106 results match your criteria vimentin solubility

Unidirectional Regulation of Vimentin Intermediate Filaments to Caveolin-1.

Int J Mol Sci 2020 Oct 9;21(20). Epub 2020 Oct 9.

The Joint Program in Infection and Immunity, Guangzhou Women and Children's Medical Center, Guangzhou Medical University, Guangzhou 510623, China.

Both the mechanosensitive vimentin cytoskeleton and endocytic caveolae contribute to various active processes such as cell migration, morphogenesis, and stress response. However, the crosstalk between these two systems has remained elusive. Here, we find that the subcellular expression between vimentin and caveolin-1 is mutual exclusive, and vimentin filaments physically arrest the cytoplasmic motility of caveolin-1 vesicles. Read More

View Article and Full-Text PDF
October 2020

An injectable liposome for sustained release of tanshinone IIA to the treatment of acute blunt muscle injury by augmenting autophagy and alleviating oxidative stress.

Am J Transl Res 2020 15;12(8):4189-4203. Epub 2020 Aug 15.

Department of Orthopaedics, The Second Affiliated Hospital and Yuying Children's Hospital of Wenzhou Medical University 109 Xue Yuan Xi Road, Wenzhou 325000, Zhejiang, China.

Acute blunt skeletal muscle injury occurs frequently in sports and traffic accidents, and even leads to muscle necrosis and impaired functionality. Current treatment options for muscle injuries remain suboptimal and often result in delayed/incomplete recovery of damaged muscles. Tanshinone IIA is extracted from Salvia Miltiorrhizae, which is effective in the treatment of injury repair. Read More

View Article and Full-Text PDF

CD44 and vimentin, markers involved with epithelial-mesenchymal transition: A proteomic analysis of sequential proteins extraction of triple-negative breast cancer cells after treatment with all-trans retinoic acid.

Gen Physiol Biophys 2020 Jul;39(4):399-405

Institute of Analytical Chemistry of the CAS, Brno, Czech Republic.

This work aimed to provide, in one isolation and separation step, an overview of the content of proteins with different solubility after treatment with all-trans retinoic acid, which is considered to be an important therapeutic agent, predominantly in acute promyelocytic leukemia. Breast, ovarian, bladder, and skin cancers have been demonstrated to be suppressed by retinoic acid, as well. The bottom-up proteomic strategies were applied for the analysis of proteins extracted from triple-negative breast cancer MDA-MB-231 cells utilizing a commercially manufactured kit. Read More

View Article and Full-Text PDF

Localization of the lens intermediate filament switch by imaging mass spectrometry.

Exp Eye Res 2020 09 16;198:108134. Epub 2020 Jul 16.

Department of Biochemistry, Vanderbilt University, Nashville, TN 37232, USA. Electronic address:

Imaging mass spectrometry (IMS) enables targeted and untargeted visualization of the spatial localization of molecules in tissues with great specificity. The lens is a unique tissue that contains fiber cells corresponding to various stages of differentiation that are packed in a highly spatial order. The application of IMS to lens tissue localizes molecular features that are spatially related to the fiber cell organization. Read More

View Article and Full-Text PDF
September 2020

Vimentin citrullination probed by a novel monoclonal antibody serves as a specific indicator for reactive astrocytes in neurodegeneration.

Neuropathol Appl Neurobiol 2020 12 1;46(7):751-769. Epub 2020 May 1.

Ilsong Institute of Life Science, Hallym University, Anyang, Gyeonggi-do, Republic of Korea.

Aims: Vimentin citrullination, the calcium (Ca )-dependent peptidylarginine deiminase (PAD)-mediated conversion of an arginine residue of vimentin to a citrulline residue, has emerged as a pathophysiological outcome of autoimmune diseases and neurodegeneration. However, the roles, functions, and expression of citrullinated vimentin have not yet been elucidated because available antibodies are limited.

Methods: We developed mouse monoclonal IgG1 and IgM specific for vimentin citrullinated at position R440 or R450 and applied Western blotting, immunohistochemistry, and immunofluorescent staining to investigate the pathogenesis of prion diseases in animal models, in patients with prion diseases, and in vitro. Read More

View Article and Full-Text PDF
December 2020

SMR peptide antagonizes mortalin promoted release of extracellular vesicles and affects mortalin protection from complement-dependent cytotoxicity in breast cancer cells and leukemia cells.

Oncotarget 2019 Sep 10;10(52):5419-5438. Epub 2019 Sep 10.

Department of Microbiology, Biochemistry, and Immunology, Morehouse School of Medicine, Atlanta, GA 30310, USA.

