The polyamines spermidine and spermine, and their precursor putrescine, have been shown to play an important role in cell migration, proliferation, and differentiation. Because of their polycationic property, polyamines are traditionally thought to be involved in DNA replication, gene expression, and protein translation. However, polyamines can also be covalently conjugated to proteins by transglutaminase 2 (TG2). This modification leads to an increase in positive charge in the polyamine-incorporated region which significantly alters the structure of proteins. It is anticipated that protein polyamine conjugation may affect the protein-protein interaction, protein localization, and protein function of the TG2 substrates. In order to investigate the roles of polyamine modification, we synthesized a spermine-conjugated antigen and generated an antiserum against spermine. In vitro TG2-catalyzed spermine incorporation assays were carried out to show that actin, tubulins, heat shock protein 70 and five types of histone proteins were modified with spermine, and modification sites were also identified by liquid chromatography and linear ion trap-orbitrap hybrid mass spectrometry. Subsequent mass spectrometry-based shotgun proteomic ana...Continue Reading
Cytotoxic necrotizing factor production by hemolytic strains of Escherichia coli causing extraintestinal infections
Polyamine starvation causes disappearance of actin filaments and microtubules in polyamine-auxotrophic CHO cells
Activation by polyamines of the acetylation of endogenous histones in isolated chromatin and nuclei from Artemia
A new enzyme-linked immunosorbent assay (ELISA) for studying immunocytochemical procedures using an antiserum produced against spermidine as a model
Identification of cytoplasmic actin as an abundant glutaminyl substrate for tissue transglutaminase in HL-60 and U937 cells undergoing apoptosis.
Bordetella bronchiseptica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gln-63 of the GTP-binding protein Rho
Partial deletion of both the spermine synthase gene and the Pex gene in the X-linked hypophosphatemic, gyro (Gy) mouse
The Rho-deamidating cytotoxic necrotizing factor 1 from Escherichia coli possesses transglutaminase activity. Cysteine 866 and histidine 881 are essential for enzyme activity.
Activation of rho through a cross-link with polyamines catalyzed by Bordetella dermonecrotizing toxin
Lysine-rich histone (H1) is a lysyl substrate of tissue transglutaminase: possible involvement of transglutaminase in the formation of nuclear aggregates in (CAG)(n)/Q(n) expansion diseases
Alteration of Rb binding to HPV 18 E7 modified by transglutaminase 2 with different type of polyamines
The propensity for deamidation and transamidation of peptides by transglutaminase 2 is dependent on substrate affinity and reaction conditions
Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin filaments
Polyamine sharing between tubulin dimers favours microtubule nucleation and elongation via facilitated diffusion
Tissue transglutaminase is an essential participant in the epidermal growth factor-stimulated signaling pathway leading to cancer cell migration and invasion
Post-translational modification of glutamine and lysine residues of HIV-1 aspartyl protease by transglutaminase increases its catalytic activity
The C terminus of tubulin, a versatile partner for cationic molecules: binding of Tau, polyamines, and calcium.
A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration.
Novel roles for biogenic monoamines: from monoamines in transglutaminase-mediated post-translational protein modification to monoaminylation deregulation diseases
Transglutaminase and polyamination of tubulin: posttranslational modification for stabilizing axonal microtubules
Modulation of Higher Order Chromatin Conformation in Mammalian Cell Nuclei Can Be Mediated by Polyamines and Divalent Cations
Snyder-Robinson syndrome: a novel nonsense mutation in spermine synthase and expansion of the phenotype
Methylglyoxal in cells elicits a negative feedback loop entailing transglutaminase 2 and glyoxalase 1
Antibody-assisted target identification reveals afatinib, an EGFR covalent inhibitor, down-regulating ribonucleotide reductase
Protein cross-linking by chlorinated polyamines and transglutamylation stabilizes neutrophil extracellular traps
ODC (Ornithine Decarboxylase)-Dependent Putrescine Synthesis Maintains MerTK (MER Tyrosine-Protein Kinase) Expression to Drive Resolution.
Cell migration is involved in a variety of physiological and pathological processes such as embryonic development, cancer metastasis, blood vessel formation and remoulding, tissue regeneration, immune surveillance and inflammation. Here is the latest research.