Daniel Aeschlimann

ORCID: 0000-0003-0930-7706
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Research Areas
  • Blood properties and coagulation
  • Celiac Disease Research and Management
  • Microscopic Colitis
  • Cell Adhesion Molecules Research
  • Tendon Structure and Treatment
  • Whipple's Disease and Interleukins
  • Skin and Cellular Biology Research
  • Osteoarthritis Treatment and Mechanisms
  • Bone Metabolism and Diseases
  • Proteoglycans and glycosaminoglycans research
  • Genetic Neurodegenerative Diseases
  • Cellular Mechanics and Interactions
  • Autoimmune Bullous Skin Diseases
  • Connective tissue disorders research
  • Erythrocyte Function and Pathophysiology
  • Cytokine Signaling Pathways and Interactions
  • Protease and Inhibitor Mechanisms
  • Viral Infections and Immunology Research
  • Caveolin-1 and cellular processes
  • Knee injuries and reconstruction techniques
  • Angiogenesis and VEGF in Cancer
  • Platelet Disorders and Treatments
  • Inflammatory Myopathies and Dermatomyositis
  • RNA regulation and disease
  • Autoimmune Neurological Disorders and Treatments

Cardiff University
2015-2025

Versus Arthritis
2017

Tampere University
2013

Sheffield Hallam University
2010-2013

Royal Hallamshire Hospital
2013

University of Manchester
2011

Ruhr University Bochum
2011

Heart and Diabetes Center North Rhine-Westphalia
2011

University of Wales
2004-2009

University of Rome Tor Vergata
2003

Biodegradable materials for spatially and temporally controlled delivery of bioactive agents such as drugs, growth factors, or cytokines are key to facilitating tissue repair. We have developed a versatile method chemical crosslinking high-molecular-weight hyaluronic acid under physiological conditions yielding biocompatible biodegradable hydrogels. The is based on the introduction functional groups onto by formation an active ester at carboxylate glucuronic moiety subsequent substitution...

10.1002/(sici)1097-4636(199911)47:2<152::aid-jbm5>3.0.co;2-i article EN Journal of Biomedical Materials Research 1999-11-01

An M, = 624,000 oligomeric protein was isolated from bovine cartilage and designated COMP (Cartilage Oligomeric Matrix Protein).The is composed of disulfide-bonded subunits with an apparent 100,000 each.It markedly anionic, probably due to its high contents aspartic acid glutamic acid, as well substitution negatively charged carbohydrates.COMP found in all cartilages analyzed, but could not be detected other tissues by enzyme-linked immunosorbent assay guanidine HCl extracts.Within a given...

10.1016/s0021-9258(18)42671-3 article EN cc-by Journal of Biological Chemistry 1992-03-01

Abstract Objective Gluten sensitivity typically presents as celiac disease, a chronic, autoimmune‐mediated, small‐intestinal disorder. Neurological disorders occur with frequency of up to 10% in these patients. However, neurological dysfunction can also be the sole presenting feature gluten sensitivity. Development autoimmunity directed toward different members transglutaminase gene family could offer an explanation for diversity manifestations We have identified novel neuronal isozyme and...

10.1002/ana.21450 article EN Annals of Neurology 2008-09-28

Tissue transglutaminase (TGase2) is a protein-crosslinking enzyme known to be associated with the in vivo apoptosis program. Here we report that could induced TGase2 -/- mice; however, clearance of apoptotic cells was defective during involution thymus elicited by dexamethasone, anti-CD3 antibody, or γ-irradiation, and liver after hyperplasia. The lack prevented production active transforming growth factor-β1 macrophages exposed cells, which required for up-regulation , accelerating deletion...

10.1073/pnas.0832466100 article EN Proceedings of the National Academy of Sciences 2003-06-16

The laminin-nidogen complex, a major component of basement membranes, incorporates [3H]putrescine and monodansylcadaverine in the presence guinea pig liver transglutaminase. Label was detected nidogen isolated, as well complexed form, but not laminin. incorporation proceeds time-dependent manner at rate similar to that achieved with N,N-dimethylcasein, characterized transglutaminase substrate. Saturation site(s), comparison level reference proteins, indicated one high affinity amine acceptor...

