Prominent publications by Paul A Janmey

KOL Index score: 14597

A family of homologous actin-binding proteins sever and cap actin filaments and accelerate actin filament assembly. The functions of two of these proteins, villin and gelsolin, and of their proteolytically derived actin binding domains were compared directly by measuring their effects, under various ionic conditions, on the rates and extents of polymerization of pyrene-labeled actin. In 1 mM Ca2+ and 150 mM KCl, villin and gelsolin have similar severing and polymerization-accelerating ...

Also Ranks for: Villin Gelsolin |  actin binding |  intact proteins |  filament severing |  terminal fragments
KOL Index score: 14547

GLUT4 (glucose transporter 4) plays a pivotal role in insulin-induced glucose uptake to maintain normal blood glucose levels. Here, we report that a cell-permeable phosphoinositide-binding peptide induced GLUT4 translocation to the plasma membrane without inhibiting IRAP (insulin-responsive aminopeptidase) endocytosis. However, unlike insulin treatment, the peptide treatment did not increase glucose uptake in 3T3-L1 adipocytes, indicating that GLUT4 translocation and activation are ...

Also Ranks for: Glut4 Translocation |  plasma membrane |  glucose uptake |  insulin signaling |  peptide treatment
KOL Index score: 14089

Gelsolin is a calcium binding protein that shortens actin filaments. This effect occurs in the presence but not in the absence of micromolar calcium ion concentrations and is partially reversed following removal of calcium ions. Once two actin molecules have bound to gelsolin in solutions containing Ca2+, one of the actins remains bound following chelation of calcium, so that the reversal of gelsolin's effect cannot be accounted for simply by its dissociation from the ends of the ...

Also Ranks for: Actin Gelsolin |  filament severing |  binding proteins |  calcium ions |  nntetraacetic acid
KOL Index score: 13916

Liver fibrosis is characterized by excessive deposition of extracellular matrix proteins by myofibroblasts derived from hepatic stellate cells and portal fibroblasts. Activation of these precursors to myofibroblasts requires matrix stiffness, which results in part from increased collagen cross-linking mediated by lysyl oxidase (LOX) family proteins. The aims of this study were to characterize the mechanical changes of early fibrosis, to identify the cells responsible for LOX production ...

Also Ranks for: Portal Fibroblasts |  stellate cells |  normal liver |  lysyl oxidases |  cellular sources
KOL Index score: 13230

Antimicrobial peptides are part of the innate host defense system, and inactivation of these peptides is implicated in airway infections in cystic fibrosis (CF). The sputum of patients with CF contains anionic polyelectrolytes, including F-actin and DNA not found in normal airway fluid. These anionic filaments aggregate to contribute to the altered viscoelastic properties of CF sputum. We hypothesized that the airway components stabilizing bundles of F-actin and DNA are in part cationic ...

Also Ranks for: Antimicrobial Activity |  cathelicidin ll37 |  factin dna |  cystic fibrosis sputum |  actin bundles
KOL Index score: 13217

BACKGROUND: Sheets of cells move together as a unit during wound healing and embryonic tissue movements, such as those occurring during gastrulation and neurulation. We have used epithelial wound closure as a model system for such movements and examined the mechanisms of closure and the importance of the Rho family of Ras-related small GTPases in this process.

RESULTS: Wounds induced in Madin-Darby canine kidney (MDCK) epithelial cell monolayers close by Rac- and ...

Also Ranks for: Wound Closure |  cell mechanics |  gtp binding |  rho activity |  signaling pathways
KOL Index score: 12993

Cell types from many tissues respond to changes in substrate stiffness by actively remodeling their cytoskeletons to alter spread area or adhesion strength, and in some cases changing their own stiffness to match that of their substrate. These cell responses to substrate stiffness are linked to substrate-induced changes in the state, localization, and amount of numerous proteins, but detailed evidence for the requirement of specific proteins in these distinct forms of mechanical response ...

Also Ranks for: Substrate Stiffness |  adherent area |  a7 cells |  cell adhesion |  atomic force
KOL Index score: 12695

The myristoylated form of c-Abl protein, as well as the P210bcr/abl protein, have been shown by indirect immunofluorescence to associate with F-actin stress fibers in fibroblasts. Analysis of deletion mutants of c-Abl stably expressed in fibroblasts maps the domain responsible for this interaction to the extreme COOH-terminus of Abl. This domain mediates the association of a heterologous protein with F-actin filaments after microinjection into NIH 3T3 cells, and directly binds to F-actin ...

