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Stephen P. Ethier's Endocrine Oncology (Contemporary Endocrinology) PDF

By Stephen P. Ethier

ISBN-10: 0896036219

ISBN-13: 9780896036215

ISBN-10: 1592592236

ISBN-13: 9781592592234

Stephen P. Ethier and a panel of best investigators comprehensively research the mobile, molecular, and endocrine components within the improvement of cancers of the breast, prostate, endometrium, and ovary. targeting defining crucial unresolved matters within the box, the authors assessment how steroid hormones functionality to manage basic mammary gland homeostasis in people, with specific emphasis at the roles of estrogen, progesterone, and development elements. accomplished and updated, Endocrine Oncology bargains either easy and scientific researchers not just the newest molecular and mobile findings on endocrine cancers, but in addition a robust severe research that would turn out beneficial to all endocrinologists and oncologists operating within the zone this present day.

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Triple primer polymerase chain reaction. A new way to quantify truncated mRNA expression. Am J Pathol 1996;148:1097–1103. 27. Leygue ER, Watson PH, Murphy LC. Estrogen receptor variants in normal human mammary tissue. J Natl Cancer Inst 1996;88:284–290. 28. Pfeffer U, Fecarotta E, Vidali G. Coexpression of multiple estrogen receptor variant messenger RNAs in normal and neoplastic breast tissues and in MCF-7 cells. Cancer Res 1995;55:2158–2165. 29. Erenburg I, Schachter B, Lopez RM, Ossowski L. Loss of an estrogen receptor isoform (ER-alpha deleted 3) in breast cancer and the consequences of its reexpression: interference with estrogen-stimulated properties of malignant transformation.

N. Hunt, PHD, Eileen M. McGowan, MSC, and Christine L. Clarke, PHD CONTENTS INTRODUCTION PROGESTERONE RECEPTOR PR AND NORMAL MAMMARY GLAND PR IN BC CONCLUSION AND FUTURE PERSPECTIVES REFERENCES INTRODUCTION The ovarian steroid hormone, progesterone (P), being fat-soluble, gains access to the intracellular compartment by diffusion through the lipid bilayer cell membrane. In target tissues such as the breast, it interacts with a specific receptor protein, progesterone receptor (PR), and induces formation of receptor dimers, which bind to palindromic hormone response elements in DNA and affect gene transcription (1,2).

Schematic representation of the ER_ variant proteins predicted to be encoded by ER_ variant mRNAs. Identical sequence is depicted by numbered exons. U, amino acid sequence unrelated to WT human ER_ amino acid sequence. U sequences are unique to any particular variant. The position of N- and C-terminal epitopes, recognized by 1D5 and AER311 Abs, respectively, are indicated. detection of ER_ variant proteins encoded by known ER_ variant mRNAs in tissues or cells in vivo. From a different perspective, the prediction that the majority of ER_ variant proteins are C-terminally truncated has implications for the determination of clinical ER status.

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Endocrine Oncology (Contemporary Endocrinology) by Stephen P. Ethier

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