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Article: Expression study of three secretory proteins (Prostatic secretory protein of 94 amino acids, probasin, and seminal vesicle secretion II) in dysplastic and neoplastic rat prostates

TitleExpression study of three secretory proteins (Prostatic secretory protein of 94 amino acids, probasin, and seminal vesicle secretion II) in dysplastic and neoplastic rat prostates
Authors
Issue Date2003
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/34304
Citation
Prostate, 2003, v. 56 n. 2, p. 81-97 How to Cite?
AbstractBACKGROUND. Prostatic secretory protein of 94 amino acids (PSP94), probasin, and seminal vesicle secretion II (SVSII) are the three major proteins secreted by the lateral lobe of the rat prostate gland. Among these proteins, rodent PSP94 but not probasin and SVSII has a human homologue and it is also a major secretory protein of the human prostate, in addition to prostatic acid phosphatase and prostate-specific antigen. METHODS. In this study, we examined and compared the mRNA expression of these three secretory markers in three rat models of prostate cancer including the sex steroid-induced dysplasia (prostatic intraepithelial neoplasia or PIN) in Noble (Nb) rat model, an androgen-independent Nb rat prostatic tumor (AIT) and Dunning rat prostatic adenocarcinomas (both androgen-dependent and -independent) by in situ hybridization (ISH), reverse transcriptase-polymerase chain reaction (RT-PCR), and immunohistochemistry. RESULTS. The transcripts for the three markers were highly expressed in the secretory epithelium of normal lateral prostate (LP). Their hybridization signals became reduced in the epithelial cells in the low-grade PINs and significantly weakened or lost in the high-grade PINs induced in the LP. Interestingly, we observed that some dysplastic cells located at the basal compartment of the PIN lesions, and nests of outpouching epithelial cells in the vicinity of PINs, expressed positive hybridization signals of three markers. In the adenocarcinoma, signals of probasin but not PSP94 and SVSII were detected. No hybridization signals were detected in both Dunning and AIT tumors. By RT-PCR, transcripts for these proteins were still detected but significantly reduced in the Dunning tumors, whereas in the AIT tumor, only SVSII transcripts were detected. Immunohistochemistry of PSP94 also showed a reduced staining in the PIN lesions, but no immunoreactivity was seen in the rat prostatic tumors. CONCLUSIONS. The mRNA expression of the three prostatic secretory markers were decreased in the hormone-induced PINs and in two rat prostatic tumors, indicating that the androgen-regulated secretory differentiation was impaired during the development of the premalignant lesion and further reduced in advanced tumors. The abnormal expression pattern of these secretory markers and androgen receptor (AR) in the basal compartment of the PIN lesions suggests that there is a population of cell types with secretory phenotype appearing in the basal cell layer during the early malignant transformation of the prostatic epithelium. © 2003 Wiley-Liss, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/67896
ISSN
2015 Impact Factor: 3.778
2015 SCImago Journal Rankings: 1.477
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKwong, Jen_HK
dc.contributor.authorLui, Ken_HK
dc.contributor.authorChan, PSFen_HK
dc.contributor.authorHo, SMen_HK
dc.contributor.authorWong, YCen_HK
dc.contributor.authorXuan, JWen_HK
dc.contributor.authorChan, FLen_HK
dc.date.accessioned2010-09-06T05:59:15Z-
dc.date.available2010-09-06T05:59:15Z-
dc.date.issued2003en_HK
dc.identifier.citationProstate, 2003, v. 56 n. 2, p. 81-97en_HK
dc.identifier.issn0270-4137en_HK
dc.identifier.urihttp://hdl.handle.net/10722/67896-
dc.description.abstractBACKGROUND. Prostatic secretory protein of 94 amino acids (PSP94), probasin, and seminal vesicle secretion II (SVSII) are the three major proteins secreted by the lateral lobe of the rat prostate gland. Among these proteins, rodent PSP94 but not probasin and SVSII has a human homologue and it is also a major secretory protein of the human prostate, in addition to prostatic acid phosphatase and prostate-specific antigen. METHODS. In this study, we examined and compared the mRNA expression of these three secretory markers in three rat models of prostate cancer including the sex steroid-induced dysplasia (prostatic intraepithelial neoplasia or PIN) in Noble (Nb) rat model, an androgen-independent Nb rat