LIVIVO - Search results -

Search results

Result 1 - 10 of total 160

Search options

Book ; Online ; E-Book: The collectin protein family and its multiple biological activities

Kishore, Uday / Madan, Taruna / Sim, Robert B.

2021

Abstract: The topic of this book, Collectins, is a family of proteins whose major function is in innate immunity, where Collectins act as pattern recognition receptors (PRRs). In general they recognize targets such as microbial surfaces and apoptotic cells, and ... ...

Author's details	edited by Uday Kishore, Taruna Madan, Robert B. Sim
Abstract	The topic of this book, Collectins, is a family of proteins whose major function is in innate immunity, where Collectins act as pattern recognition receptors (PRRs). In general they recognize targets such as microbial surfaces and apoptotic cells, and once bound to a target, Collectins promote the clearance of microorganisms and damaged host tissue. New cell-surface proteins and glycoproteins, which act as Collectin receptors, are currently being identified. Some Collectins, particularly MBL, activate the complement system, which enhances the ability of antibodies to fight pathogens, via three MBL-associated proteases, the MASPs. Additionally, recent research has begun to show wider-ranging activities of Collectins, such as: · Their role in metabolism, and therefore their involvement in lifestyle diseases such as obesity and cardiovascular disease. · Their ability to modulate the adaptive immune response, as well as to recognize and trigger apoptosis of cancer cells, which makes them effective in the annihilation of cancer cells with multiple mutations. · The regulation of their expression by gonadal steroid hormones implicates them with critical roles in both male and female fertility. · Altered levels of Collectins have been associated with various autoimmune diseases. This book brings together current knowledge of the structure, functions and biological activities of Collectins, to describe their integral role in human health.
Keywords	Natural immunity ; Lectines ; Immunitat
Subject code	616.079
Language	English
Size	1 online resource (XII, 244 p. 50 illus., 45 illus. in color.)
Edition	1st ed. 2021.
Publisher	Springer
Publishing place	Cham, Switzerland
Document type	Book ; Online ; E-Book
Remark	Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
ISBN	3-030-67048-1 ; 3-030-67047-3 ; 978-3-030-67048-1 ; 978-3-030-67047-4
DOI	10.1007/978-3-030-67048-1
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

Full text online

Accessible to users with ZB MED library card

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- Full text online
- Order with fees

Book: Activators and inhibitors of complement

Sim, Robert B.

1993

Author's details	ed. by R. B. Sim
Keywords	Complement Activation ; Complement Inactivators ; Komplement ; Immunmodulator
Subject	Immunsystem ; Immunomodulator ; Immunpharmakologisches Arzneimittel ; Complement ; Komplementsystem
Language	English
Size	X, 239 S. : Ill., graph. Darst.
Publisher	Kluwer
Publishing place	Dordrecht u.a.
Publishing country	Netherlands
Document type	Book
HBZ-ID	HT006130138
ISBN	0-7923-1819-6 ; 978-0-7923-1819-4
Database	Catalogue ZB MED Medicine, Health

In stock of ZB MED Cologne/Königswinter

Shelf mark	Loan status	Location
1994 A 300	order for loan	Magazin

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: l-ficolin-MASP arm of the complement system in schizophrenia.

Mayilyan, Karine R / Krarup, Anders / Soghoyan, Armen F / Jensenius, Jens C / Sim, Robert B

Immunobiology

2023 Volume 228, Issue 2, Page(s) 152349

Abstract: The abnormal neurodevelopment secondary to in utero adversities, such as hypoxia, malnutrition and maternal infections, underlies schizophrenia (SZ) etiology. As the genes of MBL-associated serine proteases (MASP) of the complement lectin pathway, MASP1 ... ...

