Search

Your search keyword '"Claudia Perandones"' showing total 2 results
Start Over Author "Claudia Perandones" Journal plos one
2 results on '"Claudia Perandones"'

1. Different conformations of phosphatase and tensin homolog, deleted on chromosome 10 (PTEN) protein within the nucleus and cytoplasm of neurons.

Author

Vera L Moncalero, Roxana V Costanzo, Claudia Perandones, and Martin Radrizzani

Subjects
Medicine, Science
Abstract

PTEN is a critical gene involved in the regulation of many cellular processes. The product of this gene has dual phosphatase activity and is able to dephosphorylate the 5' end of the phosphatidylinositol (3,4,5)-trisphosphate. Within the cellular nucleus, this protein has been associated with regulation of the expression of many genes, although the mechanism of this regulation remains unclear. In this paper, two specific oligonucleotide aptamers were developed and selected, using the SELEX procedure, according to their ability to detect the PTEN protein in different subcellular compartments of neurons. While one aptamer was able to detect PTEN in the nucleus, the other recognized PTEN in the cytoplasm. The recognition pattern of PTEN by both aptamers was confirmed using antibodies in western blots of the proteins purified from mouse cerebellar homogenates and subcellular fractions. Additionally, we demonstrated that the two aptamers recognized different epitopes of the target peptide. The results presented here could not be fully explained by the canonical phosphatase structure of PTEN, suggesting the existence of different conformations of phosphatase in the nucleus and the cytoplasm.

Published
2011
Full Text
View/download PDF

2. Different Conformations of Phosphatase and Tensin Homolog, Deleted on Chromosome 10 (PTEN) Protein within the Nucleus and Cytoplasm of Neurons

Author

Claudia Perandones, Roxana V. Costanzo, Vera L. Moncalero, and Martin Radrizzani

Subjects
Proteomics, Cytoplasm, Protein Conformation, Aptamer, Amino Acid Motifs, Phosphatase, Oligonucleotides, Cancer Treatment, lcsh:Medicine, Target peptide, Models, Biological, Signaling Pathways, Epitopes, Mice, Protein structure, medicine, Animals, Combinatorial Chemistry Techniques, Humans, Synthetic Peptide, PTEN, Tensin, Protein Interactions, lcsh:Science, Biology, Cell Nucleus, Neurons, Multidisciplinary, biology, Cancer Risk Factors, Cell Membrane, lcsh:R, PTEN Phosphohydrolase, medicine.anatomical_structure, Oncology, Biochemistry, biology.protein, Medicine, lcsh:Q, Molecular Neuroscience, Peptides, Nucleus, Research Article, Biotechnology, Neuroscience
Abstract

PTEN is a critical gene involved in the regulation of many cellular processes. The product of this gene has dual phosphatase activity and is able to dephosphorylate the 5′ end of the phosphatidylinositol (3,4,5)-trisphosphate. Within the cellular nucleus, this protein has been associated with regulation of the expression of many genes, although the mechanism of this regulation remains unclear. In this paper, two specific oligonucleotide aptamers were developed and selected, using the SELEX procedure, according to their ability to detect the PTEN protein in different subcellular compartments of neurons. While one aptamer was able to detect PTEN in the nucleus, the other recognized PTEN in the cytoplasm. The recognition pattern of PTEN by both aptamers was confirmed using antibodies in western blots of the proteins purified from mouse cerebellar homogenates and subcellular fractions. Additionally, we demonstrated that the two aptamers recognized different epitopes of the target peptide. The results presented here could not be fully explained by the canonical phosphatase structure of PTEN, suggesting the existence of different conformations of phosphatase in the nucleus and the cytoplasm.

Published
2011

Catalog

Books, media, physical & digital resources
See catalog results