Disease relevance of PACTAMYCIN

• Production of interleukin 2 (IL-2) in mixed lymphocyte cultures of SJL/J lymph node (LN) and gamma-irradiated, syngeneic lymphoma cells of transplantable reticulum cell sarcoma (gamma-RCS) was abolished by pactamycin pretreatment of gamma-RCS [1].
• In a run-off system composed of term polysomes, ascites S-100, and the inhibitor of initiation, pactamycin, the 25,000 molecular weight material, referred to as pre-hPL, was also synthesized [2].
• Three types of mutations were found in pactamycin resistant cells, A694G, C795U and C796U (Escherichia coli 16 S rRNA numeration) located distantly in rRNA primary structure but probably neighboring each other in the three-dimensional structure [3].
• The processing rate of the capsid precursor (peak 92) was not retarded by pactamycin [4].
• The results of pactamycin gene ordering experiments indicated that the small structural proteins of FeLV are ordered p11-p15-p10-p30 [5].

Psychiatry related information on PACTAMYCIN

• Protein synthesis and amnesia: studies with emetine and pactamycin [6].

High impact information on PACTAMYCIN

• Puromycin and pactamycin, both of which remove RNAs from polysomes, completely unlink tubulin RNA content from the level of free subunits, whereas pretreatment of cells with cycloheximide, which traps mRNAs onto stalled polyribosomes, enhances the specific degradation of tubulin RNAs in response to increases in the subunit content [7].
• The crystal structures of the universal translation-initiation inhibitors edeine and pactamycin bound to ribosomal 30S subunit have revealed that edeine induces base pairing of G693:C795, residues that constitute the pactamycin binding site [8].
• It was found that Ia antignes are rapidly secreted by a subpopulation of splenic T lymphocytes which are nonadherent and which express the surface phenotype Ly-1+, Ly-2-, and Ia-. Secretion of the Ia antigens was a metabolically active process which was inhibited by sodium azide and by Pactamycin, an inhibitor of protein synthesis [9].
• Exogenous IL-2, but not interleukin 1 (IL-1), restored the ability of pactamycin-treated gamma-RCS to induce syngeneic T-cell proliferation [1].
• The membrane-bound ribosomes found after pactamycin treatment consisted of a few polyribosomes, with a striking accumulation of native 60S subunits and an increased number of native 40S subunits [10].

Chemical compound and disease context of PACTAMYCIN

• However, pactamycin- and tunicamycin-treated cells expressed on their membranes a detectable amount (20 to 40% of the untreated control) of HSV-1 glycoproteins gB, gC and gD, left by the virus during its internalization [11].
• Blocking of HSV-1 protein synthesis or N-linked glycosylation with pactamycin or tunicamycin, respectively, prevented HSV-1-infected cells from being lysed, suggesting that HSV-1 glycoprotein synthesis is required for recognition by NK cells [11].

Biological context of PACTAMYCIN

• Here, we show that base pair formation by addition of edeine inhibits tRNA binding to the P site by preventing codon-anticodon interaction and that addition of pactamycin, which rebreaks the base pair, can relieve this inhibition [8].
• Remapping with pactamycin by using methods which take this new protein into account yielded a gag gene order of NH2-p219-p27-p12-p15-COOH [12].
• Pulse-chase kinetics and extensive pactamycin mapping studies show that the translation of rhinovirus 1A proceeds in the order: initiate-P1-S-P2-terminate, where P1 is the precursor to the capsid proteins, S is a stable primary gene product, and P2 is the precursor to a family of noncapsid products [4].
• Pactamycin resistance correlated with the presence of mutations in the 16 S rRNA gene of H. halobium single rRNA operon [3].
• These proteins in the pactamycin binding site are probably related to the initiation step of protein synthesis [13].

Anatomical context of PACTAMYCIN

• Isolated growth cones displayed incorporation of 3H-leucine that was inhibited by treatment with the protein synthesis inhibitors anisomycin and pactamycin, indicating that ribosomal-dependent translation occurs in growth cones [14].
• 40 S subunit migration has been detected in both wheat germ and reticulocyte lysates treated with edeine, pactamycin, or sodium fluoride [15].
• Pactamycin resistance in CHO cells: morphological changes induced by the drug in the wild-type and mutant cells [16].
• Through iodination, one radioactive derivative of pactamycin has been obtained with biological activities similar to the unmodified drug when tested on in vivo and cell-free systems [13].
• In the presence of subinhibitory concentrations of pactamycin, CHO cells, which are normally short, polygonal and disoriented, became greatly elongated and aligned themselves in parallel fashion to produce highly oriented colony morphologies, reminiscent of normal diploid fibroblasts [16].

Associations of PACTAMYCIN with other chemical compounds

• The premature or normal release of nascent proteins by puromycin or pactamycin, respectively, increased the permeability of the RER to 4-MalphaG by 20-30% [17].
• (a) Proteins were pulse labeled by the intravenous injection of radioactive leucine and, 5 min later, pactamycin (an inhibitor of the initiation of protein synthesis) [18].
• Expression of a cI-lacZ protein fusion was relatively resistant to kasugamycin and pactamycin, which inhibit translation initiation on transcripts with leaders [19].
• Here, we show a commensurate superinduction of IL-2 mRNA sequences by three additional inhibitors of protein synthesis with distinct modes of action: T-2 toxin, pactamycin, and sparsomycin [20].
• Binding sites of the antibiotics pactamycin and celesticetin on ribosomal RNAs [21].

Gene context of PACTAMYCIN

• A number of other protein synthesis inhibitors, including streptovitacin, acetoxycycloheximide, pactamycin, and ricin, all increased CYP2H1 mRNA expression to a similar extent [22].
• Treatment of control and heat shocked cells with the initiation inhibitor pactamycin reveals that elongation of the HSP70 nascent peptide is not completely arrested, but is slower in control cells [23].
• Preferential labeling of COOH-terminal sequences in newly synthesized fibronectin was achieved by short term incorporation of radiolabeled amino acids in the presence of pactamycin, an inhibitor of polypeptide chain initiation [24].
• Short incubations and incubations with pactamycin showed that approximately 30,000 molecular weight collagenase-resistant peptides, which are destroyed by pepsin, form the carboxyl end of the pro alpha IV chains [25].
• Since pactamycin promotes polysomes dissociation, these results suggest that cAMP enhances the stability of a polysome-free PEPCK mRNA [26].

Analytical, diagnostic and therapeutic context of PACTAMYCIN

• Unstable precursors were eliminated by incubation in the presence of pactamycin and capsid polypeptides were removed by ultracentrifugation and affinity chromatography [27].
• The inhibition of herpesvirus type 1 in cell cultures by seven inhibitors of DNA synthesis and by pactamycin was investigated by plaque inhibition in Vero cells with agarose overlay, and by yield reduction in one-step growth in HeLa cells [28].

References