Mortalin/GRP-75/mt-hsp70 is a mitochondrial chaperone protein, found in the cytoplasm, endoplasmic reticulum and cytoplasmic vesicles. It functions in many cellular processes such as mitochondrial biogenesis, intracellular trafficking, cell proliferation, signaling, immortalization and tumorigenesis. Thus, inhibition of mortalin is a promising avenue for cancer therapy. Read More

View Article and Full-Text PDF
September 2019

Changes in Human Foetal Osteoblasts Exposed to the Random Positioning Machine and Bone Construct Tissue Engineering.

Int J Mol Sci 2019 Mar 18;20(6). Epub 2019 Mar 18.

Osteoimmunology and Integrative Physiology Laboratory, Department of Biology, Texas Southern University, Cleburne, Houston, TX 77004, USA.

Human cells, when exposed to both real and simulated microgravity (s-µ), form 3D tissue constructs mirroring in vivo architectures (e.g., cartilage, intima constructs, cancer spheroids and others). Read More

View Article and Full-Text PDF

In wound repair vimentin mediates the transition of mesenchymal leader cells to a myofibroblast phenotype.

Mol Biol Cell 2018 07 2;29(13):1555-1570. Epub 2018 May 2.

Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, PA 19107.

Following injury, mesenchymal repair cells are activated to function as leader cells that modulate wound healing. These cells have the potential to differentiate to myofibroblasts, resulting in fibrosis and scarring. The signals underlying these differing pathways are complex and incompletely understood. Read More

View Article and Full-Text PDF

Regulation of keratin 5/14 intermediate filaments by CDK1, Aurora-B, and Rho-kinase.

Biochem Biophys Res Commun 2018 04 6;498(3):544-550. Epub 2018 Mar 6.

Department of Physiology, Mie University Graduate School of Medicine, Tsu, Mie 514-8507, Japan. Electronic address:

We previously reported that vimentin, GFAP, and desmin (type III intermediate filament [IF] proteins) are mitotically phosphorylated by CDK1, Aurora-B, and Rho-kinase. This phosphorylation is critical for efficient separation of these IFs and completion of cytokinesis. Keratin 5 (K5) and K14 form a heterodimer, which constitutes IF network in basal layer cells of stratified squamous epithelia. Read More

View Article and Full-Text PDF

An image-based small-molecule screen identifies vimentin as a pharmacologically relevant target of simvastatin in cancer cells.

FASEB J 2018 05 18;32(5):2841-2854. Epub 2018 Jan 18.

Department of Cell Biology and Physiology, University of North Carolina-Chapel Hill, Chapel Hill, North Carolina, USA.

Vimentin is a cytoskeletal intermediate filament protein that is expressed in mesenchymal cells and cancer cells during the epithelial-mesenchymal transition. The goal of this study was to identify vimentin-targeting small molecules by using the Tocriscreen library of 1120 biochemically active compounds. We monitored vimentin filament reorganization and bundling in adrenal carcinoma SW13 vimentin-positive (SW13-vim) cells via indirect immunofluorescence. Read More

View Article and Full-Text PDF

Host Cell Vimentin Restrains Invasion and Phosphorylation of Vimentin is Partially Regulated by Interaction with ROP18.

Int J Biol Sci 2017 5;13(9):1126-1137. Epub 2017 Sep 5.

Department of Pathogen Biology, Guangdong Provincial Key Laboratory of Tropical Disease Research, School of Public Health, Southern Medical University, Guangzhou, Guangdong Province, 510515, China.

The obligate intracellular parasite, , manipulates the cytoskeleton of its host cells to facilitate infection. A significant rearrangement of host cell vimentin around parasitophorous vacuoles is observed during the course of infection. ROP18 (ROP18) is a serine-threonine kinase secreted by rhoptry and a major virulence factor; however, the mechanisms by which this kinase modulates host factors remain poorly understood. Read More

View Article and Full-Text PDF

Dissolved molecular hydrogen (H) in Peritoneal Dialysis (PD) solutions preserves mesothelial cells and peritoneal membrane integrity.

BMC Nephrol 2017 Oct 31;18(1):327. Epub 2017 Oct 31.

Tohoku University, United Centers for Advanced Research and Translational Medicine, Center for Advanced and Integrated Renal Science, Sendai, Japan.

Background: Peritoneal dialysis (PD) is used as renal replacement therapy in patients with end-stage kidney disease. However, peritoneal membrane failure remains problematic and constitutes a critical cause of PD discontinuation. Recent studies have revealed the unique biological action of molecular hydrogen (H) as an anti-oxidant, which ameliorates tissue injury. Read More

View Article and Full-Text PDF
October 2017

Anaplasma phagocytophilum-Occupied Vacuole Interactions with the Host Cell Cytoskeleton.

