TY  - JOUR
AU  - Milićević, Zorka T.
AU  - Bajić, Vladan P.
AU  - Živković, Lada
AU  - Kasapović, Jelena
AU  - Anđelković, Uros
AU  - Spremo-Potparević, Biljana
PY  - 2014
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/5855
AB  - In breast carcinoma, disruption of the p53 pathway is one of the most common genetic alterations. The observation that the p53 can express multiple protein isoforms adds a novel level of complexity to the outcome of p53 mutations. p53 expression was analysed by Western immunoblotting and immunohistochemistry using monoclonal antibodies DO-7, Pab240, and polyclonal antiserum CM-1. The more frequently p53-positive nuclear staining has been found in the invasive breast tumors. One of the most intriguing findings is that mutant p53 appears as discrete dot-shaped regions within the nucleus of breast cancer cells. In many malignant cells, the nucleolar sequestration of p53 is evident. These observations support the view that the nucleolus is involved directly in the mediation of p53 function or indirectly by the control of the localization of p53 interplayers. p53 expressed in the nuclear fraction of breast cancer cells revealed a wide spectrum of isoforms. p53 isoforms Lambda Np53 (47 kDa) and Lambda 133p53 beta (35 kDa), known as dominant-negative repressors of p53 function, were detected as the most predominant variants in nuclei of invasive breast carcinoma cells. The isoforms expressed also varied between individual tumors, indicating potential roles of these p53 variants in human breast cancer.
T2  - Scientific World Journal
T1  - Identification of p53 and Its Isoforms in Human Breast Carcinoma Cells
DO  - 10.1155/2014/618698
ER  - 

@article{
author = "Milićević, Zorka T. and Bajić, Vladan P. and Živković, Lada and Kasapović, Jelena and Anđelković, Uros and Spremo-Potparević, Biljana",
year = "2014",
abstract = "In breast carcinoma, disruption of the p53 pathway is one of the most common genetic alterations. The observation that the p53 can express multiple protein isoforms adds a novel level of complexity to the outcome of p53 mutations. p53 expression was analysed by Western immunoblotting and immunohistochemistry using monoclonal antibodies DO-7, Pab240, and polyclonal antiserum CM-1. The more frequently p53-positive nuclear staining has been found in the invasive breast tumors. One of the most intriguing findings is that mutant p53 appears as discrete dot-shaped regions within the nucleus of breast cancer cells. In many malignant cells, the nucleolar sequestration of p53 is evident. These observations support the view that the nucleolus is involved directly in the mediation of p53 function or indirectly by the control of the localization of p53 interplayers. p53 expressed in the nuclear fraction of breast cancer cells revealed a wide spectrum of isoforms. p53 isoforms Lambda Np53 (47 kDa) and Lambda 133p53 beta (35 kDa), known as dominant-negative repressors of p53 function, were detected as the most predominant variants in nuclei of invasive breast carcinoma cells. The isoforms expressed also varied between individual tumors, indicating potential roles of these p53 variants in human breast cancer.",
journal = "Scientific World Journal",
title = "Identification of p53 and Its Isoforms in Human Breast Carcinoma Cells",
doi = "10.1155/2014/618698"
}

Milićević, Z. T., Bajić, V. P., Živković, L., Kasapović, J., Anđelković, U.,& Spremo-Potparević, B.. (2014). Identification of p53 and Its Isoforms in Human Breast Carcinoma Cells. in Scientific World Journal.
https://doi.org/10.1155/2014/618698

Milićević ZT, Bajić VP, Živković L, Kasapović J, Anđelković U, Spremo-Potparević B. Identification of p53 and Its Isoforms in Human Breast Carcinoma Cells. in Scientific World Journal. 2014;.
doi:10.1155/2014/618698 .

Milićević, Zorka T., Bajić, Vladan P., Živković, Lada, Kasapović, Jelena, Anđelković, Uros, Spremo-Potparević, Biljana, "Identification of p53 and Its Isoforms in Human Breast Carcinoma Cells" in Scientific World Journal (2014),
https://doi.org/10.1155/2014/618698 . .

