Proteomic analysis of patient tissue reveals PSA protein in the stroma of benign prostatic hyperplasia. Issue 8 (7th April 2014)
- Record Type:
- Journal Article
- Title:
- Proteomic analysis of patient tissue reveals PSA protein in the stroma of benign prostatic hyperplasia. Issue 8 (7th April 2014)
- Main Title:
- Proteomic analysis of patient tissue reveals PSA protein in the stroma of benign prostatic hyperplasia
- Authors:
- O'Malley, Katherine J.
Eisermann, Kurtis
Pascal, Laura E.
Parwani, Anil V.
Majima, Tsuyoshi
Graham, Lara
Hrebinko, Katherine
Acquafondata, Marie
Stewart, Nicolas A.
Nelson, Joel B.
Yoshimura, Naoki
Wang, Zhou - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="pros22807-sec-0001" sec-type="section"> <title>BACKGROUND</title> <p>Benign prostatic hyperplasia (BPH) is an age‐related disease frequently associated with lower urinary tract symptoms (LUTS) that involves hyperplasia of both epithelial and stromal cells. Stromal fibrosis is a distinctive feature of BPH, but the exact mechanisms underlying this phenomenon are poorly understood.</p> </sec> <sec id="pros22807-sec-0002" sec-type="section"> <title>METHODS</title> <p>In the current study, proteomics analyses were utilized to identify proteins altered in the BPH stromal compartment from patients with symptomatic BPH. Stromal cells were isolated from histological nodules of BPH by laser capture microdissection (LCM) and subjected to liquid chromatography/mass spectrometry.</p> </sec> <sec id="pros22807-sec-0003" sec-type="section"> <title>RESULTS</title> <p>Proteins identified included several stromal‐specific proteins involved in extracellular matrix (ECM) remodeling, focal adhesion, and cellular junctions. Additionally, the proteomics array identified the presence of luminal epithelial secretory protein PSA. Immunostaining, ELISA, and in situ hybridization analyses of BPH tissues verified the presence of PSA protein but absence of PSA mRNA in the stromal compartment. E‐cadherin was down‐regulated in BPH epithelial cells compared to normal adjacent tissues, suggesting that alteration of<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="pros22807-sec-0001" sec-type="section"> <title>BACKGROUND</title> <p>Benign prostatic hyperplasia (BPH) is an age‐related disease frequently associated with lower urinary tract symptoms (LUTS) that involves hyperplasia of both epithelial and stromal cells. Stromal fibrosis is a distinctive feature of BPH, but the exact mechanisms underlying this phenomenon are poorly understood.</p> </sec> <sec id="pros22807-sec-0002" sec-type="section"> <title>METHODS</title> <p>In the current study, proteomics analyses were utilized to identify proteins altered in the BPH stromal compartment from patients with symptomatic BPH. Stromal cells were isolated from histological nodules of BPH by laser capture microdissection (LCM) and subjected to liquid chromatography/mass spectrometry.</p> </sec> <sec id="pros22807-sec-0003" sec-type="section"> <title>RESULTS</title> <p>Proteins identified included several stromal‐specific proteins involved in extracellular matrix (ECM) remodeling, focal adhesion, and cellular junctions. Additionally, the proteomics array identified the presence of luminal epithelial secretory protein PSA. Immunostaining, ELISA, and in situ hybridization analyses of BPH tissues verified the presence of PSA protein but absence of PSA mRNA in the stromal compartment. E‐cadherin was down‐regulated in BPH epithelial cells compared to normal adjacent tissues, suggesting that alteration of cellular junctions could contribute to the presence of luminal epithelial secreted proteins PSA and KLK2 in the stromal compartment.</p> </sec> <sec id="pros22807-sec-0004" sec-type="section"> <title>CONCLUSIONS</title> <p>The above findings suggest that the presence of secreted proteins PSA and KLK2 from prostate luminal epithelial cells in BPH stroma is a hallmark of BPH nodules, which could in part be due to alterations in cellular junction proteins and/or increased epithelial barrier permeability. Elucidating the cause and consequence of these secreted proteins in the stromal compartment of BPH may lead to new understanding of BPH pathogenesis as well as approaches to prevent and/or treat this common disease. <italic>Prostate 74:892–900, 2014</italic>. © 2014 Wiley Periodicals, Inc.</p> </sec> </abstract> … (more)
- Is Part Of:
- Prostate. Volume 74:Issue 8(2014)
- Journal:
- Prostate
- Issue:
- Volume 74:Issue 8(2014)
- Issue Display:
- Volume 74, Issue 8 (2014)
- Year:
- 2014
- Volume:
- 74
- Issue:
- 8
- Issue Sort Value:
- 2014-0074-0008-0000
- Page Start:
- 892
- Page End:
- 900
- Publication Date:
- 2014-04-07
- Subjects:
- Prostate -- Diseases -- Periodicals
616 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0045 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/pros.22807 ↗
- Languages:
- English
- ISSNs:
- 0270-4137
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6935.194000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 4003.xml