Vet Sci 2016 Sep 21;3(3). Epub 2016 Sep 21.

Department of Microbiology and Immunology, School of Medicine, Virginia Commonwealth University Medical Center, Richmond, VA 23298, USA.

is an obligate intracellular bacterial pathogen of humans and animals. The -occupied vacuole (ApV) is a critical host-pathogen interface. Here, we report that the intermediate filaments, keratin and vimentin, assemble on the ApV early and remain associated with the ApV throughout infection. Read More

View Article and Full-Text PDF
September 2016

Dephosphorylation of MAP2D enhances its binding to vimentin in preovulatory ovarian granulosa cells.

J Cell Sci 2016 08 22;129(15):2983-96. Epub 2016 Jun 22.

Department of Cell and Molecular Biology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA School of Molecular Biosciences, Washington State University, Pullman, WA 99164, USA

Preovulatory granulosa cells express the low-molecular-mass MAP2D variant of microtubule-associated protein 2 (MAP2). Activation of the luteinizing hormone choriogonadotropin receptor by human choriogonadotropin (hCG) promotes dephosphorylation of MAP2D on Thr256 and Thr259. We sought to evaluate the association of MAP2D with the cytoskeleton, and the effect of hCG on this association. Read More

View Article and Full-Text PDF

Increased collagen cross-linking is a signature of dystrophin-deficient muscle.

Muscle Nerve 2016 06 22;54(1):71-8. Epub 2016 Feb 22.

Pennsylvania Muscle Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA.

Introduction: Collagen cross-linking is a key parameter in extracellular matrix (ECM) maturation, turnover, and stiffness. We examined aspects of collagen cross-linking in dystrophin-deficient murine, canine, and human skeletal muscle.

Methods: DMD patient biopsies and samples from mdx mice and golden retriever muscular dystrophy dog samples (with appropriate controls) were analyzed. Read More

View Article and Full-Text PDF

Alpha-Catulin Co-Localizes With Vimentin Intermediate Filaments and Functions in Pulmonary Vascular Endothelial Cell Migration via ROCK.

J Cell Physiol 2016 04 17;231(4):934-43. Epub 2015 Sep 17.

Division of Pulmonary, Critical Care and Sleep, Tupper Research Institute, Tufts Medical Center, Tufts University School of Medicine, Boston, Massachusetts.

The ubiquitous α-catulin acts as a scaffold for distinct signalosomes including RhoA/ROCK; however, its function is not well understood. While α-catulin has homology to the cytoskeletal linkers α-catenin and vinculin, it appears to be functionally divergent. Here we further investigated α-catulin function in pulmonary vascular endothelial cells (VEC) on the premise that α-catulin has a unique cytoskeletal role. Read More

View Article and Full-Text PDF

Vimentin Phosphorylation Underlies Myofibroblast Sensitivity to Withaferin A In Vitro and during Corneal Fibrosis.

PLoS One 2015 17;10(7):e0133399. Epub 2015 Jul 17.

From the Department of Neuroscience, University of Connecticut Health Center, Farmington, Connecticut, United States of America.

Vimentin is a newly recognized target for corneal fibrosis. Using primary rabbit corneal fibroblasts and myofibroblasts we show that myofibroblasts, unlike fibroblasts, display impaired cell spreading and cell polarization, which is associated with increased levels of soluble serine-38 phosphorylated vimentin (pSer38Vim). This pSer38Vim isoform is inefficiently incorporated into growing vimentin intermediate filaments (IFs) of myofibroblasts during cell spreading, and as a result, myofibroblasts maintain higher soluble pSer38Vim levels compared to fibroblasts. Read More

View Article and Full-Text PDF

Vimentin filament organization and stress sensing depend on its single cysteine residue and zinc binding.

Nat Commun 2015 Jun 2;6:7287. Epub 2015 Jun 2.

Department of Chemical and Physical Biology, Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (C.S.I.C.), Ramiro de Maeztu, 9, 28040 Madrid, Spain.

The vimentin filament network plays a key role in cell architecture and signalling, as well as in epithelial-mesenchymal transition. Vimentin C328 is targeted by various oxidative modifications, but its role in vimentin organization is not known. Here we show that C328 is essential for vimentin network reorganization in response to oxidants and electrophiles, and is required for optimal vimentin performance in network expansion, lysosomal distribution and aggresome formation. Read More

View Article and Full-Text PDF

Modulating endothelial barrier function by targeting vimentin phosphorylation.

