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After sonication and digestion of nuclei with micrococcal nuclease, the solubilized receptor was applied to a column of Matrex Gel Green A and eluted with a linear gradient of 0‐2 M NaCl. Characterized by specific binding of dihydrotestosterone, this form of the receptor was also androgen dependent and yielded an apparent M\u003Cjats:sub>r\u003C\u002Fjats:sub> of 33,000 when analyzed by polyacrylamide gel electrophoresis and silver nitrate staining. To facilitate recovery following chromatography, the receptor was precipitated with 0‐40% ammonium sulfate. Analysis of the 15‐fold enriched fraction by sucrose density‐gradient centrifugation confirmed the presence of a 3S androgen‐binding protein. About 200 ng of the precipitated protein was applied to a column of dihydrotestosterone‐17 β‐succinyl agarose (ligand concentration, 0.25 μmol\u002Fml). The fractions eluted with 50 μM dihydrotestosterone were electrophoresed and stained as before; again, the presence of a 33,000 M\u003Cjats:sub>r\u003C\u002Fjats:sub> protein sensitive to castration was demonstrated. Alternatively, when the precipitated protein was fractionated by fast protein liquid chromatography utilizing a Superose\u003Cjats:sup>TM\u003C\u002Fjats:sup> 12 HR 10\u002F30 column, the receptor coeluted with nuclear proteins in the 29,000–36,000 M\u003Cjats:sub>r\u003C\u002Fjats:sub> range as determined both by retention time and electrophoresis. In combination, the above methods may be used to obtain a receptor protein purified to near homogeneity with a yield of 5‐10%. The amount of receptor afforded by the purification sequence is small but nevertheless sufficient for chemical detection. We anticipate that with modification, the procedures may prove suitable for the recovery of nuclear androgen receptor on a preparative scale.\u003C\u002Fjats:p>",{"EN":124},"Chemical demonstration of nuclear androgen receptor following affinity chromatography with immobilized ligands",{"VOID":126},"3588412",{"VOID":128},"10.1002\u002Fpros.2990100304","PUBLICATION","VERIFIED","Auto Verify",[133],"EN","https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fpros.2990100304",[136,157,178,194,210,227],{"id":137,"sortIndex":138,"researcher":23,"roles":139,"affiliations":140,"properties":152},"5ff2639b-09f5-470d-b96d-f36709d84aea",3,[],[141],{"id":142,"sortIndex":24,"affiliation":143,"properties":23},"34910e92-453c-4631-9538-2efe43c4d94f",{"id":144,"createTime":145,"updateTime":146,"relativeEntities":147,"slug":148,"properties":149,"entityType":51,"verifyStatus":22,"verifyTime":23,"verifyNote":23,"syncStatus":22,"languages":23,"translateLanguages":23,"viewCount":24},"67cf20f5-594a-4775-9d19-1a08af7eb393","2024-01-09T14:35:14.876+00:00","2024-10-13T21:45:57.552+00:00",[],"Department-of-Cancer-Endocrinology-Cancer-Control-Agency-of-British-Columbia-Vancouver",{"title":150},{"VI":151},"Department of Cancer Endocrinology, Cancer Control Agency of British Columbia, Vancouver",{"openalex":153,"title":155},{"VOID":154},"A5077669541",{"EN":156},"Robert Snoek",{"id":158,"sortIndex":159,"researcher":23,"roles":160,"affiliations":161,"properties":173},"bb56b2fd-d869-4960-aaeb-1bc8331f01f6",4,[],[162],{"id":163,"sortIndex":24,"affiliation":164,"properties":23},"55bdddda-4267-45a7-a768-c09d5eaa08a0",{"id":165,"createTime":166,"updateTime":167,"relativeEntities":168,"slug":169,"properties":170,"entityType":51,"verifyStatus":22,"verifyTime":23,"verifyNote":23,"syncStatus":22,"languages":23,"translateLanguages":23,"viewCount":24},"26daa7a7-bf0a-44ea-ad03-8f54bbcc761e","2024-01-03T16:18:09.679+00:00","2024-10-13T21:45:57.605+00:00",[],"Department-of-Medical-Biochemistry-University-of-Calgary-Calgary-Alberta-Canada-",{"title":171},{"VI":172},"Department of Medical Biochemistry, University of Calgary, Calgary, Alberta, Canada.",{"openalex":174,"title":176},{"VOID":175},"A5023724803",{"EN":177},"Yvonne A. 