| 1. |
- Popat, S, et al.
(författare)
-
Variation in the CTLA4/CD28 gene region confers an increased risk of coeliac disease.
- 2002
-
Ingår i: Annals of human genetics. - 0003-4800 .- 1469-1809. ; 66:Pt 2, s. 125-37
-
Tidskriftsartikel (refereegranskat)abstract
- Susceptibility to coeliac disease involves HLA and non-HLA-linked genes. The CTLA4/CD28 gene region encodes immune regulatory T-cell surface molecules and is a strong candidate as a susceptibility locus. We evaluated CTLA4/CD28 in coeliac disease by genetic linkage and association and combined our findings with published studies through a meta-analysis. 116 multiplex families were genotyped across CTLA4/CD28 using eight markers. The contribution of CTLA4/CD28 to coeliac disease was assessed by non-parametric linkage and association analyses. Seven studies were identified that had evaluated the relationship between CTLA4/CD28 and coeliac disease and a pooled analysis of data undertaken. In our study there was evidence for a relationship between variation in the CTLA4/CD28 region and coeliac disease by linkage and association analyses. However, the findings did not attain formal statistical significance (p = 0.004 and 0.039, respectively). Pooling findings with published results showed significant evidence for linkage (504 families) and association (940 families): p values, 0.0001 and 0.0014 at D2S2214, respectively, and 0.0008 and 0.0006 at D2S116, respectively. These findings suggest that variation in the CD28/CTLA4 gene region is a determinant of coeliac disease susceptibility. Dissecting the sequence variation underlying this relationship will depend on further analyses utilising denser sets of markers.
|
|
| 2. |
- Babakov, V.N., et al.
(författare)
-
RelA/NF-?B transcription factor associates with a-actinin-4
- 2008
-
Ingår i: Experimental Cell Research. - : Elsevier BV. - 0014-4827 .- 1090-2422. ; 314:5, s. 1030-1038
-
Tidskriftsartikel (refereegranskat)abstract
- The NF-?B/RelA family of transcription factors regulates inducible transcription of a large number of genes in response to diverse stimuli. Little is known, however, about the location of NF-?B in the cytoplasm and the transport mechanism to the nucleus. We found that NF-?B is associated with the actin-binding protein a-actinin-4. NF-?B and a-actinin-4 co-localized along actin stress fibers and in membrane lamellae in A431 cells. After a 30-min stimulation with EGF or TNF-a, a-actinin-4 and p65 were found in the nucleus. Disruption of cytoskeleton by cytochalasin D prior to treatment with TNF-a led to increase of p65 nuclear translocation. Antibodies to p65 subunit of NF-?B co-immunoprecipitated a-actinin-4 from A431 cell lysates and nuclear extracts, but a-actinin-1 and ß-actin were not found in the precipitates. Affinity chromatography experiments displayed that p65 and p50 subunits of NF-?B can bind to matrix-bound chicken gizzard a-actinin. We suggest that the a-actinin-4 is important for the NF-?B nuclear translocation and its functions inside the nucleus. © 2007 Elsevier Inc. All rights reserved.
|
|
| 3. |
- Khotin, M.G., et al.
(författare)
-
Analysis of nuclear protein complexes comprising a-actinin-4 by 2D-electrophoresis and mass-spectrometry
- 2009
-
Ingår i: Tsitologiya. - : SP MAIK Nauka/Interperiodica. - 0041-3771. ; 51:8, s. 684-690
-
Tidskriftsartikel (refereegranskat)abstract
- Actin-binding protein a-actinin-4 is a member of spectrin super family. It is located in the cytoplasm and in the nucleus. However, nuclear functions of a-actinin-4 are still not clear. In this study, we analyzed composition of nuclear protein complexes associated with a-actinin-4 in A431 cells. Using 2D electrophoresis, we have determined that about 50 different proteins may be associated with nuclear a-actinin-4. Using mass-spectrometry, we analyzed major proteins of these complexes. ß-Actin, a- and ß-tubulins, ribonucleoprotein A2/B1, which regulates splicing and is associated with ß-actin, peroxiredoxin-1, which is involved in oxidative stress, and glycolytic enzyme D-3-phosphoglycerate dehydrogenase were identified by MALDI-TOF. Detection of these proteins in nuclear complexes with a-actinin-4 may suggest that a-actinin-4 is involved in transcription and splicing. Presence of a-actin in the investigated complexes was confirmed by tandem mass-spectrometry (MALDITOF-TOF). Immunoprecipitation of nuclear proteins with antibodies against a-tubulin confirmed association of a-actinin-4 with a-tubulin in the protein complex. Nuclear a-actinin-4 constitutes of 105 KDa fullsize isoform and two truncated isoforms of 65 and 75 kDa, whereas only the truncated isoform have been found in nuclear complexes with a-tubulin. These data suggest that a-actinin-4 is associated with a number of different nuclear protein complexes which may carry out different functions in the cell nucleus.
|
|
| 4. |
|
|
| 5. |
- Ahlen, K., et al.