J Cell Physiol 2014 Oct;229(10):1484-93

Pulmonary & Critical Care Division, Department of Medicine/Tupper Research Institute, Tufts Medical Center, Tufts University School of Medicine, Boston, Massachusetts.

Vimentin is a major intermediate filament protein in vascular endothelial cells which might be involved in their function as a barrier tissue. It is proposed to dynamically maintain integrity of the endothelium as a tightly regulated permeability barrier that is subjected to a variety of shear and contractile forces. The results described in this report demonstrate that vimentin plays that role through mechanisms that are dependent on its phosphorylation state. Read More

View Article and Full-Text PDF
October 2014

Substrate stiffness regulates solubility of cellular vimentin.

Mol Biol Cell 2014 Jan 30;25(1):87-94. Epub 2013 Oct 30.

Department of Bioengineering, University of Pennsylvania, Philadelphia, PA 19104 Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, PA 19104.

The intermediate filament protein vimentin is involved in the regulation of cell behavior, morphology, and mechanical properties. Previous studies using cells cultured on glass or plastic substrates showed that vimentin is largely insoluble. Although substrate stiffness was shown to alter many aspects of cell behavior, changes in vimentin organization were not reported. Read More

View Article and Full-Text PDF
January 2014

Withania somnifera root extract inhibits mammary cancer metastasis and epithelial to mesenchymal transition.

PLoS One 2013 12;8(9):e75069. Epub 2013 Sep 12.

Department of Hematology and Medical Oncology, Winship Cancer Institute of Emory University, Emory University School of Medicine, Atlanta, Georgia, United States of America.

Though clinicians can predict which patients are at risk for developing metastases, traditional therapies often prove ineffective and metastatic disease is the primary cause of cancer patient death; therefore, there is a need to develop anti-metastatic therapies that can be administered over long durations to specifically inhibit the motility of cancer cells. Withaniasomnifera root extracts (WRE) have anti-proliferative activity and the active component, Withaferin A, inhibits the pro-metastatic protein, vimentin. Vimentin is an intermediate filament protein and is part of the epithelial to mesenchymal transition (EMT) program to promote metastasis. Read More

View Article and Full-Text PDF

PKC activation in Niemann pick C1 cells restores subcellular cholesterol transport.

PLoS One 2013 15;8(8):e74169. Epub 2013 Aug 15.

Department of Genetics and Genomic Sciences, the Mount Sinai School of Medicine, New York, New York, United States of America.

Activation of protein kinase C (PKC) has previously been shown to ameliorate the cholesterol transport defect in Niemann Pick Type C1 (NPC1) cells, presumably by increasing the soluble levels of one of its substrates, vimentin. This activity would then restore the vimentin cycle in these cells and allow vimentin-dependent retrograde transport to proceed. Here, we further investigate the effects of PKC activation in NPC1 cells by evaluating different isoforms for their ability to solubilize vimentin and correct the NPC1 cholesterol storage phenotype. Read More

View Article and Full-Text PDF
January 2015

Alteration in composition of keratin intermediate filaments in a model of breast cancer progression and the potential to reverse hallmarks of metastasis.

Cancer Biomark 2012 ;12(2):49-64

Academic Unit of Surgical Oncology, Department of Oncology, University of Sheffield, The Medical School, Sheffield, UK.

Background: In breast cancer the development of metastasis is a major turning point in the treatment and outcome of the disease. Throughout tumour development, and especially in the development of metastasis, epithelial mesenchymal transition takes place. During this transformation into a mesenchymal phenotype, the tumour cells undergo a series of structural changes. Read More

View Article and Full-Text PDF

Calpain-mediated vimentin cleavage occurs upstream of MT1-MMP membrane translocation to facilitate endothelial sprout initiation.

Angiogenesis 2012 Jun 11;15(2):287-303. Epub 2012 Mar 11.

Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, TX 77843-1114, USA.

Endothelial cells normally line the vasculature and remain quiescent. However, these cells can be rapidly stimulated to undergo morphogenesis and initiate new blood vessel formation given the proper cues. This study reports a new mechanism for initiating angiogenic sprout formation that involves vimentin, the major intermediate filament protein in endothelial cells. Read More

View Article and Full-Text PDF

Cigarette smoke exposure induces CFTR internalization and insolubility, leading to airway surface liquid dehydration.

FASEB J 2012 Feb 11;26(2):533-45. Epub 2011 Oct 11.

Cystic Fibrosis/Pulmonary Research and Treatment Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.

