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Article ; Online: Sequence similarity of HSP65 of Mycobacterium bovis BCG with SARS-CoV-2 spike and nuclear proteins: may it predict an antigen-dependent immune protection of BCG against COVID-19?

Finotti, Paola

2021 Volume 27, Issue 1, Page(s) 37–43

Abstract: The Bacillus Calmette-Guérin (BCG) vaccine is known to have protective effects not only against tuberculosis but also against other unrelated infectious diseases caused by different pathogens. Several epidemiological studies have also documented the ... ...

Abstract	The Bacillus Calmette-Guérin (BCG) vaccine is known to have protective effects not only against tuberculosis but also against other unrelated infectious diseases caused by different pathogens. Several epidemiological studies have also documented the beneficial influence of BCG vaccine in reducing both susceptibility to and severity of SARS-CoV-2 infection. The protective, non-specific effects of BCG vaccination would be related to an antigen-independent enhancement of the innate immunity, termed trained immunity. However, the knowledge that heat shock protein (HSP)65 is the main antigen of Mycobacterium bovis BCG prompted us to verify whether sequence similarity existed between HSP65 and SARS-CoV-2 spike (S) and nuclear (N) proteins that could support an antigen-driven immune protection of BCG vaccine. The results of the in silico investigation showed an extensive sequence similarity of HSP65 with both the viral proteins, especially SARS-CoV-2 S, that also involved the regions comprising immunodominant epitopes. The finding that the predicted B cell and CD4
MeSH term(s)	BCG Vaccine/immunology ; BCG Vaccine/pharmacology ; COVID-19/immunology ; COVID-19/prevention & control ; Heat-Shock Proteins/immunology ; Humans ; Immunity, Innate/immunology ; Mycobacterium bovis/immunology ; Mycobacterium bovis/virology ; Nuclear Proteins/immunology ; SARS-CoV-2/immunology
Chemical Substances	BCG Vaccine ; Heat-Shock Proteins ; Nuclear Proteins ; heat-shock protein 65, human
Language	English
Publishing date	2021-11-09
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1362749-1
ISSN	1466-1268 ; 1355-8145
ISSN (online)	1466-1268
ISSN	1355-8145
DOI	10.1007/s12192-021-01244-y
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Article ; Online: A mutant α1antitrypsin in complex with heat shock proteins as the primary antigen in type 1 diabetes in silico investigation.

Finotti, Paola / Pagetta, Andrea

Scientific reports

2021 Volume 11, Issue 1, Page(s) 3002

Abstract: Based on previous results demonstrating that complexes of a mutant α1-antitrypsin with the heat shock proteins (HSP)70 and glucose-regulated protein94 (Grp94) circulate in the blood of patients with type 1 diabetes, we raised the hypothesis that these ... ...

Abstract	Based on previous results demonstrating that complexes of a mutant α1-antitrypsin with the heat shock proteins (HSP)70 and glucose-regulated protein94 (Grp94) circulate in the blood of patients with type 1 diabetes, we raised the hypothesis that these complexes could represent the primary antigen capable of triggering the autoimmune reactions leading to overt diabetes. As a first approach to this issue, we searched whether A1AT and HSPs had a sequence similarity to major islet antigen proteins so as to identify among the similar sequences those with potential relevance for the pathogenesis of diabetes. A thorough in silico analysis was performed to establish the score of similarity of the human proteins: A1AT, pro-insulin (INS), GAD65, IAPP, IA-2, ICA69, Grp94, HSP70 and HSP60. The sequences of A1AT and HSPs with the highest score of similarity to the islet peptides reported in the literature as the main autoantigens in human diabetes were recorded. At variance with other HSPs, also including HSP90 and Grp78, Grp94 contained the highest number and the longest sequences with structural similarity to A1AT and to well-known immunogenic peptides/epitopes of INS, GAD65, and IA-2. The similarity of A1AT with Grp94 and that of Grp94 with INS also suggested a functional relationship among the proteins. Specific sequences were identified in A1AT, Grp94 and HSP70, with the highest score of cross-similarity to a pattern of eight different islet protein epitopes. The similarity also involved recently discovered autoantigens in type 1 diabetes such as a hybrid peptides of insulin and the defective ribosomal insulin gene product. The significant similarity displayed by specific sequences of Grp94 and A1AT to the islet peptides considered main antigens in human diabetes, is a strong indication for testing these sequences as new peptides of immunogenic relevance in diabetes.
MeSH term(s)	Antigens/genetics ; Antigens/immunology ; Computer Simulation ; Diabetes Mellitus, Type 1/genetics ; Diabetes Mellitus, Type 1/immunology ; Diabetes Mellitus, Type 1/pathology ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/immunology ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins/immunology ; Humans ; Insulin/metabolism ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/immunology ; Molecular Chaperones/genetics ; Molecular Chaperones/immunology ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/genetics ; alpha 1-Antitrypsin/chemistry ; alpha 1-Antitrypsin/genetics ; alpha 1-Antitrypsin/immunology
Chemical Substances	Antigens ; HSP70 Heat-Shock Proteins ; Heat-Shock Proteins ; Insulin ; Membrane Glycoproteins ; Molecular Chaperones ; Multiprotein Complexes ; alpha 1-Antitrypsin ; endoplasmin
Language	English
Publishing date	2021-02-04
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-82730-2
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Article ; Online: A mutant α1antitrypsin in complex with heat shock proteins as the primary antigen in type 1 diabetes in silico investigation

