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Search Results: 1 - 10 of 3572 matches for " Jens Jensenius "
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Mannan-binding lectin in cerebrospinal fluid: a leptomeningeal protein
Hansotto Reiber, Barbara Padilla-Docal, Jens Jensenius, Alberto Dorta-Contreras
Fluids and Barriers of the CNS , 2012, DOI: 10.1186/2045-8118-9-17
Abstract: MBL was assayed in samples of CSF and serum with an ELISA, coated with anti MBL antibodies. Routine parameters such as albumin-, immunoglobulin- CSF/serum quotients, oligoclonal IgG and cell count were used to characterize the patient groups. Groups comprised firstly, control patients without organic brain disease with normal CSF and normal barrier function and secondly, patients without inflammatory diseases but with increased QAlb, i.e. with a blood CSF barrier dysfunction.MBL concentration in CSF was at least five-fold higher than expected for a molecular-size-dependent passage from blood. Secondly, in a QIgM/QAlb quotient diagram (Reibergram) 9/13 cases showed an intrathecal fraction in some cases over 80% of total CSF MBL concentration 3) The smaller inter-individual variation of MBL concentrations in CSF of the control group (CV?=?66%) compared to the MBL concentrations in serum (CV?=?146%) indicate an independent source of MBL in CSF. 4) The absolute MBL concentration in CSF increases with increasing QAlb. Among brain-derived proteins in CSF only the leptomeningeal proteins showed a (linear) increase with decreasing CSF flow rate, neuronal and glial proteins are invariant to changes of QAlb.MBL in CSF is predominantly brain-derived and all results pointed to the leptomeningeal cells as the source of the protein. The evaluation of this protein requires the interpretation of its absolute concentrations in CSF as a function of the albumin quotient, QAlb. This recognition of MBL in brain cells opens a new field of discussion about the function of the innate immune response in CNS in cases of acute and chronic neurological diseases.Increased protein concentrations in the cerebrospinal fluid (CSF) of patients with neurological diseases, frequently ascribed to a blood-CSF barrier dysfunction, are due to pathologically-reduced CSF flow rates [1]. This view is based on the molecular diffusion/CSF flow theory [1] which shows that the concentration of a blood-derived pr
Genetically-Defined Deficiency of Mannose-Binding Lectin Is Associated with Protection after Experimental Stroke in Mice and Outcome in Human Stroke
Alvaro Cervera,Anna M. Planas,Carles Justicia,Xabier Urra,Jens C. Jensenius,Ferran Torres,Francisco Lozano,Angel Chamorro
PLOS ONE , 2012, DOI: 10.1371/journal.pone.0008433
Abstract: The complement system is a major effector of innate immunity that has been involved in stroke brain damage. Complement activation occurs through the classical, alternative and lectin pathways. The latter is initiated by mannose-binding lectin (MBL) and MBL-associated serine proteases (MASPs). Here we investigated whether the lectin pathway contributes to stroke outcome in mice and humans.
