bromochloroacetic-acid and Infections

bromochloroacetic-acid has been researched along with Infections* in 3 studies

Reviews

1 review(s) available for bromochloroacetic-acid and Infections

Article	Year
Anti-cytoskeletal autoantibodies: diagnostic significance for liver diseases, infections and systemic autoimmune diseases. Autoimmunity, 1991, Volume: 11, Issue:2 Topics: Autoantibodies; Autoimmune Diseases; Biomarkers; Cytoskeleton; Humans; Infections; Keratins; Liver Diseases; Muscle, Smooth	1991

Other Studies

2 other study(ies) available for bromochloroacetic-acid and Infections

Article	Year
Infection by Trypanosoma cruzi. Identification of a parasite ligand and its host cell receptor. The Journal of biological chemistry, 2001, Jun-01, Volume: 276, Issue:22 The infective trypomastigote stage of Trypanosoma cruzi expresses a set of surface glycoproteins that are known collectively as Tc85 and belong to the gp85/trans-sialidase supergene family. A member of this family, Tc85-11, with adhesive properties to laminin and cell surfaces was recently cloned. In this report, the Tc85-11 domain for cell binding and its corresponding receptor on epithelial cell LLC-MK(2) are described. Using synthetic peptides corresponding to the Tc85-11 carboxyl-terminal segment, we show that the mammalian cell-binding domain colocalizes to the most conserved motif of the trypanosome gp85/trans-sialidase supergene family (VTVXNVFLYNR). Even though Tc85-11 binds to laminin, the 19-residue cell-binding peptide (peptide J) does not contain the laminin-binding site, because it does not bind to laminin or inhibit cell binding to this glycoprotein. The host cell receptor for the peptide was characterized as cytokeratin 18. Addition of anti-cytokeratin antibodies to the culture medium significantly inhibited the infection of epithelial cells by T. cruzi. Tc85-11 is a multiadhesive glycoprotein, encoding at least two different binding sites, one for laminin and one for cytokeratin 18, that allow the parasite to overcome the barriers imposed by cell membranes, extracellular matrices, and basal laminae to reach the definitive host cell. This is the first description of a direct interaction between cytokeratin and a protozoan parasite. Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Biotinylation; Blotting, Western; Cell Adhesion; Cell Line; Cell Membrane; Chromatography, Affinity; Cloning, Molecular; Dose-Response Relationship, Drug; Epithelial Cells; Glycoproteins; Humans; Infections; K562 Cells; Keratins; Laminin; Ligands; Membrane Glycoproteins; Mice; Microscopy, Fluorescence; Molecular Sequence Data; Neuraminidase; Peptides; Protein Binding; Protein Structure, Tertiary; Trypanosoma cruzi	2001
Hair destroying growth of Corynebacterium tenuis in the so-called trichomycosis axillaris. New findings from scanning electron microscopy. Archives of dermatology, 1971, Volume: 103, Issue:6 Topics: Adult; Axilla; Corynebacterium; Female; Hair; Humans; Infections; Keratins; Male; Microscopy, Electron, Scanning; Middle Aged; Mycoses; Skin Diseases; Species Specificity	1971

Article

Year

Infection by Trypanosoma cruzi. Identification of a parasite ligand and its host cell receptor.

The Journal of biological chemistry, 2001, Jun-01, Volume: 276, Issue:22

The infective trypomastigote stage of Trypanosoma cruzi expresses a set of surface glycoproteins that are known collectively as Tc85 and belong to the gp85/trans-sialidase supergene family. A member of this family, Tc85-11, with adhesive properties to laminin and cell surfaces was recently cloned. In this report, the Tc85-11 domain for cell binding and its corresponding receptor on epithelial cell LLC-MK(2) are described. Using synthetic peptides corresponding to the Tc85-11 carboxyl-terminal segment, we show that the mammalian cell-binding domain colocalizes to the most conserved motif of the trypanosome gp85/trans-sialidase supergene family (VTVXNVFLYNR). Even though Tc85-11 binds to laminin, the 19-residue cell-binding peptide (peptide J) does not contain the laminin-binding site, because it does not bind to laminin or inhibit cell binding to this glycoprotein. The host cell receptor for the peptide was characterized as cytokeratin 18. Addition of anti-cytokeratin antibodies to the culture medium significantly inhibited the infection of epithelial cells by T. cruzi. Tc85-11 is a multiadhesive glycoprotein, encoding at least two different binding sites, one for laminin and one for cytokeratin 18, that allow the parasite to overcome the barriers imposed by cell membranes, extracellular matrices, and basal laminae to reach the definitive host cell. This is the first description of a direct interaction between cytokeratin and a protozoan parasite.

Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Biotinylation; Blotting, Western; Cell Adhesion; Cell Line; Cell Membrane; Chromatography, Affinity; Cloning, Molecular; Dose-Response Relationship, Drug; Epithelial Cells; Glycoproteins; Humans; Infections; K562 Cells; Keratins; Laminin; Ligands; Membrane Glycoproteins; Mice; Microscopy, Fluorescence; Molecular Sequence Data; Neuraminidase; Peptides; Protein Binding; Protein Structure, Tertiary; Trypanosoma cruzi

2001

Hair destroying growth of Corynebacterium tenuis in the so-called trichomycosis axillaris. New findings from scanning electron microscopy.

Archives of dermatology, 1971, Volume: 103, Issue:6

Topics: Adult; Axilla; Corynebacterium; Female; Hair; Humans; Infections; Keratins; Male; Microscopy, Electron, Scanning; Middle Aged; Mycoses; Skin Diseases; Species Specificity

1971