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1.
Vojnosanit Pregl ; 72(4): 317-27, 2015 Apr.
Article in English | MEDLINE | ID: mdl-26040177

ABSTRACT

BACKGROUND/AIM: In prostate tumors, angiogenesis, measured as microvessel density, is associated with tumor stage and Gleason score. The aim of this study was determine neovascularization of prostatic adenocarcinomas in core biopsies and corresponding prostatectomies. METHODS: The study population included 61 patients who underwent radical prostatectomy (RP) for localized prostate carcinoma patients and did not receive chemohormonal, or radiation therapy before surgery. Tumor blocks were immunostained using the endothelial-specific antibody CD31 and subsequently evaluated at x 400 magnification in both biopsies and corresponding prostatectomies. RESULTS: When comparing microvessel density in core biopsies and corresponding prostatectomies, no statistically significant difference was found (p > 0.1). A statistically significant positive correlation was found when determining correlation between microvessel density (as linear and categorical variable, i.e., with the cut-off value of 48) that was associated with the Gleason score (p < 0.05) and tumor stage (p < 0.0001). There was no correlation between microvessel density and preoperative values of serum prostate-specific antigen (PSA) (p > 0.1). CONCLUSION: Microvessel density can be reliably applied to needle prostate biopsy specimens. Quantification of the microvascular density in biopsies is an accurate pre-operative predictor of tumor stage, discriminating between organ-confined and organ-extending neoplasms.


Subject(s)
Adenocarcinoma , Neovascularization, Pathologic , Prostate-Specific Antigen/blood , Prostate , Prostatectomy/methods , Prostatic Neoplasms , Adenocarcinoma/blood , Adenocarcinoma/pathology , Adenocarcinoma/physiopathology , Adenocarcinoma/surgery , Aged , Biopsy, Large-Core Needle/methods , Humans , Image-Guided Biopsy/methods , Immunohistochemistry , Male , Neoplasm Staging , Neovascularization, Pathologic/diagnosis , Neovascularization, Pathologic/pathology , Predictive Value of Tests , Prognosis , Prostate/blood supply , Prostate/diagnostic imaging , Prostate/pathology , Prostatic Neoplasms/blood , Prostatic Neoplasms/pathology , Prostatic Neoplasms/physiopathology , Prostatic Neoplasms/surgery , Retrospective Studies , Serbia , Ultrasonography
2.
Vojnosanit Pregl ; 71(11): 1018-25, 2014 Nov.
Article in English | MEDLINE | ID: mdl-25536804

ABSTRACT

BACKGROUND/AIM: Interpretation of cytological material obtained by fine needle aspiration (FNA) of salivary glands is one of the most challenging areas in cytopathology. FNA is performed easily, it is minimally invasive, inexpensive, fast, reliable and provides valuable information to clinicians about the nature of the lesion and therapeutic modalities. Ex tempore diagnosis, frozen section (FS) is a diagnostic tool that is essential in determining the modalities of surgical treatment of lesions of the salivary glands. Today this method is used in determining the status of resection margins and infiltration of adjacent anatomical structures. The aim of this study was to present our experiences in the application of FNA and FS in the diagnosis of salivary gland lesions and to determine the sensitivity, specificity, predictive value, and diagnostic reliability of these methods. METHODS: The study included 36 patients. In all the patients, cytological analysis was done before surgery and histological analysis of the surgical material. In 23 of the patients the FS diagnostics was done. Then we compared FNA and FS findings with histopathological findings. RESULTS: Correlation of cytological and histological diagnosis showed sensitivity of 83.3%, specificity 96.67%, positive predictive value 83.3%, negative predictive value of 96.77% and diagnostic accuracy of 97.2%. Based on the relationship between FS diagnosis and histopathological diagnosis, the sensitivity was 100%, specificity 96.67%, while positive predictive value and diagnostic accuracy were 100% each. CONCLUSION: The study confirmed that FNA is a sensitive, reliable diagnostic method for differentiation of lesions of the salivary glands. In cases with no posibility to definite differentiation in FNA samples, and with the need to assess the resection margins and invasion of anatomical structures, it is recommended to use FS diagnostics.


Subject(s)
Biopsy, Fine-Needle , Salivary Gland Diseases/diagnosis , Aged , Aged, 80 and over , Diagnosis, Differential , Diagnostic Imaging , Female , Humans , Male , Middle Aged , Reproducibility of Results , Salivary Gland Diseases/pathology , Salivary Gland Diseases/surgery
3.
Vojnosanit Pregl ; 70(11): 1010-4, 2013 Nov.
Article in English | MEDLINE | ID: mdl-24397195

ABSTRACT

UNLABELLED: BACKROUND/AIM: The final diagnosis of malignant pleural mesothelioma is made exclusively by histopathological examination of biopsy materials that are routinely complemented by the use of immunohistochemical analysis. The aim of this paper was to determine the significance of immunohistochemical analysis and application of certain antibodies in the diagnosis of malignant pleural mesothelioma. METHODS: This retrospective analysis included clinical data of 32 patients with the histopathological diagnosis of malignant pleural mesothelioma made in the period 2004-2009 at the Institute for Pulmonary Diseases in Sremska Kamenica. The material was processed and analyzed at the Center for Pathology. RESULTS: CK5/6 was positive, in 63% of the cases calretinin, in 94% and HBME-1 in 80% of the cases. CK7 was positive in 78%, and EMA in 83% of the cases. All the cases (100%) were negative for TTFF-1, CEA, CD20, desmin and MOC31. CONCLUSION: Immunohistochemistry has become an essential diagnostic procedure for the diagnosis and determination of the type of malignant pleural mesothelioma, and due to the lack of individual antibodies a combination of antibody with different sensitivity and specificity is in use today.