Paola Finotti / Andrea Pagetta

Scientific Reports, Vol 11, Iss 1, Pp 1-

2021 Volume 14

Abstract: Abstract Based on previous results demonstrating that complexes of a mutant α1-antitrypsin with the heat shock proteins (HSP)70 and glucose-regulated protein94 (Grp94) circulate in the blood of patients with type 1 diabetes, we raised the hypothesis that ...

Abstract	Abstract Based on previous results demonstrating that complexes of a mutant α1-antitrypsin with the heat shock proteins (HSP)70 and glucose-regulated protein94 (Grp94) circulate in the blood of patients with type 1 diabetes, we raised the hypothesis that these complexes could represent the primary antigen capable of triggering the autoimmune reactions leading to overt diabetes. As a first approach to this issue, we searched whether A1AT and HSPs had a sequence similarity to major islet antigen proteins so as to identify among the similar sequences those with potential relevance for the pathogenesis of diabetes. A thorough in silico analysis was performed to establish the score of similarity of the human proteins: A1AT, pro-insulin (INS), GAD65, IAPP, IA-2, ICA69, Grp94, HSP70 and HSP60. The sequences of A1AT and HSPs with the highest score of similarity to the islet peptides reported in the literature as the main autoantigens in human diabetes were recorded. At variance with other HSPs, also including HSP90 and Grp78, Grp94 contained the highest number and the longest sequences with structural similarity to A1AT and to well-known immunogenic peptides/epitopes of INS, GAD65, and IA-2. The similarity of A1AT with Grp94 and that of Grp94 with INS also suggested a functional relationship among the proteins. Specific sequences were identified in A1AT, Grp94 and HSP70, with the highest score of cross-similarity to a pattern of eight different islet protein epitopes. The similarity also involved recently discovered autoantigens in type 1 diabetes such as a hybrid peptides of insulin and the defective ribosomal insulin gene product. The significant similarity displayed by specific sequences of Grp94 and A1AT to the islet peptides considered main antigens in human diabetes, is a strong indication for testing these sequences as new peptides of immunogenic relevance in diabetes.
Keywords	Medicine ; R ; Science ; Q
Subject code	616
Language	English
Publishing date	2021-02-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article ; Online: Effects of purine-scaffold inhibitors on HUVECs: Involvement of the purinergic pathway and interference with ATP. Implications for preventing the adverse effects of extracellular Grp94.

Tramentozzi, Elisa / Finotti, Paola

Biochemistry and biophysics reports

2019 Volume 19, Page(s) 100661

Abstract: Background: Extracellular Glucose-regulated protein94 (Grp94) is linked to pathological conditions disrupting the obligatory intracellular location of this Heat Shock Protein (HSP). In plasma, Grp94 is linked to IgG in complexes that drive adverse ... ...