prostatic tumor (AIT) and Dunning rat prostatic adenocarcinomas (both androgen-dependent and -independent) by in situ hybridization (ISH), reverse transcriptase-polymerase chain reaction (RT-PCR), and immunohistochemistry. RESULTS. The transcripts for the three markers were highly expressed in the secretory epithelium of normal lateral prostate (LP). Their hybridization signals became reduced in the epithelial cells in the low-grade PINs and significantly weakened or lost in the high-grade PINs induced in the LP. Interestingly, we observed that some dysplastic cells located at the basal compartment of the PIN lesions, and nests of outpouching epithelial cells in the vicinity of PINs, expressed positive hybridization signals of three markers. In the adenocarcinoma, signals of probasin but not PSP94 and SVSII were detected. No hybridization signals were detected in both Dunning and AIT tumors. By RT-PCR, transcripts for these proteins were still detected but significantly reduced in the Dunning tumors, whereas in the AIT tumor, only SVSII transcripts were detected. Immunohistochemistry of PSP94 also showed a reduced staining in the PIN lesions, but no immunoreactivity was seen in the rat prostatic tumors. CONCLUSIONS. The mRNA expression of the three prostatic secretory markers were decreased in the hormone-induced PINs and in two rat prostatic tumors, indicating that the androgen-regulated secretory differentiation was impaired during the development of the premalignant lesion and further reduced in advanced tumors. The abnormal expression pattern of these secretory markers and androgen receptor (AR) in the basal compartment of the PIN lesions suggests that there is a population of cell types with secretory phenotype appearing in the basal cell layer during the early malignant transformation of the prostatic epithelium. © 2003 Wiley-Liss, Inc.en_HK
dc.languageengen_HK
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www3.interscience.wiley.com/cgi-bin/jhome/34304en_HK
dc.relation.ispartofProstateen_HK
dc.rightsThe Prostate. Copyright © John Wiley & Sons, Inc.en_HK
dc.subject.meshAdenocarcinoma - physiopathologyen_HK
dc.subject.meshAndrogen-Binding Protein - analysis - geneticsen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshDisease Models, Animalen_HK
dc.subject.meshGene Expression Regulation, Neoplasticen_HK
dc.subject.meshImmunohistochemistryen_HK
dc.subject.meshIn Situ Hybridizationen_HK
dc.subject.meshMaleen_HK
dc.subject.meshProstate - chemistry - physiopathology - secretionen_HK
dc.subject.meshProstatic Intraepithelial Neoplasia - chemistry - physiopathologyen_HK
dc.subject.meshProstatic Neoplasms - chemistry - physiopathologyen_HK
dc.subject.meshProstatic Secretory Proteins - analysis - geneticsen_HK
dc.subject.meshRNA, Messenger - analysisen_HK
dc.subject.meshRatsen_HK
dc.subject.meshRats, Inbred Strainsen_HK
dc.subject.meshReverse Transcriptase Polymerase Chain Reactionen_HK
dc.subject.meshSeminal Vesicle Secretory Proteins - analysis - geneticsen_HK
dc.subject.meshTumor Markers, Biologicalen_HK
dc.titleExpression study of three secretory proteins (Prostatic secretory protein of 94 amino acids, probasin, and seminal vesicle secretion II) in dysplastic and neoplastic rat prostatesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0270-4137&volume=56&spage=81&epage=97&date=2003&atitle=Expression+study+of+three+secretory+proteins+(prostatic+secretory+protein+of+94+amino+acids,+probasin,+and+seminal+vesicle+secretion+II)+in+dysplastic+and+neoplastic+rat+prostatesen_HK
dc.identifier.emailWong, YC:ycwong@hkucc.hku.hken_HK
dc.identifier.authorityWong, YC=rp00316en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/pros.10228en_HK
dc.identifier.pmid12746832en_HK
dc.identifier.scopuseid_2-s2.0-0042308763en_HK
dc.identifier.hkuros76479en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0042308763&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume56en_HK
dc.identifier.issue2en_HK
dc.identifier.spage81en_HK
dc.identifier.epage97en_HK
dc.identifier.isiWOS:000183733600001-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridKwong, J=7005301973en_HK
dc.identifier.scopusauthoridLui, K=15725661300en_HK
dc.identifier.scopusauthoridChan, PSF=7403497705en_HK
dc.identifier.scopusauthoridHo, SM=7403713823en_HK
dc.identifier.scopusauthoridWong, YC=7403041798en_HK
dc.identifier.scopusauthoridXuan, JW=7004718061en_HK
dc.identifier.scopusauthoridChan, FL=7202586505en_HK
dc.identifier.citeulike3906277-

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