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10.1016\u002FS0021-9258(17)39217-7",{"doi":324},"10.1016\u002FS0021-9258(17)39217-7",{"id":23,"text":326,"url":23,"identifiers":327},"10.1002\u002Fpros.2990030609",{"doi":326},{"id":23,"text":329,"url":23,"identifiers":330},"10.1111\u002Fj.1432-1033.1981.tb05717.x",{"doi":329},{"id":23,"text":332,"url":23,"identifiers":333},"10.1111\u002Fj.1462-5822.2007.00901.x",{"doi":332},{"id":23,"text":335,"url":23,"identifiers":336},"10.1016\u002F0003-2697(76)90527-3",{"doi":335},{"id":23,"text":338,"url":23,"identifiers":339},"Fulton S, 1980, Dye‐Ligand Chromatography",{},{"id":23,"text":341,"url":23,"identifiers":342},"10.1042\u002Fbj1740009",{"doi":341},{"id":23,"text":344,"url":23,"identifiers":345},"10.1002\u002Fpros.2990050202",{"doi":344},{"id":23,"text":347,"url":23,"identifiers":348},"10.1042\u002Fbj2000465",{"doi":347},{"id":23,"text":350,"url":23,"identifiers":351},"10.1016\u002F0022-4731(82)90039-5",{"doi":350},{"id":23,"text":353,"url":23,"identifiers":354},"RenniePS BowdenJ‐F BruchovskyN FrenetteP‐S FoekensJA ChengH: DNA and protein components of nuclear acceptor sites for androgen receptors in the rat prostate.J Steroid Biochem in press.",{},{"id":23,"text":356,"url":23,"identifiers":357},"10.1016\u002F0167-4781(84)90130-1",{"doi":356},false,{"id":360,"createTime":361,"updateTime":361,"relativeEntities":362,"slug":363,"properties":364,"entityType":129,"verifyStatus":130,"verifyTime":378,"verifyNote":131,"syncStatus":22,"languages":379,"translateLanguages":23,"viewCount":24,"primaryUrl":380,"fullTextUrl":23,"authors":381,"publicationType":243,"publisherRelationship":475,"citationCount":508,"citationInfo":509,"publishDate":512,"publishYear":513,"citationAnalyzeStatus":22,"lastCitationAnalyze":23,"indexDatabases":23,"openAccess":23,"references":514,"isForceReanalyzing":358},"a99ba0de-7816-4041-8ece-c6eb4d7bdf63","2024-09-03T21:36:13.070+00:00",[],"Inhibitors-of-apoptosis-proteins-in-prostate-cancer-cell-lines",{"mag":365,"keywords":367,"openalex":368,"abstract":370,"title":372,"pm":374,"doi":376},{"VOID":366},"2113148441",{},{"VOID":369},"W2113148441",{"EN":371},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:sec>\u003Cjats:title>BACKGROUND\u003C\u002Fjats:title>\u003Cjats:p>The caspases are the central executioners of apoptosis. The inhibitors of apoptosis proteins (IAPs) are a family of recently described caspase inhibitors. We hypothesised that tumor resistance to apoptosis could be due in part to IAP expression.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>METHODS\u003C\u002Fjats:title>\u003Cjats:p>The expression of NAIP, cIAP‐1, cIAP‐2, XIAP, and survivin was investigated in the prostate cancer cell lines LNCaP, PC3, and DU145. RNase protection assays and Western blotting were used to assess RNA and protein expression. Apoptotic susceptibility was determined using etoposide and assessed by propidium iodide (PI) DNA incorporation using flow cytometry.