(författare)
-
Platelet-derived growth factor-BB modulates membrane mobility of ß1 integrins
- 2004
-
Ingår i: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 314:1, s. 89-96
-
Tidskriftsartikel (refereegranskat)abstract
- Platelet-derived growth factor (PDGF)-BB elicits a migratory response including reorganization of the actin cytoskeleton in different cell types. Here we have investigated the effects of PDGF-BB stimulation on ß 1 integrin containing focal adhesions in human diploid fibroblasts adhered to collagen type I. Stimulation with PDGF-BB dissociated focal adhesions and relocated ß1 integrins from focal adhesions to the periphery of the cells. These changes were rapid and transient in character. Relocation of ß1 integrins was prevented by inhibitors of phosphoinositide-3-kinase and protein kinase C. PDGF-BB stimulated fibroblasts exhibited an increased diffusion coefficient of cell surface ß1 integrins as determined by fluorescence recovery of photobleaching. The cell surface expression of ß1 integrins was not changed after stimulation with PDGF-BB. Our data suggest that PDGF-BB increases the dynamic properties of cell-surface ß1 integrins, which most likely are important for the migratory response elicited by PDGF-BB. © 2003 Elsevier Inc. All rights reserved.
|
|
| 6. |
- Aksenova, Vasilisa, et al.
(författare)
-
Actin-binding protein alpha-actinin 4 (ACTN4) is a transcriptional co-activator of RelA/p65 sub-unit of NF-kB
- 2013
-
Ingår i: Oncotarget. - : Impact Journals LLC. - 1949-2553. ; 4:2, s. 362-372
-
Tidskriftsartikel (refereegranskat)abstract
- ACTN4 is an actin-binding protein that participates in cytoskeleton organisation. It resides both in the cytoplasm and nucleus and physically associates with various transcription factors. Here, we describe an effect of ACTN4 expression on transcriptional activity of the RelA/p65 subunit of NF-kB. We demonstrate that ACTN4 enhances RelA/p65-dependant expression of c-fos, MMP-3 and MMP-1 genes, but it does not affect TNC, ICAM1 and FN1 expression. Importantly, actin-binding domains of ACTN4 are not critical for the nuclear translocation and co-activation of RelA/p65-dependent transcription. Collectively, our data suggest that in the nucleus, ACTN4 functions as a selective transcriptional co-activator of RelA/p65.
|
|
| 7. |
|
|
| 8. |
- Amin, M., et al.
(författare)
-
Treponema denticola Msp-deduced peptide conjugate, P34BSA, promotes RhoA-dependent actin stress fiber formation independent of its internalization by fibroblasts
- 2008
-
Ingår i: Cell Motility and the Cytoskeleton. - : Wiley. - 0886-1544 .- 1097-0169. ; 65:5, s. 406-421
-
Tidskriftsartikel (refereegranskat)abstract
- P34BSA, a BSA conjugate of a synthetic 10-mer peptide deduced from Treponema denticola major outer sheath protein (Msp), stabilizes actin filaments in fibroblasts and retards cell motility. We reported previously that it is internalized by cells, binds and bundles actin filaments in vitro, and activates RhoA, yet, its site and mechanism of action were not defined. We have assessed P34BSA's modes of interaction with and signaling to fibroblasts. At 4°C, P34BSA was not internalized, but it bound to the plasma membrane and promoted actin stress fiber formation at ~80% capacity compared with 37°C controls, casting doubt that cellular uptake is a critical step for its cytoskeleton-stabilizing property. In Rho G-LISA™ and co-immunoprecipitation assays, P34BSA was found to activate RhoA, even at 4°C, to promote its interaction with guanosine nucleotide exchange factor p114RhoGEF. It also caused phosphorylation of cofilin. Upon RhoA inhibition, either by C3 transferase RhoA inhibitor or by transfection with a dominant negative RhoA construct, P34BSA did not achieve the stress fiber formation seen with P34BSA alone. By inhibiting phosphatidylinositol-3 kinase (PI 3-K) with LY294002, the P34BSA effects were completely blocked. Depletion of cholesterol with methyl-ß-cyclodextrin (MßCD) partially inhibited P34BSA signaling via the plasma membrane to the cytoskeleton. This suggests that multivalent P34BSA activation of lipid raft components requires active PI 3-K, and initiates the pathway through a RhoGEF and RhoA, which mediates stress fiber formation in fibroblasts. Hence, P34BSA may represent a novel tool to investigate RhoA-dependent processes, such as remodeling filamentous actin in eukaryotic cells. © 2008 Wiley-Liss, Inc.
|
|
| 9. |
- Bairagi, Samiran, et al.
(författare)
-
Zinc gallate (ZnGa2O4) epitaxial thin films : determination of optical properties and bandgap estimation using spectroscopic ellipsometry
- 2022
-
Ingår i: Optical Materials Express. - : Optica Publishing Group. - 2159-3930. ; 12:8, s. 3284-3295
-
Tidskriftsartikel (refereegranskat)abstract
- Electronic grade ZnGa2O4 epitaxial thin films were grown on c-plane sapphire substrates by metal-organic chemical vapor deposition and investigated using spectroscopic ellipsometry. Their thickness, roughness and optical properties were determined using a Multiple Sample Analysis based approach by the regression analysis of optical model and measured data. These samples were then compared to samples which had undergone ion etching, and it was observed that etching time up to four minutes had no discernible impact on its optical properties. Line shape analysis of resulting absorption coefficient dispersion revealed that ZnGa(2)O(4 )exhibited both direct and indirect interband transitions. The modified Cody formalism was employed to determine their optical bandgaps. These values were found to be in good agreement with values obtained using other popular bandgap extrapolation procedures. Published by Optica Publishing Group under the terms of the Creative Commons Attribution 4.0 License. Further distribution of this work must maintain attribution to the author(s) and the published articles title, journal citation, and DOI.
|
|
| 10. |
|
|