TY  - JOUR
AU  - Anđelković, Uros
AU  - Theisgen, Stephan
AU  - Scheidt, Holger A.
AU  - Petković, Marijana
AU  - Huster, Daniel
AU  - Vujčić, Zoran
PY  - 2012
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4695
AB  - Understanding the effect of surface charge on the stability of proteins is one prerequisite for tailoring proteins with increased thermal stability. Here, we investigated the origin of the altered thermal stability observed between the four recently isolated isoforms (EINV1-EINV4) of external invertase. External invertase from yeast Saccharomyces cerevisiae, a homodimeric glycoprotein, represents a widely used model for studying the influence of the glyco component on protein stability. The stability of the four isoforms of invertase decreases from EINV1 to EINV4, which is accompanied by an increase in negative surface charge density. Mass spectrometry analysis revealed that the isoforms share identical protein parts indicating that the differences in stability are the result of post-translational modifications. P-31 NMR analysis revealed that the isoforms contain negatively charged phosphate groups in diester and monoester forms attached to the glycan part. The total amount of phosphate bound to the polymannan component varies between the different isoforms. These results, together with the analysis of the amount of polymannan components, show that negative surface charge density does not entirely depend on the amount of phosphate but rather on its distribution. This suggests that charged groups bound to the glyco-component of a protein can influence the stability of glycoproteins. (C) 2011 Elsevier Masson SAS. All rights reserved.
T2  - Biochimie
T1  - The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density
VL  - 94
IS  - 2
SP  - 510
EP  - 515
DO  - 10.1016/j.biochi.2011.08.020
ER  - 

@article{
author = "Anđelković, Uros and Theisgen, Stephan and Scheidt, Holger A. and Petković, Marijana and Huster, Daniel and Vujčić, Zoran",
year = "2012",
abstract = "Understanding the effect of surface charge on the stability of proteins is one prerequisite for tailoring proteins with increased thermal stability. Here, we investigated the origin of the altered thermal stability observed between the four recently isolated isoforms (EINV1-EINV4) of external invertase. External invertase from yeast Saccharomyces cerevisiae, a homodimeric glycoprotein, represents a widely used model for studying the influence of the glyco component on protein stability. The stability of the four isoforms of invertase decreases from EINV1 to EINV4, which is accompanied by an increase in negative surface charge density. Mass spectrometry analysis revealed that the isoforms share identical protein parts indicating that the differences in stability are the result of post-translational modifications. P-31 NMR analysis revealed that the isoforms contain negatively charged phosphate groups in diester and monoester forms attached to the glycan part. The total amount of phosphate bound to the polymannan component varies between the different isoforms. These results, together with the analysis of the amount of polymannan components, show that negative surface charge density does not entirely depend on the amount of phosphate but rather on its distribution. This suggests that charged groups bound to the glyco-component of a protein can influence the stability of glycoproteins. (C) 2011 Elsevier Masson SAS. All rights reserved.",
journal = "Biochimie",
title = "The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density",
volume = "94",
number = "2",
pages = "510-515",
doi = "10.1016/j.biochi.2011.08.020"
}

Anđelković, U., Theisgen, S., Scheidt, H. A., Petković, M., Huster, D.,& Vujčić, Z.. (2012). The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density. in Biochimie, 94(2), 510-515.
https://doi.org/10.1016/j.biochi.2011.08.020

Anđelković U, Theisgen S, Scheidt HA, Petković M, Huster D, Vujčić Z. The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density. in Biochimie. 2012;94(2):510-515.
doi:10.1016/j.biochi.2011.08.020 .

Anđelković, Uros, Theisgen, Stephan, Scheidt, Holger A., Petković, Marijana, Huster, Daniel, Vujčić, Zoran, "The thermal stability of the external invertase isoforms from Saccharomyces cerevisiae correlates with the surface charge density" in Biochimie, 94, no. 2 (2012):510-515,
https://doi.org/10.1016/j.biochi.2011.08.020 . .