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1.
Ukr Biochem J ; 87(5): 103-12, 2015.
Artigo em Inglês | MEDLINE | ID: mdl-26717601

RESUMO

It is known that benign breast tissue exhibit relatively low angiogenic capacity. Activation of angiogenesis in mammary pre-malignant lesions could be associated with disease progression and high risk of transformation into the breast cancer. However, insight into the underlying molecular mechanisms involved in angiogenesis regulation in non-cancerous breast pathologies is still poorly defined. The purpose of the present study was to determine levels of plasminogen and its proteolytic fragments (angiostatins) in mammary dysplasia (mastopathy and breast cyst) and benign neoplasms (fibroadenomas). Plasminogen and angiostatins were analyzed using immunoblotting and quantified by densitometric scanning. The significant increase in plasminogen levels was found in fibrocystic, cysts, and non-proliferatious fibroadenoma masses (4.7-, 3.7-, and 3.5-fold, respectively) compared to healthy breast tissues (control). In the same benign lesions, 6.7-, 4-, and 3.7-fold increase in plasminogen 50 kDa fragment (angiostatin) levels as compared with control were also observed. Activation of matrix metalloproteinase-9, which was detected using gelatine zymography, could be responsible for plasminogen cleavage and abundance of angiostatin infibrocystic and cyst masses. In contrast, dramatic decrease of both plasminogen and angiostatin levels (3.8- and 5.3-folds, respectively) was shown in tissues of proliferatious form of fibroadenoma in comparison with that of the dormant type of this neoplasm. Based on the obtained results, we concluded that angiostatin, a potent vessel growth inhibitor and anti-inflammatory molecule, can play a crucial role in pathophysiology of non-cancerous breast diseases. Further studies are needed to evaluate potential diagnostic and clinical implications of these proteins for prediction and therapy of benign breast pathologies.


Assuntos
Angiostatinas/metabolismo , Cisto Mamário/metabolismo , Neoplasias da Mama/metabolismo , Fibroadenoma/metabolismo , Doença da Mama Fibrocística/metabolismo , Plasminogênio/metabolismo , Cisto Mamário/irrigação sanguínea , Cisto Mamário/patologia , Neoplasias da Mama/irrigação sanguínea , Neoplasias da Mama/patologia , Feminino , Fibroadenoma/irrigação sanguínea , Fibroadenoma/patologia , Doença da Mama Fibrocística/irrigação sanguínea , Doença da Mama Fibrocística/patologia , Humanos , Immunoblotting
2.
Biomed Khim ; 60(5): 602-7, 2014.
Artigo em Russo | MEDLINE | ID: mdl-25386891

RESUMO

The method of extraction and purification of thiamine pyrophosphokinase from non-malignant and tumor tissue of myometrium has been elaborated. Kinetic characteristics of T-kinase from non-malignant and tumor tissue of women myometrium have been studied. It has been shown, that malignization of myometrium is accompanied by a decrease in affinity of thiamine pyrophosphokinase from tumor to thiamine and by an increase in sensitivity of the enzyme from tumor to thiochrome.


Assuntos
Leiomiossarcoma/enzimologia , Miométrio/enzimologia , Tiamina Pirofosfoquinase/metabolismo , Neoplasias Uterinas/enzimologia , Estudos de Casos e Controles , Feminino , Humanos , Tiamina Pirofosfoquinase/antagonistas & inibidores , Tiamina/análogos & derivados , Tiamina/farmacologia
3.
Biomed Khim ; 54(2): 167-78, 2008.
Artigo em Russo | MEDLINE | ID: mdl-18522218

RESUMO

The literature and our experimantal data about the role of carboxypeptidases in carcinogenesis have been reviewed. Activity of all groups of the enzymes increases under development of different tumors. In some cases it is possible to suppose existence of protective role of these enzymes which is directed to inhibition of tumor development.


Assuntos
Carboxipeptidases/fisiologia , Transformação Celular Neoplásica , Neoplasias/enzimologia , Humanos , Neoplasias/patologia
4.
Biomed Khim ; 53(2): 205-11, 2007.
Artigo em Russo | MEDLINE | ID: mdl-17639722

RESUMO

The correlation between activity of trypsyn-like proteases, carboxypeptidases A and B and estrogen level in the womb body has been studied. Correlation analysis suggest the existence of induction of trypsyn-like proteases by estrogens, these proteases activate carboxypeptidases A and B. It has been shown, that carboxypeptidases can play sufficient role in the malignisation process.


Assuntos
Carboxipeptidase B/biossíntese , Carboxipeptidases A/biossíntese , Neoplasias do Endométrio/enzimologia , Estrogênios/metabolismo , Regulação Neoplásica da Expressão Gênica , Serina Endopeptidases/biossíntese , Indução Enzimática , Feminino , Humanos
5.
Ukr Biokhim Zh (1999) ; 76(2): 124-7, 2004.
Artigo em Russo | MEDLINE | ID: mdl-15915724

RESUMO

Activity and optimal pH of cathepsin-L-like proteinases was studied in benign and malignant tumours of the womb body. In the benign tumors activity of cathepsin-L-like proteinases changes depending on the expansion and depth of extension benign tumour and is defined by proliferative potential of tumour cells of myometrium and endometrium. Activity of cathepsin-L-like proteinases in malignant epithelial tumour of endometrium--adenocarcinoma is inversely proportional to the level of differentiation of the tumour cells.


Assuntos
Envelhecimento , Catepsinas/metabolismo , Cisteína Endopeptidases/metabolismo , Leiomioma/enzimologia , Neoplasias Uterinas/enzimologia , Adulto , Idoso , Envelhecimento/metabolismo , Envelhecimento/patologia , Estudos de Casos e Controles , Catepsina L , Diferenciação Celular , Proliferação de Células , Endométrio/enzimologia , Feminino , Humanos , Leiomioma/patologia , Pessoa de Meia-Idade , Miométrio/enzimologia , Neoplasias Uterinas/patologia
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