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1.
Braz. j. med. biol. res ; 33(11): 1387-91, Nov. 2000. ilus, graf
Article in English | LILACS | ID: lil-273213

ABSTRACT

Endometrium is one of the fastest growing human tissues. Sex hormones, estrogen and progesterone, in interaction with several growth factors, control its growth and differentiation. Insulin-like growth factor 1 (IGF-1) interacts with cell surface receptors and also with specific soluble binding proteins. IGF-binding proteins (IGF-BP) have been shown to modulate IGF-1 action. Of six known isoforms, IGF-BP-1 has been characterized as a marker produced by endometrial stromal cells in the late secretory phase and in the decidua. In the current study, IGF-1-BP concentration and affinity in the proliferative and secretory phase of the menstrual cycle were measured. Endometrial samples were from patients of reproductive age with regular menstrual cycles and taking no steroid hormones. Cytosolic fractions were prepared and binding of 125I-labeled IGF-1 performed. Cross-linking reaction products were analyzed by SDS-polyacrylamide gel electrophoresis (7.5 percent) followed by autoradiography. 125I-IGF-1 affinity to cytosolic proteins was not statistically different between the proliferative and secretory endometrium. An approximately 35-kDa binding protein was identified when 125I-IGF-1 was cross-linked to cytosol proteins. Secretory endometrium had significantly more IGF-1-BP when compared to proliferative endometrium. The specificity of the cross-linking process was evaluated by the addition of 100 nM unlabeled IGF-1 or insulin. Unlabeled IGF-1 totally abolished the radioactivity from the band, indicating specific binding. Insulin had no apparent effect on the intensity of the labeled band. These results suggest that IGF-BP could modulate the action of IGF-1 throughout the menstrual cycle. It would be interesting to study this binding protein in other pathologic conditions of the endometrium such as adenocarcinomas and hyperplasia


Subject(s)
Humans , Female , Cytosol/metabolism , Endometrium/metabolism , Insulin-Like Growth Factor Binding Protein 1/metabolism , Menstrual Cycle/metabolism , Affinity Labels , Autoradiography , Cytosol/metabolism , Electrophoresis, Polyacrylamide Gel , Endometrium/metabolism , Insulin-Like Growth Factor Binding Protein 1/metabolism , Membrane Proteins , Sensitivity and Specificity
2.
Braz. j. med. biol. res ; 29(12): 1593-7, Dec. 1996. ilus, graf
Article in English | LILACS | ID: lil-188439

ABSTRACT

Colon carcinoma is the most common tumor of the gastrointestinal tract. According to some investigators, insulin, epidermal growth factor (EGF) and insulin-like growth factor I (IGF-I) may be involved in the neoplastic proliferation. Insulin-binding and receptor tyrosine kinase activity were investigated in colon carcinomas and in normal colons. The insulin receptor concentration, as shown by binding assays, was 17.4 ñ 4.3 fmol/mug in normal colon and 29.69 ñ 9.4 fmol/mug in colon carcinoma. Nevertheless, the insulin affinity of the receptor was similar in both groups (Kd ( 1 nM). Both normal and neoplastic colon showed phosphorylation of the insulin receptor. The electrophoretic migration of the Beta-subunit of the insulin receptors purified from colon carcinomas was similar to that of normal colon and both tissues demonstrated an insulin-dependent autophosphorylation. The receptor tyrosine kinase activity was measured by the incorporation of [gamma32P]ATP into the Beta-subunit. The basal and the insulin-stimulated tyrosine kinase activities were significantly higher in colon carcinomas compared to normal colon tissues (2.2 and 1.6 times, respectively). Understanding the metabolism of neoplastic cells may contribute to the development of prevention strategies as well as new therapies. It is now necessary to study other steps of the insulin signal transduction pathway, such as insulin receptor substrate 1 phosphorylation.


Subject(s)
Humans , Colonic Neoplasms/chemistry , In Vitro Techniques , Receptor, Insulin/analysis , Wheat Germ Agglutinins
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