Abstract	Background: Extracellular Glucose-regulated protein94 (Grp94) is linked to pathological conditions disrupting the obligatory intracellular location of this Heat Shock Protein (HSP). In plasma, Grp94 is linked to IgG in complexes that drive adverse effects on vascular cells and are biomarker of gastro-intestinal cancer. By blocking ATP site in different HSPs, purine-scaffold inhibitors are used as promising anti-cancer compounds, but their effects on vasculature are not known. Methods: We tested the capacity of two purine-scaffold inhibitors, PU-H71 and PU-WS13, to prevent the binding of Grp94 to IgG and to antagonize the effects of Grp94 and native Grp94-IgG complexes on HUVECs in different experimental conditions. Results: PU-H71 and PU-WS13 blocked Grp94 and the formation of Grp94-IgG complexes in absence of cells. Instead, in presence of HUVECs rather than Grp94 PU-inhibitors targeted cells causing stimulation of Akt and VEGF pathways and displaying angiogenic-like effects similar to, although less intense than that provoked by Grp94 and Grp94-IgG complexes. Unlike Grp94 and Grp94-IgG complexes, PU-inhibitors also activated the purinergic pathway and increased the expression of the ATP receptor P2X7. Effects of PU-inhibitors on HUVECs were reversed by ATP and in presence of ATP PU-inhibitors were again able to block Grp94. Conclusions: PU-inhibitors can display direct effects on endothelial cells by targeting the ATP receptor P2X7. In absence of ATP, PU-inhibitors preferentially bind to cells rather than Grp94. ATP antagonizes the PU-inhibitor binding to cells thus restoring the capacity to block Grp94 and Grp94-IgG complex formation. Results have implications for enhancing the therapeutic efficacy of PU-inhibitors against circulating pathogenic Grp94.
Language	English
Publishing date	2019-07-03
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2831046-9
ISSN	2405-5808 ; 2405-5808
ISSN (online)	2405-5808
ISSN	2405-5808
DOI	10.1016/j.bbrep.2019.100661
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Article ; Online: Synergistic Effects of A Combined Treatment of Glioblastoma U251 Cells with An Anti-miR-10b-5p Molecule and An AntiCancer Agent Based on 1-(3',4',5'-Trimethoxyphenyl)-2-Aryl-1

Zurlo, Matteo / Romagnoli, Romeo / Oliva, Paola / Gasparello, Jessica / Finotti, Alessia / Gambari, Roberto

International journal of molecular sciences

2022 Volume 23, Issue 11

Abstract: 1) Background: In the development of new and more effective anticancer approaches, combined treatments appear of great interest. Combination therapy could be of importance in the management of glioblastoma (GBM), a lethal malignancy that accounts for 42% ...

Abstract	(1) Background: In the development of new and more effective anticancer approaches, combined treatments appear of great interest. Combination therapy could be of importance in the management of glioblastoma (GBM), a lethal malignancy that accounts for 42% of cancer of the central nervous system, with a median survival of 15 months. This study aimed to verify the activity on a glioblastoma cancer cell line of one of the most active compounds of a novel series of tubulin polymerization inhibitors based on the 1-(3',4',5'-trimethoxyphenyl)-2-aryl-1
MeSH term(s)	Antagomirs ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Brain Neoplasms/metabolism ; Cell Line, Tumor ; Cell Proliferation ; Gene Expression Regulation, Neoplastic ; Glioblastoma/drug therapy ; Glioblastoma/genetics ; Glioblastoma/metabolism ; Humans ; Imidazoles/pharmacology ; MicroRNAs/metabolism
Chemical Substances	Antagomirs ; Antineoplastic Agents ; Imidazoles ; MicroRNAs
Language	English
Publishing date	2022-05-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23115991
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Article ; Online: Effects of purine-scaffold inhibitors on HUVECs

Elisa Tramentozzi / Paola Finotti

Biochemistry and Biophysics Reports, Vol 19, Iss , Pp - (2019)

Involvement of the purinergic pathway and interference with ATP. Implications for preventing the adverse effects of extracellular Grp94

