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Estrogen receptors regulate galectin‑3 in androgen‑independent DU‑145 prostate cancer cells. 2023

Deborah S Souza, and Carla Macheroni, and Carolina M Vicente, and Renan P Cavalheiro, and Vanessa L Campo, and Catarina S Porto
Laboratory of Experimental Endocrinology, Department of Pharmacology, Paulista School of Medicine (EPM), Federal University of São Paulo (UNIFESP), São Paulo, SP 04039‑032, Brazil.

The aim of the present study was to investigate the role of estrogen receptor (ER)α and ERβ, and galectin‑3 (GAL‑3) in migration and invasion of androgen‑independent DU‑145 prostate cancer cells, and to examine the regulation of the expression of GAL‑3 by the activation of these receptors. Wound healing and cell invasion assays were performed using the control (basal level of cellular function) and treated DU‑145 cells. At 24 h of treatment, 17β‑estradiol (E2), the ERα‑selective agonist, 4,4',4"‑(4‑propyl‑(1H)‑pyrazole‑1,3,5‑triyl)trisphenol (PPT), or the ERβ‑selective agonist, 2,3‑bis(4‑hydroxyphenyl)‑propionitrile (diarylprepionitrile; DPN), increased the migration and invasion of the DU‑145 cells. Pre‑treatment with the ERα‑ and ERβ‑selective antagonists blocked these effects, indicating that ERα and ERβ are upstream receptors regulating these processes. Western blot analysis and immunofluorescence staining for the detection of the GAL‑3 were performed using the control and treated DU‑145 cells. Treatment of the DU‑145 cells with E2, PPT or DPN for 24 h increased the expression of the GAL‑3 compared to the control. Furthermore, a specific inhibitor of GAL‑3 (VA03) inhibited the migration and invasion of DU‑145 cells, indicating the involvement of the complex ERα/GAL‑3 and ERβ/GAL‑3 in the regulation of these processes. On the whole, the present study demonstrates that the activation of both ERs increases the expression and signaling of GAL‑3, and promotes the migration and invasion of DU‑145 cells. The findings of the present study provide novel insight into the signatures and molecular mechanisms of ERα and ERβ in DU‑145 cells.

UI MeSH Term Description Entries
D008297 Male Males
D011471 Prostatic Neoplasms Tumors or cancer of the PROSTATE. Cancer of Prostate,Prostate Cancer,Cancer of the Prostate,Neoplasms, Prostate,Neoplasms, Prostatic,Prostate Neoplasms,Prostatic Cancer,Cancer, Prostate,Cancer, Prostatic,Cancers, Prostate,Cancers, Prostatic,Neoplasm, Prostate,Neoplasm, Prostatic,Prostate Cancers,Prostate Neoplasm,Prostatic Cancers,Prostatic Neoplasm
D011960 Receptors, Estrogen Cytoplasmic proteins that bind estrogens and migrate to the nucleus where they regulate DNA transcription. Evaluation of the state of estrogen receptors in breast cancer patients has become clinically important. Estrogen Receptor,Estrogen Receptors,Estrogen Nuclear Receptor,Estrogen Receptor Type I,Estrogen Receptor Type II,Estrogen Receptors Type I,Estrogen Receptors Type II,Receptor, Estrogen Nuclear,Receptors, Estrogen, Type I,Receptors, Estrogen, Type II,Nuclear Receptor, Estrogen,Receptor, Estrogen
D004958 Estradiol The 17-beta-isomer of estradiol, an aromatized C18 steroid with hydroxyl group at 3-beta- and 17-beta-position. Estradiol-17-beta is the most potent form of mammalian estrogenic steroids. 17 beta-Estradiol,Estradiol-17 beta,Oestradiol,17 beta-Oestradiol,Aerodiol,Delestrogen,Estrace,Estraderm TTS,Estradiol Anhydrous,Estradiol Hemihydrate,Estradiol Hemihydrate, (17 alpha)-Isomer,Estradiol Monohydrate,Estradiol Valerate,Estradiol Valeriante,Estradiol, (+-)-Isomer,Estradiol, (-)-Isomer,Estradiol, (16 alpha,17 alpha)-Isomer,Estradiol, (16 alpha,17 beta)-Isomer,Estradiol, (17-alpha)-Isomer,Estradiol, (8 alpha,17 beta)-(+-)-Isomer,Estradiol, (8 alpha,17 beta)-Isomer,Estradiol, (9 beta,17 alpha)-Isomer,Estradiol, (9 beta,17 beta)-Isomer,Estradiol, Monosodium Salt,Estradiol, Sodium Salt,Estradiol-17 alpha,Estradiol-17beta,Ovocyclin,Progynon-Depot,Progynova,Vivelle,17 beta Estradiol,17 beta Oestradiol,Estradiol 17 alpha,Estradiol 17 beta,Estradiol 17beta,Progynon Depot
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000728 Androgens Compounds that interact with ANDROGEN RECEPTORS in target tissues to bring about the effects similar to those of TESTOSTERONE. Depending on the target tissues, androgenic effects can be on SEX DIFFERENTIATION; male reproductive organs, SPERMATOGENESIS; secondary male SEX CHARACTERISTICS; LIBIDO; development of muscle mass, strength, and power. Androgen,Androgen Receptor Agonist,Androgen Effect,Androgen Effects,Androgen Receptor Agonists,Androgenic Agents,Androgenic Compounds,Agents, Androgenic,Agonist, Androgen Receptor,Agonists, Androgen Receptor,Compounds, Androgenic,Effect, Androgen,Effects, Androgen,Receptor Agonist, Androgen,Receptor Agonists, Androgen
D047628 Estrogen Receptor alpha One of the ESTROGEN RECEPTORS that has marked affinity for ESTRADIOL. Its expression and function differs from, and in some ways opposes, ESTROGEN RECEPTOR BETA. ERalpha,Estradiol Receptor alpha,Estrogen Receptor 1,Estrogen Receptors alpha,Receptor alpha, Estrogen,Receptor alpha, Estradiol,alpha, Estradiol Receptor
D047629 Estrogen Receptor beta One of the ESTROGEN RECEPTORS that has greater affinity for ISOFLAVONES than ESTROGEN RECEPTOR ALPHA does. There is great sequence homology with ER alpha in the DNA-binding domain but not in the ligand binding and hinge domains. ERbeta,ERbetacx,Estrogen Receptor 2,Estrogen Receptors beta,Receptor beta, Estrogen
D037502 Galectin 3 A multifunctional galactin initially discovered as a macrophage antigen that binds to IMMUNOGLOBULIN E, and as 29-35-kDa lectin that binds LAMININ. It is involved in a variety of biological events including interactions with galactose-containing glycoconjugates, cell proliferation, CELL DIFFERENTIATION, and APOPTOSIS. Mac-2 Antigen,CBP-30,CBP-35,CBP35,Carbohydrate-Binding Protein 35,Epsilon-Binding Protein,Galectin-3,HL-29,IgE Binding Protein,IgEBP,L-29 Lectin,L-31,L-34,L30 Lectin,LGALS3,Macrophage-2 Antigen,Antigen, Mac-2,Antigen, Macrophage-2,Binding Protein, IgE,Carbohydrate Binding Protein 35,Epsilon Binding Protein,L 29 Lectin,Mac 2 Antigen,Macrophage 2 Antigen,Protein, IgE Binding

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