10.1016/s0021-9258(18)98617-5 article EN cc-by Journal of Biological Chemistry 1991-08-01

We isolated and characterized the gene encoding human transglutaminase (TG)<sub>X</sub>(<i>TGM5</i>) mapped it to 15q15.2 region of chromosome 15 by fluorescence <i>in situ</i> hybridization. The consists 13 exons separated 12 introns spans about 35 kilobases. Further sequence analysis mapping showed that this locus contained three genes arranged in tandem:<i>EPB42</i> (band 4.2 protein), <i>TGM5</i>, a novel (<i>TGM7</i>). A full-length cDNA for (TG<sub>Z</sub>) was obtained anchored...

10.1074/jbc.m102553200 article EN cc-by Journal of Biological Chemistry 2001-08-01

The expression of tissue transglutaminase in skeletal tissues is strictly regulated and correlates with chondrocyte differentiation cartilage calcification endochondral bone formation maturation tracheal (Aeschlimann, D., A. Wetterwald, H. Fleisch, M. Paulsson. 1993. J. Cell Biol. 120:1461-1470). We now demonstrate the reaction product, gamma-glutamyl-epsilon-lysine cross-link, matrix hypertrophic using a novel cross-link specific antibody. Incorporation synthetic substrate...

10.1083/jcb.129.3.881 article EN The Journal of Cell Biology 1995-05-01

Calcifying cartilages show a restricted expression of tissue transglutaminase. Immunostaining newborn rat paw bones reveals only in the epiphyseal growth plate. Tissue transglutaminase appears first intracellularly proliferation/maturation zone and remains until calcification lower hypertrophic zone. Externalization occurs before mineralization. Subsequently, enzyme is present interterritorial matrix during provisional calcified cartilage cores bone trabeculae. In trachea, mineralization...

10.1083/jcb.120.6.1461 article EN The Journal of Cell Biology 1993-03-15

The previous finding of an immunologic response primarily directed against transglutaminase (TG)6 in patients with gluten ataxia (GA) led us to investigate the role TG6 antibodies diagnosing GA.This was a prospective cohort study. We recruited from ataxia, gluten/neurology, celiac disease (CD), and movement disorder clinics based at Royal Hallamshire Hospital (Sheffield, UK) CD clinic, Tampere University (Tampere, Finland). groups included idiopathic sporadic GA, CD, neurology healthy...

10.1212/wnl.0b013e3182919070 article EN Neurology 2013-04-11

Transglutaminase 2 (TG2), a protein cross-linking enzyme with many additional biological functions, acts as coreceptor for integrin beta(3). We have previously shown that TG2(-/-) mice develop an age-dependent autoimmunity due to defective in vivo clearance of apoptotic cells. Here we report TG2 on the cell surface and guanine nucleotide-bound form promotes phagocytosis. Besides being binding partner beta(3), receptor known mediate uptake cells via activating Rac1, also show binds MFG-E8...

10.4049/jimmunol.0803444 article EN The Journal of Immunology 2009-02-09

Objectives: Non-coeliac gluten sensitivity (NCGS) refers to patients with primarily gastrointestinal symptoms without enteropathy that symptomatically benefit from gluten-free diet (GFD). Little is known about its pathophysiology, propensity neurological manifestations, and if these differ coeliac disease (CD). We investigated the clinical immunological characteristics of presenting manifestations CD those NCGS. Methods: compared clinical, neurophysiological, imaging data NCGS dysfunction...

10.1038/ajg.2015.434 article EN The American Journal of Gastroenterology 2016-02-02

Tissue transglutaminase (TG2) affects cell-matrix interactions in cell spreading, migration and extracellular matrix (ECM) reorganisation. Using fibroblasts deficient TG2 or overexpressing normal crosslinking-deficient enzyme, we show that the crosslinking activity intracellular G-protein function signal transduction contribute differentially to regulation of interactions. TG2-deficient cells displayed attachment but delayed spreading on ECM substrata defects motility unrelated crosslinking....

