Urinary prostaglandins E2 correlates to overactive bladder symptoms in patients with benign prostatic hyperplasia / 中华男科学杂志

<p><b>OBJECTIVE</b>To measure the levels of urinary prostaglandins E2 (PGE2) in benign prostatic hyperplasia (BPH) patients with or without overactive bladder (OAB) symptoms and determine whether urinary PGE2 can serve as a biomarker for BPH-related OAB.</p><p><b>METHODS</b>This study included 86 BPH patients and 34 male control subjects without lower urinary tract symptoms. Based on the OAB symptom scores (OABSS), the BPH cases were classified as BPH/OAB (n =49) and BPH/non-OAB (n = 37) to be treated orally with tamsulosin alone and tamsulosin + tolterodine-tartrate, respectively, for 12 weeks. We measured the urinary PGE2 levels of all the subjects by ELISA before and after medication, the total PGE2 level normalized to the concentration of the urinary creatinine (PGE2/Cr). We also obtained the residual urine volume, Qmax, prostate volume, PSA level, IPSS and OABSS of the BPH patients, and compared them among different groups.</p><p><b>RESULTS</b>The baseline PGE2/Cr level was significantly lower in the control than in the BPH/OAB and BPH/non-OAB groups (both P <0.05), and higher in the BPH/OAB than in the BPH/non-OAB patients (P <0.05). After 12 weeks'treatment, the urinary PGE2/Cr level was remarkably decreased with relief of the OAB symptoms in the BPH/OAB patients (P <0.05) , but not in the BPH/non-OAB group (P >0.05). The concentration of PGE2 was not correlated with the IPSS storage score and OABSS of the BPH/OAB patients (P >0.05).</p><p><b>CONCLUSION</b>Patients with BPH/OAB have significantly higher urinary PGE2/Cr levels than those with BPH/non-OAB and normal controls, which tend to decrease with the alleviation of OAB symptoms. Our findings suggest that urinary PGE2 can be a potential biomarker for BPH/OAB.</p>

Cloning and expression of a new rat procarboxypeptidase B gene in Escherichia coli and purification of recombination carboxypeptidase B.

A new coding sequence of the procarboxypeptidase B gene was obtained from SD rat fresh pancreas by RT-PCR and highly expressed in Escherichia coli in inclusion bodies. The folded procarboxypeptidase B was subjected to trypsin enzymatic cleavage to produce active carboxypeptidase B, subsequently, carboxypeptidase B was effectively purified with anion exchange chromatography DEAE-FF and hydrophobic interaction chromatography Octyl FF, as a result, 40 mg carboxypeptidase B per litre cell culture with specific activity 7.42 u/mg was achieved. Further research showed that the obtained recombinant carboxypeptidase B could substitute carboxypeptidase B isolated from pancreas.