Abstract	The abnormal neurodevelopment secondary to in utero adversities, such as hypoxia, malnutrition and maternal infections, underlies schizophrenia (SZ) etiology. As the genes of MBL-associated serine proteases (MASP) of the complement lectin pathway, MASP1 and MASP2, are expressed in the developing cortex and are functionally important for neuronal migration, we hypothesize that the malfunction ofl-ficolin-MASP arm may also be involved in schizophrenia pathophysiology as it was shown for MBL-MASP complexes. We investigated serum l-ficolin and plasma MASP-2 levels, the activity of l-ficolin-bound MASP-2, as well as an array of the complement-related variables in chronic schizophrenic patients in the acute phase of the disease and controls without physical or mental diagnoses. The median concentration of l-ficolin in Armenian controls was 3.66 μg/ml and similar to those reported for other Caucasian populations. SZ-cases had ∼40 % increase in serum l-ficolin (median 5.08 μg/ml; P < 0.0024). In the pooled sample, l-ficolin level was higher in males than in females (P < 0.0031), but this gender dichotomy was not affecting the variable association with schizophrenia (P < 0.016). Remarkably, MASP-2 plasma concentration showed gender-dependent significant variability in the group of patients but not in controls. When adjusted for gender and gender*diagnosis interaction, a significantly high MASP-2 level in female patients versus female controls was observed (median: 362 ng/ml versus 260 ng/ml, respectively; P < 0.0020). A significant increase in l-ficolin-bound MASP-2 activity was also observed in schizophrenia (on the median, cases vs controls: 7.60 vs 6.50 RU; P < 0.021). Correlation analyses of the levels of l-ficolin and MASP-2, l-ficolin-(MASP-2) activity and the demographic data did not show any significant association with the age of individuals, family history, age at onset and duration of the illness, and smoking. Noteworthy, the levels of l-ficolin and MASP-2 in circulation were significantly associated with the type of schizophrenia (paranoid SZ-cases had much higher l-ficolin (P < 0.0035) and lower MASP-2 levels than the other types combined (P < 0.049)). Correlations were also found between: (i) the classical pathway functional activity and l-ficolin level (rs = 0.19, P < 0.010); (ii) the alternative pathway functional activity and MASP-2 level (rs = 0.26, P < 0.00035); (iii) the activity of l-ficolin-bound MASP2 and the downstream C2 component haemolytic activity (rs = -0.19, P < 0.017); and (iv) l-ficolin and the upstream C-reactive protein (CRP) serum concentrations (r = 0.28, P < 0.018). Overall, the results showed l-ficolin-related lectin pathway alterations in schizophrenia pathophysiology. It is likely that in addition to the MBL-MASP component over-activity reported previously, the alterations of the lectin pathway in schizophrenia also involve variations of l-ficolin-(MASP-2) on protein concentration and activity levels.
MeSH term(s)	Male ; Humans ; Female ; Mannose-Binding Protein-Associated Serine Proteases/metabolism ; Schizophrenia ; Lectins ; Complement Pathway, Mannose-Binding Lectin ; Complement System Proteins ; Mannose-Binding Lectin/genetics ; Ficolins
Chemical Substances	Mannose-Binding Protein-Associated Serine Proteases (EC 3.4.21.-) ; Lectins ; Complement System Proteins (9007-36-7) ; Mannose-Binding Lectin
Language	English
Publishing date	2023-02-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	563292-4
ISSN	1878-3279 ; 0171-2985
ISSN (online)	1878-3279
ISSN	0171-2985
DOI	10.1016/j.imbio.2023.152349
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ud II Zs.32: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Complement Proteins as Soluble Pattern Recognition Receptors for Pathogenic Viruses.

Murugaiah, Valarmathy / Varghese, Praveen M / Beirag, Nazar / De Cordova, Syreeta / Sim, Robert B / Kishore, Uday

Viruses

2021 Volume 13, Issue 5

Abstract: The complement system represents a crucial part of innate immunity. It contains a diverse range of soluble activators, membrane-bound receptors, and regulators. Its principal function is to eliminate pathogens via activation of three distinct pathways: ... ...