10.1242/jcs.01188 article EN Journal of Cell Science 2004-06-17

Abstract Inflammation‐mediated bone loss is a major feature of various diseases including rheumatoid arthritis, osteoarthritis and advanced periodontitis. Enhanced osteoclast development or activity at the inflammation site results in resorption. IL‐23 heterodimeric cytokine belonging to IL‐6/IL‐12 family that has been implicated pathogenesis arthritis demonstrated play role osteoclastogenesis via stimulation IL‐17 production. In this study we investigated whether contributes regulation...

10.1002/eji.200838192 article EN European Journal of Immunology 2008-10-01

Background Celiac disease (CD) is an autoimmune gastrointestinal disorder characterized by the presence of anti-transglutaminase 2 (TG2) and anti-gliadin antibodies. Amongst neurological dysfunctions associated with CD, ataxia represents most common one. Methods We analyzed immunohistochemistry, anti-neural reactivity serum from 20 CD patients. To determine role anti-TG2 antibodies in ataxia, two single chain variable fragments (scFv), isolated a phage-display IgA antibody library, were...

10.1371/journal.pone.0009698 article EN cc-by PLoS ONE 2010-03-12

The proteoglycan decorin is expressed by sprouting but not quiescent endothelial cells, and angiogenesis dysregulated in its absence. Previously, we have shown that core protein can bind to activate insulin-like growth factor-I receptor (IGF-IR) cells. In this study, show promotes alpha2beta1 integrin-dependent cell adhesion migration on fibrillar collagen type I. We provide evidence modulates cell-matrix interaction context stimulating cytoskeletal focal reorganization through activation of...

10.1074/jbc.m710025200 article EN cc-by Journal of Biological Chemistry 2008-04-16

Transglutaminases (TG) form a family of enzymes that catalyse various post-translational modifications glutamine residues in proteins and peptides including intra- intermolecular isopeptide bond formation, esterification deamidation. We have characterized novel member the mammalian TG family, TG6, which is expressed human carcinoma cell line with neuronal characteristics mouse brain. Besides full-length protein, alternative splicing results short variant lacking second β-barrel domain man...

10.1007/s00726-011-1091-z article EN cc-by-nc Amino Acids 2011-10-07

ZED1227 is a small molecule tissue transglutaminase (TG2) inhibitor. The compound selectively binds to the active state of TG2, forming stable covalent bond with cysteine in its catalytic center. was designed for treatment celiac disease. Celiac disease an autoimmune-mediated chronic inflammatory condition intestine affecting about 1–2% people Caucasian populations. autoimmune triggered by dietary gluten. Consumption staple foods containing wheat, barley, or rye leads destruction intestinal...

10.3390/cells11101667 article EN cc-by Cells 2022-05-17

Increasing evidence indicates that tissue transglutaminase (tTG) plays a role in the assembly and remodeling of extracellular matrices promotes cell adhesion. Using an inducible system we have previously shown tTG associates with matrix deposited by stably transfected 3T3 fibroblasts overexpressing enzyme. We now show confocal microscopy colocalizes pericellular fibronectin these cells, immunogold electron two proteins are found clusters at surface. Expression vectors encoding full-length or...

10.1074/jbc.274.43.30707 article EN cc-by Journal of Biological Chemistry 1999-10-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTTransglutaminase-catalyzed crosslinking of fibrils collagen V/XI in A204 rhabdomyosarcoma cellsJean-Philippe Kleman, Daniel Aeschlimann, Mats Paulsson, and Michel van der RestCite this: Biochemistry 1995, 34, 42, 13768–13775Publication Date (Print):October 1, 1995Publication History Published online1 May 2002Published inissue 1 October 1995https://pubs.acs.org/doi/10.1021/bi00042a007https://doi.org/10.1021/bi00042a007research-articleACS...

10.1021/bi00042a007 article EN Biochemistry 1995-10-01
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