Non-Synonymous Polymorphisms in the FCN1 Gene Determine Ligand-Binding Ability and Serum Levels of M-Ficolin
Christian Gytz Ammitzb?ll, Troels R?nn Kj?r, Rudi Steffensen, Kristian Stengaard-Pedersen, Hans J?rgen Nielsen, Steffen Thiel, Martin B?gsted, Jens Christian Jensenius
PLOS ONE , 2012, DOI: 10.1371/journal.pone.0050585
Abstract: Background The innate immune system encompasses various recognition molecules able to sense both exogenous and endogenous danger signals arising from pathogens or damaged host cells. One such pattern-recognition molecule is M-ficolin, which is capable of activating the complement system through the lectin pathway. The lectin pathway is multifaceted with activities spanning from complement activation to coagulation, autoimmunity, ischemia-reperfusion injury and embryogenesis. Our aim was to explore associations between SNPs in FCN1, encoding M-ficolin and corresponding protein concentrations, and the impact of non-synonymous SNPs on protein function. Principal Findings We genotyped 26 polymorphisms in the FCN1 gene and found 8 of these to be associated with M-ficolin levels in a cohort of 346 blood donors. Four of those polymorphisms were located in the promoter region and exon 1 and were in high linkage disequilibrium (r2≥0.91). The most significant of those were the AA genotype of ?144C>A (rs10117466), which was associated with an increase in M-ficolin concentration of 26% compared to the CC genotype. We created recombinant proteins corresponding to the five non-synonymous mutations encountered and found that the Ser268Pro (rs150625869) mutation lead to loss of M-ficolin production. This was backed up by clinical observations, indicating that an individual homozygote of Ser268Pro would be completely M-ficolin deficient. Furthermore, the Ala218Thr (rs148649884) and Asn289Ser (rs138055828) were both associated with low M-ficolin levels, and the mutations crippled the ligand-binding capability of the recombinant M-ficolin, as indicated by the low binding to Group B Streptococcus. Significance Overall, our study interlinks the genotype and phenotype relationship concerning polymorphisms in FCN1 and corresponding concentrations and biological functions of M-ficolin. The elucidations of these associations provide information for future genetic studies in the lectin pathway and complement system.
Leprosy Association with Low MASP-2 Levels Generated by MASP2 Haplotypes and Polymorphisms Flanking MAp19 Exon 5
Angelica Beate Winter Boldt, Isabela Goeldner, Ewalda R. S. Stahlke, Steffen Thiel, Jens Christian Jensenius, Iara José Taborda de Messias-Reason
PLOS ONE , 2013, DOI: 10.1371/journal.pone.0069054
Abstract: Background The gene MASP2 (mannan-binding lectin (MBL)-associated serine protease 2) encodes two proteins, MASP-2 and MAp19 (MBL-associated protein of 19 kDa), bound in plasma to MBL and ficolins. The binding of MBL/MASP-2 and ficolin/MASP-2 complexes to microorganisms activates the lectin pathway of complement and may increase the ingestion of intracellular pathogens such as Mycobacterium leprae. Methods We haplotyped 11 MASP2 polymorphisms with multiplex sequence-specific PCR in 219 Brazilian leprosy patients (131 lepromatous, 29 borderline, 21 tuberculoid, 14 undetermined, 24 unspecified), 405 healthy Brazilians and 291 Danish blood donors with previously determined MASP-2 and MAp19 levels. We also evaluated MASP-2 levels in further 46 leprosy patients and 69 Brazilian controls. Results Two polymorphisms flanking exon 5 of MASP2 were associated with a dominant effect on high MASP-2 levels and an additive effect on low MAp19 levels. Patients presented lower MASP-2 levels (P = 0.0012) than controls. The frequency of the p.126L variant, associated with low MASP-2 levels (below 200 ng/mL), was higher in the patients (P = 0.0002, OR = 4.92), as was the frequency of genotypes with p.126L (P = 0.00006, OR = 5.96). The *1C2-l [AG] haplotype, which harbors p.126L and the deficiency-causing p.439H variant, has a dominant effect on the susceptibility to the disease (P = 0.007, OR = 4.15). Genotypes composed of the *2B1-i and/or *2B2A-i haplotypes, both associated with intermediate MASP-2 levels (200–600 ng/mL), were found to be protective against the disease (P = 0.0014, OR = 0.6). Low MASP-2 levels (P = 0.022), as well as corresponding genotypes with *1C2-l and/or *2A2-l but without *1B1-h or *1B2-h, were more frequent in the lepromatous than in other patients (P = 0.008, OR = 8.8). Conclusions In contrast with MBL, low MASP-2 levels increase the susceptibility to leprosy in general and to lepromatous leprosy in particular. MASP2 genotypes and MASP-2 levels might thus be of prognostic value for leprosy progression.