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>RESULTS\u003C\u002Fjats:title>\u003Cjats:p>DU145 and PC3 cells were more resistant to apoptosis than LNCaP cells. All the IAPs were identified in the cell lines with variation in IAP expression between different cell types. Immunohistochemistry demonstrated cIAP‐1 expression in PC3 cells was nuclear, while the expression of cIAP‐2 and XIAP was perinuclear. Growing LNCaP cells in charcoal‐stripped or androgen‐supplemented medium resulted in no alteration in IAP expression.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>CONCLUSIONS\u003C\u002Fjats:title>\u003Cjats:p>This study characterises the expression of IAP in three of the most commonly used prostate cancer cells. IAP may make an important contribution to apoptotic resistance in patients with prostate cancer. 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Cancer Res, 60, 2547",{},{"id":23,"text":617,"url":23,"identifiers":618},"Hiromitsu M, 2000, Expression of the IAP (inhibitor of apoptosis protein) gene family in prostate cancer, Eur Urol, 37, 104",{},{"id":23,"text":620,"url":23,"identifiers":621},"10.1038\u002F25141",{"doi":620},{"id":23,"text":623,"url":23,"identifiers":624},"Tang DG, 1998, Extended survivability of prostate cancer cells in the absence of trophic factors: increased proliferation, evasion of apoptosis, and the role of apoptosis proteins, Cancer Res, 58, 3466",{},{"id":23,"text":626,"url":23,"identifiers":627},"Berchem G, 1995, Androgens induce resistance to Bcl‐2‐mediated apoptosis in LNCaP prostate cancer cells, Cancer Res, 55, 735",{},{"id":23,"text":629,"url":23,"identifiers":630},"Tso C, 2000, Androgen deprivation induces selective outgrowth of aggressive hormone‐refractory prostate cancer clones expressing distinct cellular and molecular properties not present in parental androgen‐dependent cancer cells, Cancer J, 6, 213",{},{"id":23,"text":632,"url":23,"identifiers":633},"Krajewska M, 1996, Immunohistochemical analysis of Bcl‐2, bax, Bcl‐x, and mcl‐1 expression in prostate cancers, Am J Pathol, 148, 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androgen receptor (AR) mediates the biological responses of androgens in the prostate gland. In prostate cancer, this pathway is often deregulated and causes an uncontrolled proliferation.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>METHODS\u003C\u002Fjats:title>\u003Cjats:p>The current study focuses on the effects of an inhibition of protein kinase CK2 on the AR‐mediated transcription in LNCaP prostate cancer cells. We used chemical inhibitors of CK2 as well as dominant‐negative kinase mutants to downregulate the CK2 activity. We determined the effects of the inhibition by Western blot analysis of endogenous target genes of the AR as well as by reporter assays.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>RESULTS\u003C\u002Fjats:title>\u003Cjats:p>We found that inhibition of CK2 led to a downregulation of the AR‐dependent transcription. Moreover, the amount of the AR protein decreased significantly.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>CONCLUSION\u003C\u002Fjats:title>\u003Cjats:p>According to the fact that AR pathways are involved in the development and progression of prostate cancer, the ability to modulate AR function should provide an alternative basis for the development of new cancer therapies. 