Abstract	The complement system represents a crucial part of innate immunity. It contains a diverse range of soluble activators, membrane-bound receptors, and regulators. Its principal function is to eliminate pathogens via activation of three distinct pathways: classical, alternative, and lectin. In the case of viruses, the complement activation results in effector functions such as virion opsonisation by complement components, phagocytosis induction, virolysis by the membrane attack complex, and promotion of immune responses through anaphylatoxins and chemotactic factors. Recent studies have shown that the addition of individual complement components can neutralise viruses without requiring the activation of the complement cascade. While the complement-mediated effector functions can neutralise a diverse range of viruses, numerous viruses have evolved mechanisms to subvert complement recognition/activation by encoding several proteins that inhibit the complement system, contributing to viral survival and pathogenesis. This review focuses on these complement-dependent and -independent interactions of complement components (especially C1q, C4b-binding protein, properdin, factor H, Mannose-binding lectin, and Ficolins) with several viruses and their consequences.
MeSH term(s)	Complement Activation/immunology ; Complement System Proteins/genetics ; Complement System Proteins/immunology ; Cytokine Release Syndrome ; Cytopathogenic Effect, Viral ; Humans ; Immunity, Innate ; Receptors, Pattern Recognition/immunology ; Viruses/immunology
Chemical Substances	Receptors, Pattern Recognition ; Complement System Proteins (9007-36-7)
Language	English
Publishing date	2021-05-02
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v13050824
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Enterococcus faecalis Escapes Complement-Mediated Killing via Recruitment of Complement Factor H.

Ali, Youssif M / Sim, Robert B / Schwaeble, Wilhelm / Shaaban, Mona I

The Journal of infectious diseases

2019 Volume 220, Issue 6, Page(s) 1061–1070

Abstract: Background: Enterococcus faecalis is considered to be the most important species of enterococci responsible for blood stream infections in critically ill patients. In blood, the complement system is activated via the classical pathway (CP), the lectin ... ...

Abstract	Background: Enterococcus faecalis is considered to be the most important species of enterococci responsible for blood stream infections in critically ill patients. In blood, the complement system is activated via the classical pathway (CP), the lectin pathway (LP), or the alternative pathway (AP), and it plays a critical role in opsonophagocytosis of bacteria including E faecalis. Methods: In a mouse model of enterococcus peritonitis, BALB-C mice were challenged with a high dose of E faecalis 12 hours after intraperitoneal administration of anti-Factor H (FH) antibodies or isotype control. Four hours later, control mice developed higher bacterial burden in blood and organs compared with mice treated with anti-FH antibodies. Results: We demonstrate that complement recognition molecules C1q, CL-11, and murine ficolin-A bind the enterococcus and drive the CP and the LP in human and mouse. We further describe that E faecalis evades the AP by recruitment of FH on its surface. Our results show a strong C3b deposition on E faecalis via both the CP and the LP but not through the AP. Conclusions: These findings indicate that E faecalis avoids the complement phagocytosis by the AP via sequestering complement FH from the host blood.
MeSH term(s)	Animals ; Antibodies, Bacterial/blood ; Complement C3b/immunology ; Complement C4b/immunology ; Complement Factor H/immunology ; Complement Pathway, Mannose-Binding Lectin/immunology ; Complement System Proteins/immunology ; Disease Models, Animal ; Enterococcus faecalis/immunology ; Gram-Positive Bacterial Infections/immunology ; Humans ; Lectins ; Mice ; Mice, Inbred BALB C ; Peritonitis/immunology ; Peritonitis/microbiology ; Peritonitis/pathology ; Phagocytosis/immunology ; Ficolins
Chemical Substances	Antibodies, Bacterial ; Lectins ; Complement C3b (80295-43-8) ; Complement C4b (80295-50-7) ; Complement Factor H (80295-65-4) ; Complement System Proteins (9007-36-7)
Language	English
Publishing date	2019-04-18
Publishing country	United States
Document type	Journal Article
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiz226
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uh II Zs.50: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MO 445: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Complement Proteins as Soluble Pattern Recognition Receptors for Pathogenic Viruses

Murugaiah, Valarmathy / Varghese, Praveen M / Beirag, Nazar / De Cordova, Syreeta / Sim, Robert B / Kishore, Uday