2019

Abstract	Background: Extracellular Glucose-regulated protein94 (Grp94) is linked to pathological conditions disrupting the obligatory intracellular location of this Heat Shock Protein (HSP). In plasma, Grp94 is linked to IgG in complexes that drive adverse effects on vascular cells and are biomarker of gastro-intestinal cancer. By blocking ATP site in different HSPs, purine-scaffold inhibitors are used as promising anti-cancer compounds, but their effects on vasculature are not known. Methods: We tested the capacity of two purine-scaffold inhibitors, PU-H71 and PU-WS13, to prevent the binding of Grp94 to IgG and to antagonize the effects of Grp94 and native Grp94-IgG complexes on HUVECs in different experimental conditions. Results: PU-H71 and PU-WS13 blocked Grp94 and the formation of Grp94-IgG complexes in absence of cells. Instead, in presence of HUVECs rather than Grp94 PU-inhibitors targeted cells causing stimulation of Akt and VEGF pathways and displaying angiogenic-like effects similar to, although less intense than that provoked by Grp94 and Grp94-IgG complexes. Unlike Grp94 and Grp94-IgG complexes, PU-inhibitors also activated the purinergic pathway and increased the expression of the ATP receptor P2X7. Effects of PU-inhibitors on HUVECs were reversed by ATP and in presence of ATP PU-inhibitors were again able to block Grp94. Conclusions: PU-inhibitors can display direct effects on endothelial cells by targeting the ATP receptor P2X7. In absence of ATP, PU-inhibitors preferentially bind to cells rather than Grp94. ATP antagonizes the PU-inhibitor binding to cells thus restoring the capacity to block Grp94 and Grp94-IgG complex formation. Results have implications for enhancing the therapeutic efficacy of PU-inhibitors against circulating pathogenic Grp94. Keywords: Endothelial cells, Purine-based inhibitors, Heat shock proteins, Angiogenic proteins, Signal transduction pathways
Keywords	Biology (General) ; QH301-705.5 ; Biochemistry ; QD415-436
Subject code	500
Language	English
Publishing date	2019-09-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: Synergistic Effects of A Combined Treatment of Glioblastoma U251 Cells with An Anti-miR-10b-5p Molecule and An AntiCancer Agent Based on 1-(3′,4′,5′-Trimethoxyphenyl)-2-Aryl-1 H -Imidazole Scaffold

Matteo Zurlo / Romeo Romagnoli / Paola Oliva / Jessica Gasparello / Alessia Finotti / Roberto Gambari

International Journal of Molecular Sciences, Vol 23, Iss 5991, p

2022 Volume 5991

Abstract	(1) Background: In the development of new and more effective anticancer approaches, combined treatments appear of great interest. Combination therapy could be of importance in the management of glioblastoma (GBM), a lethal malignancy that accounts for 42% of cancer of the central nervous system, with a median survival of 15 months. This study aimed to verify the activity on a glioblastoma cancer cell line of one of the most active compounds of a novel series of tubulin polymerization inhibitors based on the 1-(3′,4′,5′-trimethoxyphenyl)-2-aryl-1 H -imidazole scaffold, used in combination with a miRNA inhibitor molecule targeting the oncomiRNA miR-10b-5p. This microRNA was selected in consideration of the role of miR-10b-5p on the onset and progression of glioblastoma. (2) Methods: Apoptosis was analyzed by Annexin-V and Caspase 3/7 assays, efficacy of the anti-miR-10b-5p was assessed by determining the miR-10b-5p content by RT-qPCR. (3) Results: The results obtained show that a “combination therapy” performed by combining the use of an anti-miR-10b-5p and a 1-(3′,4′,5′-trimethoxyphenyl)-2-aryl-1 H -imidazole derivative is an encouraging strategy to boost the efficacy of anticancer therapies and at the same time to reduce side effects.
Keywords	microRNA ; anti-miR ; miR-10b-5p ; glioma ; apoptosis ; tubulin ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	570
Language	English
Publishing date	2022-05-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Synergistic effects of the combined treatment of U251 and T98G glioma cells with an anti‑tubulin tetrahydrothieno[2,3‑c]pyridine derivative and a peptide nucleic acid targeting miR‑221‑3p.