Also Ranks for: Actin Binding |  cooh terminus |  abl protein |  tyrosine kinase |  bundling activity
KOL Index score: 12285

AGONISTS that stimulate protein kinase C (PKC) induce profound changes in cell morphology correlating with the reorganization of submembranous actin1,2, but no direct connection between PKC and actin assembly has been identified3. The myristoylated, alanine-rich C kinase substrate (MARCKS) binds calmodulin4,5 and is a predominant, specific substrate of PKC which is phosphorylated during macrophage and neutrophil activation6–8, growth factor-dependent mitogenesis9,10and ...

Also Ranks for: Protein Kinase |  actin filament |  calcium calmodulin |  marcks pkc |  plasma membrane
KOL Index score: 11655

Both phosphoinositides and small GTP-binding proteins of the Rho family have been postulated to regulate actin assembly in cells. We have reconstituted actin assembly in response to these signals in Xenopus extracts and examined the relationship of these pathways. We have found that GTPgammaS stimulates actin assembly in the presence of endogenous membrane vesicles in low speed extracts. These membrane vesicles are required, but can be replaced by lipid vesicles prepared from purified ...

Also Ranks for: Actin Assembly |  xenopus egg |  binding protein |  small gtp |  cell extracts
KOL Index score: 11450

Actin filaments of different lengths were prepared by polymerizing actin in the presence of various concentrations of gelsolin, a protein which accelerates actin polymerization by stabilizing nuclei from which filaments grow and which binds to their fast growing ends. The lengths of the actin filaments following polymerization were measured by electron microscopy and showed that the number-average filament length agreed with the predicted length if each gelsolin molecule acted as a seed ...

Also Ranks for: Actin Filaments |  electron microscopy |  quasielastic light |  distribution lengths |  diffusion gelsolin
KOL Index score: 11275

The cellular and molecular pathways initiated by traumatic brain injury (TBI) may compromise the function and structural integrity of mitochondria, thereby contributing to cerebral metabolic dysfunction and cell death. The extent to which TBI affects regional mitochondrial populations with respect to structure, function, and swelling was assessed 3 hours and 24 hours after lateral fluid-percussion brain injury in the rat. Significantly less mitochondrial protein was isolated from the ...

Also Ranks for: Brain Injury |  cortex hippocampus |  mitochondria mitochondrial |  tbi rats |  24 hours
KOL Index score: 11259

Bundles of F-actin and DNA present in the sputum of cystic fibrosis (CF) patients but absent from normal airway fluid contribute to the altered viscoelastic properties of sputum that inhibit clearance of infected airway fluid and exacerbate the pathology of CF. Previous strategies to remove these filamentous aggregates have focused on DNase to enzymatically depolymerize DNA to constituent monomers and gelsolin to sever F-actin to small fragments. The high densities of negative surface ...

Also Ranks for: Cystic Fibrosis |  dna factin |  actin bundles |  airway fluid |  gelsolin humans
KOL Index score: 11187

Gelsolin is a Ca2+- and polyphosphoinositide-modulated actin-binding protein which severs actin filaments, nucleates actin assembly, and caps the "barbed" end of actin filaments. Proteolytic cleavage analysis of human plasma gelsolin has shown that the NH2-terminal half of the molecule severs actin filaments almost as effectively as native gelsolin in a Ca2+-insensitive but polyphosphoinositide-inhibited manner. Further proteolysis of the NH2-terminal half generates two unique fragments ...

Also Ranks for: Actin Filaments |  protein binding |  native gelsolin |  phosphatidylinositol 45 |  peptide fragments
KOL Index score: 11113

We determined the plasma kinetics of both actin and complexes of actin with the two high affinity actin-binding proteins of plasma, gelsolin, and vitamin D-binding protein (DBP). Actin is cleared rapidly from the plasma by the liver (half-disappearance time, 0.5 h). Using radiolabeled actin-binding proteins, we found that actin accelerated the clearance of both plasma gelsolin and the vitamin D-binding protein. In separate experiments we found that DBP-actin complexes were cleared more ...

Also Ranks for: Plasma Gelsolin |  binding protein |  dbp actin |  rabbits vitamin

Key People For Actin Filaments

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Paul A Janmey:Expert Impact

Concepts for whichPaul A Janmeyhas direct influence:Actin filaments,  Plasma gelsolin,  Mechanical properties,  Salmon thrombin,  Lipid droplets,  Actin assembly,  Neural differentiation,  Compression stiffening.

Paul A Janmey:KOL impact

Concepts related to the work of other authors for whichfor which Paul A Janmey has influence:Mechanical properties,  Extracellular matrix,  Actin cytoskeleton,  Tissue engineering,  Cell adhesion,  Plasma membrane,  Protein kinase.



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Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, Pennsylvania; Department of Physiology, University of Pennsylvania, Philadelphia, Pennsylvania. Electronic address: | Department of Bioengine