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Pàgina 1 des de 24 resultats
RNAi of FACE1 protease results in growth inhibition of human cells expressing lamin A: implications for Hutchinson-Gilford progeria syndrome.
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FACE 1 is the endoprotease responsible for cleavage of prelamin A to lamin A. Transfection of HeLa cells with siRNA for human FACE 1 results in a strong phenotype. Protein and mRNA levels for FACE 1 are knocked down and cell division stops abruptly. Two populations of cells are detected. The first
Replication factor C1, the large subunit of replication factor C, is proteolytically truncated in Hutchinson-Gilford progeria syndrome.
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Hutchinson-Gilford progeria syndrome (HGPS) is a rare genetic disorder because of a LMNA gene mutation that produces a mutant lamin A protein (progerin). Progerin also has been correlated to physiological aging and related diseases. However, how progerin causes the progeria remains unknown. Here, we
Increased lability of triosephosphate isomerase in progeria and Werner's syndrome fibroblasts.
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Triosephosphate isomerase was found to have an increased thermolabile component in skin fibroblasts from patients with progeria and Werner's syndrome when compared with normal fibroblasts. Mixtures of cell extracts from progeria or Werner's syndrome with normal fibroblasts gave intermediate levels
[Cellular DNA repair, proliferative activity and biochemical characteristics in the human premature aging syndrome (progeria)].
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Fibroblasts of a patient with the Hutchinson-Gilford progeria show a decreased proliferative activity in culture and run through no more than 19 subcultivations. Progeria cells rejoin gamma-induced single strand DNA breaks to the same extent and with the same rate as do normal cells. Spontaneous and
Elevated levels of glycoprotein gp200 in progeria fibroblasts.
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The glycosylation of proteins in fibroblasts from people with the premature ageing disease Hutchinson-Gilford Progeria Syndrome (progeria) was investigated. Protein was prepared from fibroblast cell lines established from skin biopsy taken from progeria patients and control donors. Glycoproteins
Inhibiting farnesylation reverses the nuclear morphology defect in a HeLa cell model for Hutchinson-Gilford progeria syndrome.
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Hutchinson-Gilford progeria syndrome (HGPS) is a devastating premature aging disease resulting from a mutation in the LMNA gene, which encodes nuclear lamins A and C. Lamin A is synthesized as a precursor (prelamin A) with a C-terminal CaaX motif that undergoes farnesylation, endoproteolytic
Survey of plasma proteins in children with progeria pre-therapy and on-therapy with lonafarnib.
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BackgroundHutchinson-Gilford progeria syndrome (HGPS) is an ultra-rare, fatal, segmental premature aging syndrome caused by the aberrant lamin A protein, progerin. The protein farnesyltransferase inhibitor, lonafarnib, ameliorates some aspects of cardiovascular and bone disease.MethodsWe performed a
Genomic instability and DNA damage responses in progeria arising from defective maturation of prelamin A.
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Progeria syndromes have in common a premature aging phenotype and increased genome instability. The susceptibility to DNA damage arises from a compromised repair system, either in the repair proteins themselves or in the DNA damage response pathways. The most severe progerias stem from mutations
Prelamin A, Zmpste24, misshapen cell nuclei, and progeria--new evidence suggesting that protein farnesylation could be important for disease pathogenesis.
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Prelamin A undergoes multistep processing to yield lamin A, a structural protein of the nuclear lamina. Prelamin A terminates with a CAAX motif, which triggers farnesylation of a C-terminal cysteine (the C of the CAAX motif), endoproteolytic release of the last three amino acids (the AAX), and
A new pathway that regulates 53BP1 stability implicates cathepsin L and vitamin D in DNA repair.
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Genomic instability due to telomere dysfunction and defective repair of DNA double-strand breaks (DSBs) is an underlying cause of ageing-related diseases. 53BP1 is a key factor in DNA DSBs repair and its deficiency is associated with genomic instability and cancer progression. Here, we uncover a
Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences.
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In the presence of O2, Fe(III) or Cu(II), and an appropriate electron donor, a number of enzymic and nonenzymic oxygen free radical-generating systems are able to catalyze the oxidative modification of proteins. Whereas random, global modification of many different amino acid residues and extensive
Omi/HtrA2 Participates in Age-Related Autophagic Deficiency in Rat Liver.
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Liver is a vital organ with many important functions, and the maintenance of normal hepatic function is necessary for health. As an essential mechanism for maintaining cellular homeostasis, autophagy plays an important role in ensuring normal organ function. Studies have indicated that the
Ste24: An Integral Membrane Protein Zinc Metalloprotease with Provocative Structure and Emergent Biology.
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Ste24, an integral membrane protein zinc metalloprotease, is found in every kingdom of eukaryotes. It was discovered approximately twenty years ago by yeast genetic screens identifying it as a factor responsible for processing the yeast mating a-factor pheromone. In animals, Ste24 processes prelamin
The Tripartite Architecture of the Eukaryotic Integral Membrane Protein Zinc Metalloprotease Ste24.
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Ste24 enzymes, a family of eukaryotic integral membrane proteins, are zinc metalloproteases (ZMPs) originally characterized as "CAAX proteases" targeting prenylated substrates, including a-factor mating pheromone in yeast and prelamin A in humans. Recently, Ste24 was shown to also cleave
Reduction of unscheduled DNA synthesis and plasminogen activator activity in Hutchinson-Gilford fibroblasts during passaging in vitro: partial correction by interferon-beta.
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Two fibroblast cell lines (PG3KT and PG1NA) derived from Hutchinson-Gilford syndrome (progeria) cases were characterized, at various population doubling levels (PDL), with respect to the capacity of ultraviolet light (UV, mainly 254 nm wavelength)-induced unscheduled DNA synthesis (UDS) and
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