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II from self‐aggregation and enhances its kinase activity, J Biol Chem, 267, 7042, 10.1016\u002FS0021-9258(19)50533-6",{"doi":853},"10.1016\u002FS0021-9258(19)50533-6",{"id":23,"text":855,"url":23,"identifiers":856},"10.1073\u002Fpnas.94.26.14500",{"doi":855},{"id":23,"text":858,"url":23,"identifiers":859},"10.1074\u002Fjbc.M212260200",{"doi":858},{"id":23,"text":861,"url":23,"identifiers":862},"10.1158\u002F0008-5472.CAN-04-3250",{"doi":861},{"id":23,"text":864,"url":23,"identifiers":865},"Hessenauer A, 2003, CK2‐mediated pathways are interrupted in hormone‐refractory prostate carcinoma cell lines, Int J Oncol, 22, 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for peripheral benzodiazepine receptors (PBZr), binding sites in isolated mitochondrial (m‐fraction) and microsomal fractions (p‐fraction) from R‐3327 Dunning AT‐1 tumors, ventral and dorsolateral prostate were studied. Binding of PK 11195 in both m‐ and p‐fractions from AT‐1 tumors, but only in m‐fraction from ventral and dorsolateral prostate, was specific, saturable, and of high affinity. The PBZr density in m‐fraction from AT‐1 tumors was 6‐fold and 20‐fold higher than that in ventral and dorsolateral prostate, respectively. The receptor density in p‐fraction from AT‐1 tumors was approximately 25% of that found in the m‐fraction. Clear differences were observed in the competition by both diazepam and flunitrazepam for binding sites in m‐ and p‐fractions from tumors. These data indicate that the receptors were not only localized to the mitochondria, but were also present in considerable amounts in the microsomal fractions. The unusually high amounts of receptors in the fast growing anaplastic prostatic tumor suggest their involvement in the regulation of cell proliferation and possibly in tumorigenesis. © 1994 Wiley‐Liss, Inc.\u003C\u002Fjats:p>",{"EN":881},"Characterization of peripheral benzodiazepine receptors in rat prostatic 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RRH, 1986, The peripheral‐type benzodiazepine receptor: Localization to the mitochondrial outer membrane, J Biol Chem, 261, 576, 10.1016\u002FS0021-9258(17)36131-8",{"doi":979},"10.1016\u002FS0021-9258(17)36131-8",{"id":23,"text":981,"url":23,"identifiers":982},"10.1111\u002Fj.1471-4159.1986.tb12965.x",{"doi":981},{"id":23,"text":984,"url":23,"identifiers":985},"10.1016\u002F0024-3205(83)90063-2",{"doi":984},{"id":23,"text":987,"url":23,"identifiers":988},"10.1073\u002Fpnas.74.9.3805",{"doi":987},{"id":23,"text":990,"url":23,"identifiers":991},"10.1016\u002F0024-3205(87)90307-9",{"doi":990},{"id":23,"text":993,"url":23,"identifiers":994},"10.1159\u002F000125126",{"doi":993},{"id":23,"text":996,"url":23,"identifiers":997},"10.1016\u002FS0140-6736(75)90197-X",{"doi":996},{"id":23,"text":999,"url":23,"identifiers":1000},"10.1016\u002F0014-2999(85)90026-3",{"doi":999},{"id":23,"text":1002,"url":23,"identifiers":1003},"10.1016\u002F0014-2999(87)90210-X",{"doi":1002},{"id":23,"text":1005,"url":23,"identifiers":1006},"10.1073\u002Fpnas.81.3.753",{"doi":1005},{"id":23,"text":1008,"url":23,"identifiers":1009},"10.1002\u002Fjnr.490300303",{"doi":1008},{"id":23,"text":1011,"url":23,"identifiers":1012},"10.1016\u002F0304-3835(90)90146-O",{"doi":1011},{"id":23,"text":1014,"url":23,"identifiers":1015},"10.1042\u002Fcs0780155",{"doi":1014},{"id":23,"text":1017,"url":23,"identifiers":1018},"10.1016\u002F0014-2999(88)90135-5",{"doi":1017},{"id":23,"text":1020,"url":23,"identifiers":1021},"10.1016\u002F0006-2952(90)90321-B",{"doi":1020},{"id":23,"text":1023,"url":23,"identifiers":1024},"10.1016\u002F0306-3623(92)90098-5",{"doi":1023},{"id":23,"text":1026,"url":23,"identifiers":1027},"10.1016\u002F0024-3205(92)90358-V",{"doi":1026},{"id":23,"text":1029,"url":23,"identifiers":1030},"Dunning 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681",{},{"id":23,"text":1053,"url":23,"identifiers":1054},"O'Donnell ME, 1986, Role of cyclic GMP