Cigarette smoke (CS) exposure induces mucus obstruction and the development of chronic bronchitis (CB). While many of these responses are determined genetically, little is known about the effects CS can exert on pulmonary epithelia at the protein level. We, therefore, tested the hypothesis that CS exerts direct effects on the CFTR protein, which could impair airway hydration, leading to the mucus stasis characteristic of both cystic fibrosis and CB. Read More

View Article and Full-Text PDF
February 2012

A Protein Epitope Signature Tag (PrEST) library allows SILAC-based absolute quantification and multiplexed determination of protein copy numbers in cell lines.

Mol Cell Proteomics 2012 Mar 30;11(3):O111.009613. Epub 2011 Sep 30.

Department of Proteomics and Signal Transduction, Max-Planck Institute of Biochemistry, D-82152 Martinsried, Germany.

Mass spectrometry-based proteomics increasingly relies on relative or absolute quantification. In relative quantification, stable isotope based methods often allow mixing at early stages of sample preparation, whereas for absolute quantification this has generally required recombinant expression of full length, labeled protein standards. Here we make use of a very large library of Protein Epitope Signature Tags (PrESTs) that has been developed in the course of the Human Protein Atlas Project. Read More

View Article and Full-Text PDF

Alexander disease causing mutations in the C-terminal domain of GFAP are deleterious both to assembly and network formation with the potential to both activate caspase 3 and decrease cell viability.

Exp Cell Res 2011 Oct 2;317(16):2252-66. Epub 2011 Jul 2.

Institute of Molecular Medicine, College of Life Sciences, National Tsing Hua University, Hsinchu 300, Taiwan.

Alexander disease is a primary genetic disorder of astrocyte caused by dominant mutations in the astrocyte-specific intermediate filament glial fibrillary acidic protein (GFAP). While most of the disease-causing mutations described to date have been found in the conserved α-helical rod domain, some mutations are found in the C-terminal non-α-helical tail domain. Here, we compare five different mutations (N386I, S393I, S398F, S398Y and D417M14X) located in the C-terminal domain of GFAP on filament assembly properties in vitro and in transiently transfected cultured cells. Read More

View Article and Full-Text PDF
October 2011

2D-PAGE of ovarian cancer: analysis of soluble and insoluble fractions using medium-range immobilized pH gradients.

Biochem Biophys Res Commun 2011 Mar 15;406(3):408-13. Epub 2011 Feb 15.

Department of Obstetrics and Gynaecology, University of Melbourne, Victoria, Australia.

Ovarian cancer remains a leading cause of cancer death. A comparative proteomic study was performed on normal ovarian tissue (n=5) and grade 3 ovarian tumours (n=5) to search for differentially expressed proteins. In contrast to other studies, here we extracted proteins in soluble and insoluble protein fractions using commercial kits and also utilised three medium-range IPG strips that encompassed the broad pH range of 3-10 (pH 3-6, 5-8 and 7-10). Read More

View Article and Full-Text PDF

Recruitment of APPL1 to ubiquitin-rich aggresomes in response to proteasomal impairment.

Exp Cell Res 2011 May 19;317(8):1093-107. Epub 2011 Feb 19.

International Institute of Molecular and Cell Biology, Warsaw, Poland.

Inhibitors of proteasomes have been shown to affect endocytosis of multiple membrane receptors, in particular at the step of cargo sorting for lysosomal degradation. Here we demonstrate that the inhibition of proteasomes causes specific redistribution of an endosomal adaptor APPL1, which undergoes initial solubilization from APPL endosomes followed by clustering in the perinuclear region. MG132 treatment decreases APPL1 labeling of endosomes while the staining of the canonical early endosomes with EEA1 remains unaffected. Read More

View Article and Full-Text PDF

Keratin hypersumoylation alters filament dynamics and is a marker for human liver disease and keratin mutation.

J Biol Chem 2011 Jan 9;286(3):2273-84. Epub 2010 Nov 9.

Department of Molecular & Integrative Physiology, University of Michigan Medical School, Ann Arbor, Michigan 48109-5622, USA.

Keratin polypeptide 8 (K8) associates noncovalently with its partners K18 and/or K19 to form the intermediate filament cytoskeleton of hepatocytes and other simple-type epithelial cells. Human K8, K18, and K19 variants predispose to liver disease, whereas site-specific keratin phosphorylation confers hepatoprotection. Because stress-induced protein phosphorylation regulates sumoylation, we hypothesized that keratins are sumoylated in an injury-dependent manner and that keratin sumoylation is an important regulatory modification. Read More

View Article and Full-Text PDF
January 2011