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Titolo:
Nuclear translocation of lactosylated poly-L-lysine/cDNA complex in cysticfibrosis airway epithelial cells
Autore:
Klink, DT; Chao, S; Glick, MC; Scanlin, TF;
Indirizzi:
Univ Penn, Abramson Pediat Res Ctr, Childrens Hosp Philadelphia, Cyst Fibrosis Ctr,Sch Med, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA19104 r,Sch Med, Philadelphia, PA 19104 USA Univ Penn, Dept Pediat, Childrens Hosp Philadelphia, Sch Med, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 , Sch Med, Philadelphia, PA 19104 USA
Titolo Testata:
MOLECULAR THERAPY
fascicolo: 6, volume: 3, anno: 2001,
pagine: 831 - 841
SICI:
1525-0016(200106)3:6<831:NTOLPC>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
MEDIATED GENE-TRANSFER; RIBONUCLEOPROTEIN COMPLEX; GLYCOSYLATED POLYLYSINES; PORE COMPLEX; DNA; THERAPY; IMPORT; GALECTIN-3; IDENTIFICATION; LOCALIZATION;
Keywords:
lactosylated poly-L-lysine; gene transfer; nonviral vector; cystic fibrosis airway epithelial cells; nuclear translocation; confocal microscopy;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Scanlin, TF Univ Penn, Abramson Pediat Res Ctr, Childrens Hosp Philadelphia, Cyst Fibrosis Ctr,Sch Med, Room 402,3615 Civ Ctr Blvd, Philadelphia, PA 19104 USA Univ Penn Room 402,3615 Civ Ctr Blvd Philadelphia PA USA 19104
Citazione:
D.T. Klink et al., "Nuclear translocation of lactosylated poly-L-lysine/cDNA complex in cysticfibrosis airway epithelial cells", MOL THER, 3(6), 2001, pp. 831-841

Abstract

Poly-L-lysine, with 40% of its amino groups substituted with lactose, is an effective vector to transfer the CFTR gene into CF airway epithelial cells and correct the chloride channel dysfunction. The intracellular fate of the lactosylated poly-L-lysine/cDNA complex was studied using confocal microscopy. In the presence of chloroquine the complex remained intact during internalization, intracellular transport, and, most importantly, transport into the nucleus. When cells were transfected in the presence of agents that enhance transfection efficiency such as ESCA peptide, a fusogenic peptide, or glycerol a similar fate of the lactosylated poly-L-lysine/cDNA complex was seen. However, when these agents were omitted from the transfection medium, the complex remained in the perinuclear region. Uncomplexed lactosylated poly-L-lysine reached the nucleus efficiently. In contrast mannosylated poly-L-lysine or unsubstituted poly-L-lysine complexed to plasmid did not. Therefore the nuclear accumulation of the complex may be attributed to the substitution of poly-L-lysine with lactose. It is hypothesized that the lactose residues provide for nuclear localization by means of targeting a potential lectin-like protein with galactose/lactose specificity. This mechanismmay be responsible for the nuclear internalization of the complex.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/02/20 alle ore 22:08:33