Subject(s)
Biomarkers, Tumor/analysis , Calbindin 2/analysis , Lung Neoplasms/chemistry , Lung Neoplasms/pathology , Mesothelioma/chemistry , Mesothelioma/pathology , Pleural Neoplasms/chemistry , Pleural Neoplasms/pathology , Aged , Aged, 80 and over , Biopsy , Female , Humans , Immunohistochemistry , Keratin-7/analysis , Male , Mesothelioma, Malignant , Middle Aged , Retrospective Studies , Sensitivity and Specificity
4.
Vojnosanit Pregl ; 62(5): 357-63, 2005 May.
Article in Serbian | MEDLINE | ID: mdl-15913039

ABSTRACT

BACKGROUND: Chronic lymphocytic leukemia (CLL) is a neoplastic disease characterized by the accumulation of morphologically mature monoclonal CD5+ B cells in the early phase (G0/G1) of the cell cycle. The accumulation of neoplastically transformed B-lymphocytes (CLL cells) is primarily the consequence of apoptosis blocking in these cells. Bcl-2 proteins are well-known modulators of this process. Some of these proteins are anti-apoptotic while the others are pro-apoptotic. All contain at least one of the four conserved regions called the Bcl-2 homologous domains (BH1-BH4). Evidence indicates that Bcl-2 and Bax form homo- and heterodimers. The anti-apoptotic effect of Bcl-2 protein is based on its ability to bind Bax protein in the heterodimer form, and thus to block the forming of Bax/Bax proapoptotic homodimers. The ratio of Bcl-2/Bax represents the cell autonomous rheostat which determinates the type of the cell reaction to an apoptotic stimulus. METHODS: The aim of this study was to determine the level of interaction between these two proteins in CLL cells using the co-immunoprecipition method. The study included the analysis of 20 peripheral blood specimens from 20 patients with CLL, and 20 peripheral blood specimens from healthy persons, who were in the control group. Specimens were precipitated with the monoclonal antibody for Bcl-2 protein, and immunoblotted with the palyclonal antibady for Bax protein (IP: Bcl-2/WB:Bax). At the same time, specimens were precipitated with the polyclonal antibody for Bax protein, and immunoblotted with the monoclonal antibody for Bcl-2 protein (IP: Bax/WB:Bcl-2). The intensity of Bcl-2 and Bax protein's binding compared to the control samples of the peripheral blood from healthy persons, was increased in CLL cells. RESULTS: IP: Bax/WB: Bcl-2 showed a high level of "free" Bcl-2 protein which was not bound in the heterodimer form to Bax protein. Simultaneously IP: Bcl-2/WB: Bax showed that a higher quantity of Bax protein was bound in the heterodimer form to Bcl-2 protein as opposed to the quantity of pro-apoptotic Bax protein potentialy bound in the homodimer form. CONCLUSION: Further studies involving larger groups of patients are necessary to explore the potential significance of the Bcl-2/Bax protein ratio as a prognositc parameter in the CLL treatment.


Subject(s)
B-Lymphocytes/metabolism , Leukemia, Lymphocytic, Chronic, B-Cell/metabolism , Proto-Oncogene Proteins c-bcl-2/metabolism , Apoptosis , Humans , Immunoblotting , Leukemia, Lymphocytic, Chronic, B-Cell/physiopathology , Protein Binding , bcl-2-Associated X Protein
5.
Vojnosanit Pregl ; 61(1): 41-6, 2004.
Article in Serbian | MEDLINE | ID: mdl-15022388

ABSTRACT

Chronic lymphocytic leukemia (CLL) is a neoplastic disease characterized by the accumulation of morphologically mature monoclonal CD 5+ B cells in the early phase (G0/G1) of the cell cycle. It is considered that the accumulation of neoplastically transformed lymphocytes B (CLL cells) is primarily the consequence of the disturbance, i.e., blockade of these cells' apoptosis process. Apoptosis is the specific process of programmed cell death regulated by numerous extracellular and intracellular mechanisms. The Bcl-2 proteins are well-known modulators of this process. Some of these proteins (such as Bcl-2, and Bcl-XI) are anti-apoptotic, while others (such as Bad or Bax) are pro-apoptotic. Our study included the analysis of 20 peripheral blood specimens from 20 patients with CLL, and 20 peripheral blood specimens of healthy persons who represented the control group. Using Western blotting analysis, we quantitatively examined the protein expression of Bcl-2 family (Bcl-2, Bax, Bad, and Bcl-XI). The level of Bcl-2 (p = 3.68 x 10(-10)), Bax (p = 0.019), and Bad (p = 0.073) proteins expression was significantly increased in all the analyzed peripheral blood samples of patients, while the level of Bcl-XI protein (p = 0.75) did not significantly differ in peripheral blood samples of patients, compared to the controls. The results of this study showed that the increased level of expression of Bcl-2, Bax, and Bad protein represented the most striking feature of CLL cells. Moreover, the variations in the expression of only one protein of the Bcl-2 family could not represent the prognostic parameter in the treatment of this disease.


Subject(s)
B-Lymphocytes/chemistry , Leukemia, Lymphocytic, Chronic, B-Cell/metabolism , Proto-Oncogene Proteins c-bcl-2/analysis , Apoptosis , Blotting, Western , Carrier Proteins/analysis , Humans , Proto-Oncogene Proteins/analysis , bcl-2-Associated X Protein , bcl-Associated Death Protein , bcl-X Protein
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