Viruses. 2021 May 02, v. 13, no. 5

2021

Abstract	The complement system represents a crucial part of innate immunity. It contains a diverse range of soluble activators, membrane-bound receptors, and regulators. Its principal function is to eliminate pathogens via activation of three distinct pathways: classical, alternative, and lectin. In the case of viruses, the complement activation results in effector functions such as virion opsonisation by complement components, phagocytosis induction, virolysis by the membrane attack complex, and promotion of immune responses through anaphylatoxins and chemotactic factors. Recent studies have shown that the addition of individual complement components can neutralise viruses without requiring the activation of the complement cascade. While the complement-mediated effector functions can neutralise a diverse range of viruses, numerous viruses have evolved mechanisms to subvert complement recognition/activation by encoding several proteins that inhibit the complement system, contributing to viral survival and pathogenesis. This review focuses on these complement-dependent and -independent interactions of complement components (especially C1q, C4b-binding protein, properdin, factor H, Mannose-binding lectin, and Ficolins) with several viruses and their consequences.
Keywords	chemotaxis ; complement ; lectins ; pathogenesis ; phagocytosis ; virion
Language	English
Dates of publication	2021-0502
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v13050824
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article ; Online: Complement Activation-Independent Attenuation of SARS-CoV-2 Infection by C1q and C4b-Binding Protein.

Beirag, Nazar / Varghese, Praveen M / Neto, Martin Mayora / Al Aiyan, Ahmad / Khan, Haseeb A / Qablan, Moneeb / Shamji, Mohamed H / Sim, Robert B / Temperton, Nigel / Kishore, Uday

Viruses

2023 Volume 15, Issue 6

Abstract: The complement system is a key component of the innate immune response to viruses and proinflammatory events. Exaggerated complement activation has been attributed to the induction of a cytokine storm in severe SARS-CoV-2 infection. However, there is ... ...

Abstract	The complement system is a key component of the innate immune response to viruses and proinflammatory events. Exaggerated complement activation has been attributed to the induction of a cytokine storm in severe SARS-CoV-2 infection. However, there is also an argument for the protective role of complement proteins, given their local synthesis or activation at the site of viral infection. This study investigated the complement activation-independent role of C1q and C4b-binding protein (C4BP) against SARS-CoV-2 infection. The interactions of C1q, its recombinant globular heads, and C4BP with the SARS-CoV-2 spike and receptor binding domain (RBD) were examined using direct ELISA. In addition, RT-qPCR was used to evaluate the modulatory effect of these complement proteins on the SARS-CoV-2-mediated immune response. Cell binding and luciferase-based viral entry assays were utilised to assess the effects of C1q, its recombinant globular heads, and C4BP on SARS-CoV-2 cell entry. C1q and C4BP bound directly to SARS-CoV-2 pseudotype particles via the RBD domain of the spike protein. C1q via its globular heads and C4BP were found to reduce binding as well as viral transduction of SARS-CoV-2 spike protein expressing lentiviral pseudotypes into transfected A549 cells expressing human ACE2 and TMPRSS2. Furthermore, the treatment of the SARS-CoV-2 spike, envelope, nucleoprotein, and membrane protein expressing alphaviral pseudotypes with C1q, its recombinant globular heads, or C4BP triggered a reduction in mRNA levels of proinflammatory cytokines and chemokines such as IL-1β, IL-8, IL-6, TNF-α, IFN-α, and RANTES (as well as NF-κB) in A549 cells expressing human ACE2 and TMPRSS2. In addition, C1q and C4BP treatment also reduced SARS-CoV-2 pseudotype infection-mediated NF-κB activation in A549 cells expressing human ACE2 and TMPRSS2. C1q and C4BP are synthesised primarily by hepatocytes; however, they are also produced by macrophages, and alveolar type II cells, respectively, locally at the pulmonary site. These findings support the notion that the locally produced C1q and C4BP can be protective against SARS-CoV-2 infection in a complement activation-independent manner, offering immune resistance by inhibiting virus binding to target host cells and attenuating the infection-associated inflammatory response.
MeSH term(s)	Humans ; Complement C4b-Binding Protein/chemistry ; Complement C4b-Binding Protein/metabolism ; Complement C1q/metabolism ; Angiotensin-Converting Enzyme 2/genetics ; Angiotensin-Converting Enzyme 2/metabolism ; NF-kappa B/metabolism ; COVID-19 ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Complement Activation ; Complement System Proteins/metabolism ; Protein Binding
Chemical Substances	Complement C4b-Binding Protein ; spike protein, SARS-CoV-2 ; Complement C1q (80295-33-6) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; NF-kappa B ; Spike Glycoprotein, Coronavirus ; Complement System Proteins (9007-36-7)
Language	English
Publishing date	2023-05-29
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v15061269
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Book: Carbon nanotubes for biomedical applications