Polymorphisms in the MASP1 Gene Are Associated with Serum Levels of MASP-1, MASP-3, and MAp44
Christian Gytz Ammitzb?ll, Rudi Steffensen, Hans J?rgen Nielsen, Steffen Thiel, Kristian Stengaard-Pedersen, Martin B?gsted, Jens Christian Jensenius
PLOS ONE , 2013, DOI: 10.1371/journal.pone.0073317
Abstract: Introduction MASP-1 is the first protein in the activation of the lectin pathway and MASP-1 is, like its isoforms MASP-3 and MAp44, encoded by the MASP1 gene. Our aim was to explore associations between polymorphisms in MASP1 and corresponding concentrations of MASP-1, MASP-3, and MAp44 in plasma as well as the genetic contribution to the equilibrium between the three proteins. Methods Fifteen SNPs were genotyped in the MASP1 gene in 350 blood donors. Corresponding plasma concentrations of MASP-1, MASP-3, and MAp44 were measured. Results A total of 10 different SNPs showed associations with the concentration of one or some of the three proteins (rs113938200, rs190590338, rs35089177, rs3774275, rs67143992, rs698090, rs72549154, rs72549254, rs75284004, rs7625133), and several of these were in strong linkage. SNPs located in the mutually exclusive splice region had opposite effects on the protein concentrations. Being e.g. homozygote for the minor allele of rs3774275 was associated with an increase in median concentration of 13% in MASP-1(P=0.03), 29% in MAp44 (P<0.001), and a decrease in MASP-3 of 26% (P<0.001) compared to homozygosis for the major allele. Heterozygosis of rs113938200 (p.Asn368Asp in MAp44) was associated with a reduced MAp44 concentration of 61% (P=0.005). Rs190590338 located in the promoter region was associated in the heterozygote form with an increased MASP-1 concentration of 35% (P = 0.002). A multivariate linear regression model including sex, age, M- and H-ficolin, MBL, and the 15 SNPs explained 20-48% of the variation in the concentration of the three proteins and the SNPs investigated contributed with the most explanatory power (12-23%). Discussion The present study described 10 SNPs, which were associated with the concentration of one or some of the three proteins originating from the MASP1 gene and in a multivariate model it was shown that the SNPs contributed with the most explanatory power to the protein concentrations.
Mannose-binding lectin deficiency with eosinophilic meningoencephalitis due to Angiostrongylus cantonensis in children: a case series
Bárbara Padilla-Docal, Alberto J Dorta-Contreras, Raisa Bu-Coifiu-Fanego, René H Martínez-Alderete, Olga de Paula-Almeida, Hansotto Reiber, Jens Jensenius
Journal of Medical Case Reports , 2011, DOI: 10.1186/1752-1947-5-330
Abstract: Three Caucasian boys (aged five-years-old, 10-years-old and six-years-old) with a diagnosis of eosinophilic meningoencephalitis caused by Angiostrongylus cantonensis were studied. Serum immunoglobulin A (IgA), IgM, IgG, and complements C3c and C4 levels were quantified by using an immunodiffusion technique. Immunoglobulin E in serum was quantified by nephelometry and mannose-binding lectin by time-resolved fluorometry. Mannose-binding lectin deficiency was observed in the three patients. The first patient showed a reduction in the levels of IgA and IgM and an increase in the values of IgE and C4. The second patient showed a reduction in mannose-binding lectin level with increased IgG, C4 and IgE levels, and the third patient showed a decrease in mannose-binding lectin level and increased levels of IgM and complement C3c as well as a low level of C4.To the best of our knowledge, this is the first report of mannose-binding lectin deficiency associated with Angiostrongylus cantonensis meningoencephalitis in children, and it may contribute to the understanding of the participation of this component of the lectin pathway in the development of the disease.Eosinophilic meningitis, a potentially fatal disease caused by Angiostrongylus cantonensis, a parasitic nematode, is