Zurlo, Matteo / Romagnoli, Romeo / Oliva, Paola / Gasparello, Jessica / Finotti, Alessia / Gambari, Roberto

International journal of oncology

2021 Volume 59, Issue 2

Abstract: In the development of novel and more effective anticancer approaches, combined treatments appear to be of great interest, based on the possibility of obtaining relevant biological or therapeutic effects using lower concentrations of single drugs. ... ...

Abstract	In the development of novel and more effective anticancer approaches, combined treatments appear to be of great interest, based on the possibility of obtaining relevant biological or therapeutic effects using lower concentrations of single drugs. Combination therapy may prove to be of utmost significance in the management of glioblastoma (GBM), a lethal malignancy that accounts for 42% of cancer cases of the central nervous system, with a median survival rate of 15 months. As regards novel therapeutic approaches, the authors have recently demonstrated that peptide nucleic acids (PNAs) that target microRNA (miRNA/miR)‑221 are very active in inducing the apoptosis of glioma cells. Furthermore, in a recent study, the authors described two novel series of tubulin polymerization inhibitors based on the 4,5,6,7‑tetrahydrothieno[2,3‑c]pyridine and 4,5,6,7‑tetrahydrobenzo[b]thiophene scaffold, which exerted a potent anti‑proliferative effect on a variety of tumor cell lines. The present study aimed to verify the activity on glioblastoma cancer cell lines of one of the most active compounds tested, corresponding to 2‑(3', 4', 5'‑trimethoxyanilino)‑3‑cyano/alkoxycarbonyl‑6‑substituted‑4 5,6,7‑tetrahydrothiene[2,3‑c] pyridine (compound 3b), used in combination with an anti‑miR‑221‑3p PNA, already demonstrated to be able to induce high levels of apoptosis. To the best of our knowledge, the results obtained herein demonstrate for the first time a 'combination therapy' performed by the combined use of a PNA targeting miR‑221 and the tetrahydrothiene[2,3‑c]pyridine derivative 3b, supporting the concept that the combined treatment of GBM cells with a PNA against a specific upregulated oncomiRNA (in the present study a PNA targeting miR‑221‑3p was used) and anti‑tubulin agents (in the present study derivative 3b was used) is an encouraging strategy which may be used to enhance the efficacy of anticancer therapies and at the same time, to reduce side‑effects.
MeSH term(s)	Brain Neoplasms/drug therapy ; Brain Neoplasms/genetics ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Cell Survival/drug effects ; Drug Synergism ; Gene Expression Regulation, Neoplastic/drug effects ; Glioma/drug therapy ; Glioma/genetics ; Humans ; MicroRNAs/genetics ; Peptide Nucleic Acids/pharmacology ; Pyridines/pharmacology ; Tubulin Modulators/pharmacology ; Up-Regulation/drug effects
Chemical Substances	MIRN221 microRNA, human ; MicroRNAs ; Peptide Nucleic Acids ; Pyridines ; Tubulin Modulators
Language	English
Publishing date	2021-07-19
Publishing country	Greece
Document type	Journal Article
ZDB-ID	1154403-x
ISSN	1791-2423 ; 1019-6439
ISSN (online)	1791-2423
ISSN	1019-6439
DOI	10.3892/ijo.2021.5241
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Article: The role played by serine proteases in the development and worsening of vascular complications in type 1 diabetes mellitus.

Finotti, Paola

Current diabetes reviews

2008 Volume 2, Issue 3, Page(s) 295–305

Abstract: Much attention has been given to the role played by serine proteases in the development and worsening of vascular complications in Type 1 diabetes mellitus. A generalized increase in proteolytic activity, either due to a true increase in concentration of ...

