TY - JOUR
TI - Sex steroid receptors in skeletal differentiation and epithelial neoplasia: Is tissue-specific intervention possible?
AU - Copland, J.A.
AU - Sheffield-Moore, M.
AU - Koldzic-Zizanovic, N.
AU - Gentry, S.
AU - Lamprou, G.
AU - Tzortzatou-Stathopoulou, F.
AU - Zoumpourlis, V.
AU - Urban, R.J.
AU - Vlahopoulos, S.A.
JO - BioEssays
PY - 2009
VL - 31
TODO - 6
SP - 629-641
PB - 
SN - 0265-9247, 1521-1878
TODO - 10.1002/bies.200800138
TODO - androgen;  androgen receptor;  BRCA1 protein;  cyclin D1;  estrogen;  estrogen receptor;  finasteride;  letrozole;  protein inhibitor of activated STAT;  raloxifene;  selective estrogen receptor modulator;  sex hormone;  steroid receptor;  steroid receptor coactivator 1;  tamoxifen;  sex hormone;  steroid receptor, bone development;  bone growth;  breast cancer;  cancer risk;  carcinogenesis;  cytology;  drug mechanism;  enzyme inhibition;  hormone action;  human;  molecular biology;  muscle development;  muscle growth;  prostate cancer;  protein function;  protein protein interaction;  regulatory mechanism;  review;  tissue differentiation;  animal;  bone;  chemical structure;  chemistry;  genetics;  metabolism;  neoplasm;  pathology;  physiology;  protein conformation;  signal transduction;  skeletal muscle, Animals;  Bone and Bones;  Gonadal Steroid Hormones;  Humans;  Models, Molecular;  Muscle, Skeletal;  Neoplasms, Glandular and Epithelial;  Osteogenesis;  Protein Conformation;  Receptors, Steroid;  Signal Transduction
TODO - Sex steroids, through their receptors, have potent effects on the signal pathways involved in osteogenic or myogenic differentiation. However, a considerable segment of those signal pathways has a prominent role in epithelial neoplastic transformation. The capability to intervene locally has focused on specific ligands for the receptors. Nevertheless, many signals are mapped to interactions of steroid receptor motifs with heterologous regulatory proteins. Some of those proteins interact with the glucocorticoid receptor and other factors essential to cell fate. Interactions of steroid receptor domain motifs with heterologous proteins affect specific target pathways; consequently, manipulation of specified protein modules complexed with steroid receptors may be a next major step for enhancing molecular targeted therapeutics. In the future, intervention at specific sections of receptor primary sequence may prove therapeutically more efficient in targeting pathways of choice than ligand selectivity can be. © 2009 Wiley Periodicals, Inc.
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