in atrial nartiuretic factor stimulation of Na+, K+, Cl‐ cotransport in vascular smooth muscle cells, J Biol Chem, 261, 15461, 10.1016\u002FS0021-9258(18)66734-1",{"doi":1055},"10.1016\u002FS0021-9258(18)66734-1",{"id":23,"text":1057,"url":23,"identifiers":1058},"Constantinou A, 1990, Induction of differentiation and DNA strand breakage in human HL‐60 and K‐562 leukemia cells by genistein, Cancer Res, 50, 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Exp Ther, 223, 517",{},{"id":23,"text":1087,"url":23,"identifiers":1088},"10.1111\u002Fj.1471-4159.1987.tb01007.x",{"doi":1087},{"id":23,"text":1090,"url":23,"identifiers":1091},"10.1016\u002F0024-3205(91)90090-X",{"doi":1090},{"id":23,"text":1093,"url":23,"identifiers":1094},"10.1210\u002Fendo-116-2-567",{"doi":1093},{"id":23,"text":1096,"url":23,"identifiers":1097},"10.1002\u002Fpros.2990170402",{"doi":1096},{"id":23,"text":1099,"url":23,"identifiers":1100},"10.1073\u002Fpnas.78.6.3935",{"doi":1099},{"id":23,"text":1102,"url":23,"identifiers":1103},"10.1016\u002F0006-8993(91)91369-C",{"doi":1102},{"id":23,"text":1105,"url":23,"identifiers":1106},"Marangos PJ, 1982, Characterization of peripheral‐type benzodiazepine binding sites in brain using [3H]Ro 5‐4864, Mol Pharmacol, 22, 26",{},{"id":23,"text":1108,"url":23,"identifiers":1109},"Schoemaker H, 1983, Specific high‐affinity binding sites for [3H]Ro 5‐4864 in rat brain and kidney, J Pharmacol Exp Ther, 225, 61",{},{"id":23,"text":1111,"url":23,"identifiers":1112},"Starosta‐Rubinstein S, 1987, Imaging of a glioma using peripheral benzodiazepine receptor ligands, Neurobiology, 84, 891",{},{"id":23,"text":1114,"url":23,"identifiers":1115},"10.1111\u002Fj.1471-4159.1983.tb00888.x",{"doi":1114},{"id":23,"text":1117,"url":23,"identifiers":1118},"10.1016\u002F0883-2897(89)90111-6",{"doi":1117},{"id":23,"text":1120,"url":23,"identifiers":1121},"10.1016\u002F0014-2999(89)90843-1",{"doi":1120},{"id":23,"text":1123,"url":23,"identifiers":1124},"Hirsch JD, 1989, Mitochondrial benzodiazepine receptors mediate inhibition of mitochondrial respiratory control, Mol Pharmacol, 35, 157",{},{"id":23,"text":1126,"url":23,"identifiers":1127},"SnyderSH VermaA TrifilettiRR: The peripheral‐type benzodiazepine receptor: A protein of mitochondrial outer membranes utilizing porphyrins as endogenous ligands.FASEB J1282 1987.",{"doi":1128},"10.1096\u002Ffasebj.1.4.2820823",{"id":1130,"createTime":1131,"updateTime":1131,"relativeEntities":1132,"slug":1133,"properties":1134,"entityType":129,"verifyStatus":130,"verifyTime":1131,"verifyNote":131,"syncStatus":22,"languages":1148,"translateLanguages":23,"viewCount":24,"primaryUrl":1149,"fullTextUrl":23,"authors":1150,"publicationType":243,"publisherRelationship":1320,"citationCount":1352,"citationInfo":1353,"publishDate":1355,"publishYear":1356,"citationAnalyzeStatus":22,"lastCitationAnalyze":23,"indexDatabases":23,"openAccess":23,"references":1357,"isForceReanalyzing":358},"6b5faa7f-7e14-43c1-b4a0-9ee101b642a0","2024-11-26T21:12:37.466+00:00",[],"Transrectal-ultrasound-in-the-diagnosis-of-prostate-cancer-Location-echogenicity-histopathology-and-staging",{"mag":1135,"keywords":1137,"openalex":1138,"abstract":1140,"title":1142,"pm":1144,"doi":1146},{"VOID":1136},"2065450760",{},{"VOID":1139},"W2065450760",{"EN":1141},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:p>Adenocarcinoma of the prostate produces specific ultrasonic findings that can be used in diagnosis. We have examined 211 patients using transrectal ultrasound in both the sagittal and axial planes. Thirty‐three carcinomas were detected, and 31 histologically confirmed; 24 by needle biopsy, six by transurethral resection, one by total prostatectomy, and two by the demonstration of distant metatases. On ultrasound, all of the carcinomas were less echogenic than normal prostate. All appeared to originate in the peripheral zone of the prostate and produced asymmetry of the gland. The majority of carcinomas in this series showed capsular involvement and ten penetrated and extended beyond the prostatic capsule.