Identification of a specifically expressed modified form of novel PSP‐94 protein in the secretion of benign prostatic hyperplasia

Xu, Kexin; Wang, Xianghong; Ling, Ming-Tat; Lee, Davy T. W.; Fan, Tianyong; Chan, Franky L.; Xuan, James J. W.; Tsao, Sai‐Wah; Wong, Yi‐Lee

doi:10.1002/elps.200390167

Cited by 4 publications

(7 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…7 Also, PSP61, a modified isoform of human MSP consisting of the N-terminal 61 residues, was discovered in patients with benign prostatic hyperplasia (BPH) and suggested as a specific biological marker for the diagnosis of BPH. 8 These findings demonstrate the importance of MSP in clinical diagnosis in prostate pathophysiology. However, in general, the biological functions of MSPs are still poorly understood.…”

mentioning

confidence: 93%

Novel Solution Structure of Porcine β-Microseminoprotein

Wang

Lou

et al. 2005

Journal of Molecular Biology

View full text Add to dashboard Cite

mentioning

confidence: 93%

Novel Solution Structure of Porcine β-Microseminoprotein

Wang

Lou

et al. 2005

Journal of Molecular Biology

View full text Add to dashboard Cite

“…Changes in splice site selection have been frequently observed in cancer (e.g., MDM2, Bin1, and FGFR-2 genes in breast, skin, and prostate cancers; refs. [7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Splicing Factor Tra2-β1 Is Specifically Induced in Breast Cancer and Regulates Alternative Splicing of theCD44Gene

et al. 2006

View full text Add to dashboard Cite

The human CD44 gene undergoes extensive alternative splicing of multiple variable exons positioned in a cassette in the middle of the gene. Expression of alternative exons is often restricted to certain tissues and could be associated with tumor progression and metastasis of several human malignancies, including breast cancer. Exon v4 contains multiple copies of a C/A-rich exon enhancer sequence required for optimal inclusion of the exon and binding to the nucleic acid-binding proteins YB-1 and human Tra2-B1. Here, we show that hTra2-B1, a member of the extended family of serine/arginine-rich (SR) splicing factors, enhances the in vivo inclusion of CD44 exons v4 and v5. It increased inclusion of exons v4 and v5 and acted synergistically with YB-1. Activation required the C/A-rich enhancer within exon v4. Several other SR proteins had none or only a slight effect on CD44 exon inclusion. In contrast, SC35 inhibited exon usage and antagonized the effects of Tra2 or YB-1. In a matched pair analysis of human breast cancers and their corresponding nonpathologic tissue controls, we found a significant induction of Tra2-B1 in invasive breast cancer, both on the RNA and protein levels. Together with our functional data, these results suggest an important role for Tra2-B1 in breast cancer. Induction of this splicing factor might be responsible for splicing of CD44 isoforms associated with tumor progression and metastasis. (Cancer Res 2006; 66(9): 4774-80)

show abstract

“…One of them was recently identified as as1-Casein (one of the proteins presented in Spot 3). 14 In this study, to confirm the twodimensional results and further study the significance of as1-Casein expression in BPH patients, we first performed Western blotting to study the as1-Casein protein expression in EPS derived from BPH patients and BPHfree controls. As shown in Figure 1, specific as1-Casein bands with molecular weights of 45 and 10 kDa were detected in BPH-EPS whereas no corresponding bands were found in the BPH-free controls when same amount of protein was analyzed.…”

Section: Resultsmentioning

confidence: 77%

“…12,13 Recently, using two-dimensional gel electrophoresis, we identified a group of prostatic secretory proteins specifically present in human expressed prostatic secretion (EPS) from BPH patients. 14 Subsequent analysis showed that one of the proteins is as1-Casein, a protein that is usually produced by mammary epithelial cells. 14 The aim of this study was to investigate the possible usefulness of as1-Casein in the differential diagnosis between BPH and prostate cancer, and its possibility as a specific marker for BPH.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Evidence of a novel biomarker, αs1-Casein, a milk protein, in benign prostate hyperplasia

Wang

et al. 2006

Prostate Cancer Prostatic Dis

View full text Add to dashboard Cite

Benign prostate hyperplasia (BPH) is a common disease in elderly men. Although it is a nonmalignant disease, it has a significant detrimental impact on the quality of life in patients with latestage disease. Owing to the lack of specific markers, diagnosis of early-stage BPH has been proven unsuccessful. Recently, using two-dimensional electrophoresis, we identified a group of prostatic secretory proteins that are specifically produced by BPH cells (Xu et al., Electrophoresis 2003; 24: 1311). In this study, we investigated the potential diagnostic value of one of the secretory proteins, as1-Casein, in BPH by inmmunohistological staining of normal, BPH and prostate cancer tissues. We found that 90% (20 out of 22) of BPH tissues showed moderate to strong as1-Casein protein expression whereas none of the normal tissues (0 out of 10) and less than 10% of the prostate cancer tissues (3 out of 30) showed similar staining intensity. Our results suggest that as1-Casein may be a potential biomarker for early identification of BPH patients.

show abstract

Identification of a specifically expressed modified form of novel PSP‐94 protein in the secretion of benign prostatic hyperplasia

Cited by 4 publications

References 25 publications

Novel Solution Structure of Porcine β-Microseminoprotein

Novel Solution Structure of Porcine β-Microseminoprotein

Splicing Factor Tra2-β1 Is Specifically Induced in Breast Cancer and Regulates Alternative Splicing of theCD44Gene

Evidence of a novel biomarker, αs1-Casein, a milk protein, in benign prostate hyperplasia

Contact Info

Product

Resources

About