considered an emerging infectious disease [1]. Adult A. cantonensis live in the pulmonary arteries of its definitive hosts, that is, rodents, especially rats, which pass infective first-stage larvae (L1) in their feces. The life cycle also involves mollusks harboring larval stages. In humans, larvae fail to mature, and hence humans and their excreta play no role in the transmission and direct dissemination of the parasite. Humans become infected by ingesting third-stage larvae (L3) in raw or undercooked intermediate host mollusks (for example, snails and slugs) or paratenic hosts (for example, freshwater prawns, crabs, frogs and fish) [1]. Lettuce and vegetable juice have also been identified as sources of
Low Levels of Mannan-Binding Lectin or Ficolins Are Not Associated with an Increased Risk of Cytomegalovirus Disease in HIV-Infected Patients
Adrian Egli, Juliane Sch?fer, Michael Osthoff, Steffen Thiel, Christina Mikkelsen, Andri Rauch, Hans H. Hirsch, Heiner C. Bucher, James Young, Jens C. Jensenius, Manuel Battegay, Marten Trendelenburg, the Swiss HIV Cohort Study
PLOS ONE , 2013, DOI: 10.1371/journal.pone.0051983
Abstract: Background In HIV-infected patients, prediction of Cytomegalovirus (CMV) disease remains difficult. A protective role of mannan-binding lectin (MBL) and ficolins against CMV disease has been reported after transplantation, but the impact in HIV-infected patients is unclear. Methods In a case-control study nested within the Swiss HIV Cohort Study, we investigated associations between plasma levels of MBL/ficolins and CMV disease. We compared HIV-infected patients with CMV disease (cases) to CMV-seropositive patients without CMV disease (controls) matched for CD4 T-cells, sampling time, and use of combination antiretroviral therapy. MBL and M-ficolin, L-ficolin, and H-ficolin were quantified using ELISA. Results We analysed 105 cases and 105 matched controls. CMV disease was neither associated with MBL (odds ratio [OR] 1.03 per log10 ng/mL increase (95% CI 0.73–1.45)) nor with ficolins (OR per log10 ng/mL increase 0.66 (95% CI 0.28–1.52), 2.34 (95% CI 0.44–12.36), and 0.89 (95% CI 0.26–3.03) for M-ficolin, L-ficolin, and H-ficolin, respectively). We found no evidence of a greater association between MBL and CMV disease in patients with low CD4 counts; however in the multivariable analysis, CMV disease was more likely in patients with an increased HIV RNA (OR 1.53 per log10 copies/mL; 95% CI 1.08–2.16), or a shorter duration of HIV-infection (OR 0.91 per year; 95% CI 0.84–0.98). Conclusions CMV disease is not associated with low levels of MBL/ficolins, suggesting a lack of a protective role in HIV-infected patients.
Double Quantum Entanglement to Understand Superconductivity  [PDF]
Jens Cordelair
World Journal of Condensed Matter Physics (WJCMP) , 2013, DOI: 10.4236/wjcmp.2013.34032
Abstract:

The feature of quantum entanglement in doublet and multiplet systems is briefly described and used to create a new model for the superconducting phase.

Superconductivity  [PDF]
Jens Cordelair
World Journal of Condensed Matter Physics (WJCMP) , 2014, DOI: 10.4236/wjcmp.2014.44026
Abstract: The feature of quantum entanglement is used to create a new model for the superconducting state.
Entanglement: A Modern Aspect of Nature  [PDF]
Jens Cordelair
World Journal of Condensed Matter Physics (WJCMP) , 2015, DOI: 10.4236/wjcmp.2015.53025
Abstract: The intention of this paper is to provide an easy to understand introduction to the peculiarities of entangled systems. A novel description for strong (mass entanglement) and weak (spin-or-bital and thermal entanglement) quantum entangled particles is discussed and applied to the phenomena of superconductivity, superfluidity and ultracold gases. A brief statement about how to represent the physical reality of quantum-entanglement as Quantum-Field-Theory (QFT) is noted.
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