\u003C\u002Fjats:p>\u003Cjats:p>The results of this series indicate that transrectal ultrasound can be used to detect cancer of the prostate gland. 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effect of [D‐Leu\u003Cjats:sup>6\u003C\u002Fjats:sup>, des‐Gly‐NH\u003Cjats:sub>2\u003C\u002Fjats:sub>\u003Cjats:sup>10\u003C\u002Fjats:sup>, Proethylamide\u003Cjats:sup>9\u003C\u002Fjats:sup>]‐GnRH, leuprolide, was determined for the human primary prostate tumor cell line ALVA‐31 by in vitro mitogenic assays. Prostate tumor cell proliferation was inhibited up to 50% by leuprolide. Inhibition was not observed in parallel cultures treated with other low molecular weight bioactive peptides. The incorporation and metabolic reduction of testosterone was not affected by concentrations of leuprolide that were inhibitory in the mitogenic assay. Specific high‐affinity binding of \u003Cjats:sup>125\u003C\u002Fjats:sup>I‐labeled leuprolide was also demonstrated on intact tumor cells with an estimated effective median dose (ED\u003Cjats:sub>50\u003C\u002Fjats:sub>) of <1 × 10\u003Cjats:sup>–9\u003C\u002Fjats:sup>M. Inhibition of prostate tumor growth was further demonstrated in Balb\u002Fc athymic intact and castrate male mice bearing ALVA‐31 tumor xenografts following chronic administration of leuprolide. These data clearly demonstrate that leuprolide can inhibit the growth of a human prostate carcinoma cell line. 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is a member of the endoplasmatic reticulum protein disulphide isomerase gene family implicated in tumor metastasis. Its expression pattern, function, and utility as a marker remains to be further investigated.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>METHODS\u003C\u002Fjats:title>\u003Cjats:p>Using real‐time RT‐PCR and immunohistochemistry, changes of expression in different tumor stages were explored in microdissected tumor samples. AGR2 transcript level in urine sediments was scrutinized for suitability as a tumor marker. AGR2 androgen regulation and function were analyzed in cellular prostate cancer models.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>RESULTS\u003C\u002Fjats:title>\u003Cjats:p>AGR2 is highly expressed in prostate cancer compared to benign tissue in particular also in low‐grade tumors and PIN lesions. AGR2 transcripts were detected in urine sediments of patients undergoing prostate biopsy with significantly higher levels in tumor patients. The urine AGR2\u002FPSA transcript ratio allowed much better discrimination between cancer and benign patients than serum total PSA or %freePSA. Prostate tumor cells express and secrete variable amounts of AGR2 protein, the highest level was found in PC3 cells. In androgen receptor‐positive cell lines AGR2 is upregulated by androgens. Increased expression enhanced the migratory and invasive potential but decreased growth and proliferation in vitro and in vivo.