm (p < 0.001), compared with the control. When VSMC were treated with the NF-κB p65 inhibitor plus PCu and PCm, there was a significant decrease in MCP-1 production (p < 0.005). This effect was not observed with PCS. Conclusions: VSMC are involved in atherosclerosis lesion formation and production of MCP-1, which contributes to the inflammatory response initiation. Our results suggest that PC mediates MCP-1 production in VSMC, probably through NF-κB p65 pathway, although we hypothesize that PCS acts through a different subunit pathway since NF-κB p65 inhibitor was not able to inhibit MCP-1 production.
Language	Portuguese
Publishing date	2016-06
Publishing country	Brazil
Document type	Journal Article
ZDB-ID	2057873-8
ISSN	2175-8239 ; 0101-2800
ISSN (online)	2175-8239
ISSN	0101-2800
DOI	10.5935/0101-2800.20160024
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Article: Sevelamer reduces endothelial inflammatory response to advanced glycation end products.

Gregório, Paulo C / Favretto, Giane / Sassaki, Guilherme L / Cunha, Regiane S / Becker-Finco, Alessandra / Pecoits-Filho, Roberto / Souza, Wesley M / Barreto, Fellype C / Stinghen, Andréa E M

Clinical kidney journal

2017 Volume 11, Issue 1, Page(s) 89–98

Abstract: Background: Advanced glycation end products (AGEs) have been related to the pathogenesis of cardiovascular diseases (CVD), chronic kidney disease (CKD) and diabetes mellitus. We sought to investigate the binding capacity of sevelamer to both AGEs and ... ...

Abstract	Background: Advanced glycation end products (AGEs) have been related to the pathogenesis of cardiovascular diseases (CVD), chronic kidney disease (CKD) and diabetes mellitus. We sought to investigate the binding capacity of sevelamer to both AGEs and uremic serum Methods: AGEs were prepared by albumin glycation and characterized by absorbance and electrophoresis. Human endothelial cells were incubated in culture media containing AGEs and uremic serum with or without sevelamer. Receptor for advanced glycation end product (RAGE) expression was evaluated through immunocytochemistry and western blot to explore the interactions between AGEs and the endothelium. Inflammatory and endothelial dysfunction biomarkers, such as interleukin 6 (IL-6) and IL-8, monocyte chemoattractant protein-1 (MCP-1), plasminogen activator inhibitor-1 (PAI-1) and serum amyloid A (SAA) were also measured in cell supernatant. The chemotactic property of the supernatant was evaluated. Results: AGEs significantly induced the expression of RAGE, inflammatory and endothelial activation biomarkers [IL-6, (P Conclusions: Sevelamer decreased both endothelial expression of RAGE and endothelial dysfunction biomarkers, induced by AGEs, and uremic serum. Further studies are necessary for a better understanding of the potential protective role of sevelamer on uremic serum and AGEs-mediated endothelial dysfunction.
Language	English
Publishing date	2017-09-05
Publishing country	England
Document type	Journal Article
ZDB-ID	2655800-2
ISSN	2048-8513 ; 2048-8505
ISSN (online)	2048-8513
ISSN	2048-8505
DOI	10.1093/ckj/sfx074
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