Abstract	Much attention has been given to the role played by serine proteases in the development and worsening of vascular complications in Type 1 diabetes mellitus. A generalized increase in proteolytic activity, either due to a true increase in concentration of specific proteases or defects of their protease inhibitors, represents an early marker of diabetes. However, the precise molecular mechanism whereby an unopposed proteolytic activity leads to overt vascular alterations has not fully been elucidated as yet. The picture is further complicated by the fact that, although sharing the same function, serine proteases constitute a structurally heterogeneous class of molecules. Besides classical proteases, for most part belonging to coagulative and fibrinolytic systems, other unrelated molecules exhibit serine-like protease activity and are capable of triggering both inflammatory and immune reactions. The specific role of these non classical serine proteases in the complex pathogenesis of diabetes and its vascular complications is attracting a new investigative interest, as these molecules may represent additional therapeutic targets. This review will focus on most recent acquisitions on this issue relevant to Type 1 diabetes.
MeSH term(s)	Antibody Formation ; Cell Division ; Diabetes Mellitus, Type 1/complications ; Diabetes Mellitus, Type 1/enzymology ; Diabetic Angiopathies/enzymology ; Diabetic Angiopathies/immunology ; Heat-Shock Proteins/physiology ; Humans ; Immunity, Cellular ; Immunoglobulins/physiology ; Inflammation/immunology ; Inflammation/physiopathology ; Models, Biological ; Muscle, Smooth, Vascular/cytology ; Muscle, Smooth, Vascular/physiology ; Serine Endopeptidases/metabolism
Chemical Substances	Heat-Shock Proteins ; Immunoglobulins ; Serine Endopeptidases (EC 3.4.21.-)
Language	English
Publishing date	2008-01-02
Publishing country	United Arab Emirates
Document type	Journal Article ; Review
ISSN	1573-3998
ISSN	1573-3998
DOI	10.2174/157339906777950624
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Article ; Online: Proteomic Investigation on Grp94-IgG Complexes Circulating in Plasma of Type 1 Diabetic Subjects.

Roveri, Antonella / Zaccarin, Mattia / Pagetta, Andrea / Tramentozzi, Elisa / Finotti, Paola

Journal of diabetes research

2015 Volume 2015, Page(s) 815839

Abstract: The glucose-regulated protein94 (Grp94) has been found in complexes with IgG in plasma of Type 1 (T1) diabetic subjects; however, the pathogenetic meaning of Grp94-IgG complexes has not yet been elucidated. To shed light on the nature and structure of ... ...

Abstract	The glucose-regulated protein94 (Grp94) has been found in complexes with IgG in plasma of Type 1 (T1) diabetic subjects; however, the pathogenetic meaning of Grp94-IgG complexes has not yet been elucidated. To shed light on the nature and structure of these complexes in vivo, we conducted a proteomic analysis on plasma of both T1 diabetic subjects and healthy control subjects. IgG purified from plasma was submitted to 2D PAGE followed by Western blotting and mass analysis. Grp94 was detected in plasma of all diabetic but not control subjects and found linked with its N-terminus to the IgG heavy chain. Mass analysis of heavy chain of IgG that binds Grp94 also in vitro, forming stable complexes with characteristics similar to those of native ones, permitted identifying CH2 and CH3 regions as those involved in binding Grp94. At the electron microscopy, IgG from diabetic plasma appeared as fibrils of various lengthes and dimensions, suggestive of elevated aggregating tendency conferred to IgG by Grp94. The nonimmune nature of complexes turned out to be responsible for the particular stability and structure adopted by complexes in plasma of diabetic subjects. Results are of relevance to understanding the pathogenetic mechanisms underlying diabetes and its complications.
MeSH term(s)	Adult ; Blotting, Western ; Case-Control Studies ; Diabetes Mellitus, Type 1/blood ; Electrophoresis, Gel, Two-Dimensional ; Female ; Humans ; Immunoglobulin G/blood ; Immunoglobulin G/metabolism ; Immunoglobulin G/ultrastructure ; Immunoglobulin Heavy Chains/metabolism ; Male ; Membrane Glycoproteins/blood ; Membrane Glycoproteins/metabolism ; Membrane Glycoproteins/ultrastructure ; Microscopy, Electron ; Multiprotein Complexes/blood ; Multiprotein Complexes/metabolism ; Multiprotein Complexes/ultrastructure ; Proteomics ; Young Adult
Chemical Substances	Immunoglobulin G ; Immunoglobulin Heavy Chains ; Membrane Glycoproteins ; Multiprotein Complexes ; endoplasmin
Language	English
Publishing date	2015-06-08
Publishing country	England
Document type	Journal Article
ZDB-ID	2711897-6
ISSN	2314-6753 ; 2314-6745
ISSN (online)	2314-6753
ISSN	2314-6745
DOI	10.1155/2015/815839
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