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>CONCLUSION\u003C\u002Fjats:title>\u003Cjats:p>AGR2 enhances the invasion phenotype of prostate cancer cells while at the same time attenuating cell‐cycle progression. This function, its expression pattern and the increased level of AGR transcripts in urine sediments of prostate cancer patients call for further exploration as a prostate cancer marker and a modulator of tumor growth and invasion. 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Foxa family (a1, a2, and a3) of proteins are transcription factors that are central to endodermal development. Recently, Foxa1 has been shown to regulate the transcription of several murine and human prostate specific genes involved in differentiated function by interacting with DNA promoter sequences and androgen receptors. Currently, the developmental expression pattern of Foxa proteins in the murine prostate is unknown.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>Methods\u003C\u002Fjats:title>\u003Cjats:p>Male CD‐1 mice (embryonic, prepubertal, pubertal, and adult) were used for immunohistochemical analysis of Foxa1, a2, and a3. Immunofluorescence was also performed for androgen receptor and cytokeratin 14 expression. Prostate tissue from pre‐pubertal, pubertal, and adult mice were analyzed by Western blot and RT‐PCR analysis for Foxa1, a2, and a3 expression.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>Results\u003C\u002Fjats:title>\u003Cjats:p>Strong Foxa1 immunoreactivity was observed in epithelial cells throughout prostate development, growth, and adult differentiation. Prominent Foxa2 protein expression was only observed in the early stages of prostate development and was exclusively localized to epithelial cells of the forming buds. RT‐PCR analysis identified low Foxa2 mRNA expression levels in the ventral and dorsolateral lobes of the adult prostate, with Foxa2 epithelial cell expression being localized to periurethral regions of the murine adult prostatic complex. Foxa3 expression was not observed in the murine prostate.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>\u003Cjats:sec>\u003Cjats:title>Conclusions\u003C\u002Fjats:title>\u003Cjats:p>Foxa proteins represent epithelial cell markers in the murine prostate gland. The early expression of Foxa1 and a2 proteins in prostate formation suggests that these proteins play an important role in normal prostate development, in addition to differentiated secretory function. © 2004 Wiley‐Liss, Inc.\u003C\u002Fjats:p>\u003C\u002Fjats:sec>",{"EN":2408},"Expression of Foxa transcription factors in the developing and adult murine 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of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, Tennessee",{"openalex":2457,"orcid":2459,"title":2461},{"VOID":2458},"A5038078180",{"VOID":2460},"https:\u002F\u002Forcid.org\u002F0000-0003-4264-7438",{"EN":2462},"Nan Gao",{"id":2464,"sortIndex":180,"researcher":23,"roles":2465,"affiliations":2466,"properties":2500},"6ccc227e-c5c8-41e7-bae2-8893c4dd5f29",[],[2467,2477,2488,2494],{"id":2468,"sortIndex":180,"affiliation":2469,"properties":23},"017638cb-6432-4ea8-bef2-9723e3e6e83c",{"id":2470,"createTime":2471,"updateTime":2471,"relativeEntities":2472,"slug":2473,"properties":2474,"entityType":51,"verifyStatus":22,"verifyTime":23,"verifyNote":23,"syncStatus":22,"languages":23,"translateLanguages":23,"viewCount":24},"952f456b-9567-4884-a1e8-094c1cf64125","2024-10-09T20:00:34.577+00:00",[],"The-Vanderbilt-Ingram-Cancer-Center-Vanderbilt-University-Nashville-Tennessee",{"title":2475},{"EN":2476},"The Vanderbilt Ingram Cancer Center, Vanderbilt University, 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