Klingeler, Rüdiger / Sim, Robert B

(Carbon nanostructures)

2011

Author's details	Rüdiger Klingeler; Robert B. Sim eds
Series title	Carbon nanostructures
Keywords	Biomedical engineering ; Biomedical materials ; Nanomedicine ; Nanostructured materials/Therapeutic use ; Nanostructures ; Nanotechnology ; Kohlenstoff-Nanoröhre ; Biomedizin ; Multifunktionelle Verbindungen
Language	English
Size	XIX, 278 S., Ill., graph. Darst.
Publisher	Springer
Publishing place	Berlin u.a.
Document type	Book
Note	Literaturangaben
ISBN	9783642148019 ; 9783642148026 ; 3642148018 ; 3642148026
Database	Library catalogue of the German National Library of Science and Technology (TIB), Hannover

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Factor H as a regulator of the classical pathway activation.

Kishore, Uday / Sim, Robert B

Immunobiology

2012 Volume 217, Issue 2, Page(s) 162–168

Abstract: C1q, the first subcomponent of the classical pathway, is a charge pattern recognition molecule that binds a diverse range of self, non-self and altered self ligands, leading to pro-inflammatory complement activation. Although complement is required for ... ...

Abstract	C1q, the first subcomponent of the classical pathway, is a charge pattern recognition molecule that binds a diverse range of self, non-self and altered self ligands, leading to pro-inflammatory complement activation. Although complement is required for tissue homeostasis as well as defence against pathogens, exaggerated complement activation can be damaging to the tissue. Therefore, a fine balance between complement activation and inhibition is necessary. We have recently found that factor H, a polyanion recognition molecule and soluble regulator of alternative pathway activation in blood and on cell surfaces, can directly compete with C1q in binding to anionic phospholipids (cardiolipin), lipid A and Escherichia coli (three known activators of the classical pathway) and acts as a direct down regulator of the complement classical pathway. This ability of factor H to dampen classical pathway activation is distinct from its role as an alternative pathway down-regulator. Thus, by directly competing for specific C1q ligands (exogenous as well as endogenous), factor H is likely to be involved in fine-tuning and balancing the C1q-driven inflammatory processes in autoimmunity and infection. However, in the case of apoptotic cells, C1q-mediated enhancement of uptake/adhesion of the apoptotic cells by monocytes was reduced by factor H. Thus, factor H may be important in controlling the inflammation, which might arise from C1q deposition on apoptotic cells.
MeSH term(s)	Apoptosis/immunology ; Cardiolipins/immunology ; Cardiolipins/metabolism ; Complement C1q/immunology ; Complement C1q/metabolism ; Complement Factor H/immunology ; Complement Factor H/metabolism ; Complement Pathway, Classical/immunology ; Escherichia coli/immunology ; Escherichia coli/metabolism ; Humans ; Inflammation Mediators/immunology ; Inflammation Mediators/metabolism ; Lipid A/immunology ; Lipid A/metabolism
Chemical Substances	Cardiolipins ; Inflammation Mediators ; Lipid A ; Complement C1q (80295-33-6) ; Complement Factor H (80295-65-4)
Language	English
Publishing date	2012-02
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	563292-4
ISSN	1878-3279 ; 0171-2985
ISSN (online)	1878-3279
ISSN	0171-2985
DOI	10.1016/j.imbio.2011.07.024
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ud II Zs.32: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Book: Immunobiology of the shark

Smith, Sylvia L / Sim, Robert B / Flajnik, M. F

2015

Title variant	Shark
Author's details	edited by Sylvia L. Smith, Department of Biological Sciences, Florida International University; Robert B. Sim, Department of Pharmacology, University of Oxford; Martin F. Flajnik, Department of Microbiology and Immunology, University of Maryland at Baltimore
Keywords	Sharks/Immunology. ; Chondrichthyes/Immunology.
Language	English
Dates of publication	2015-2015
Size	xvii, 307 pages :, illustrations (chiefly color) ;, 26 cm
Document type	Book
ISBN	1466595744 ; 9781466595743
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

Full text online

Kategorien

Order via subito

Inter-library loan at ZB MED

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED