1. Volume 51, Issue 2, Pages 447-456 (February 2007)
Terazosin Modifies the Content of Glycosaminoglycans and the Activity of Matrix Metalloproteinase 2 in the Rat Ventral Prostate 
Dionisios Mitropoulos, Eleni Papakonstantinou, Alexios J. Aletras, Nikolaos Kalinderis, Anastasios Zervas, Dimitrios Hatzichristou, George Karakiulakis 
European Urology 
Volume 51, Issue 2, Pages (February 2007)
DOI: /j.eururo
Copyright © 2006 European Association of Urology Terms and Conditions

2. Fig. 1
Terazosin decreases the content of chondroitin sulphate and increases the content of dermatan sulphate in the ventral lobe of the rat prostate. (A) Total glycosaminoglycans (GAGs; 2μl, containing 4μg uronic acids) isolated from prostate tissue homogenates as described in “Materials and methods, were subjected to electrophoresis on cellulose acetate membranes. Arrows indicate mobility of glycan populations from untreated (control; npG) or terazosin-treated animals (tpG; 1.2mg/kg body weight, every second day for 120 d). (B) Quantification of the intensity of the Alcian blue staining using a computer-assisted image analysis program. Each bar represents the mean±SD from 8–10 animals. Statistical significance: *p<0.05; ***p<0.01, as compared to controls, the GAG content of which was regarded as 100%. HA=hyaluronic acid, DS=dermatan sulphate, HS=heparan sulphate, CS=chondroitin sulphate.
European Urology  , DOI: ( /j.eururo )
Copyright © 2006 European Association of Urology Terms and Conditions

3. Fig. 2
Estimation of molecular mass of glycosaminoglycans from the ventral lobe of the rat prostate. Total glycosaminoglycans (GAGs; 2μl, containing 10μg uronic acids) isolated from prostate tissue homogenates as described in “Materials and methods,” were subjected to polyacrylamide gel electrophoresis. Lanes 1 and 3, untreated; lanes 2 and 4, terazosin treated (1.2mg/kg body weight, every second day for 120 d). Arrows on the left indicate molecular weight markers: HA=hyaluronic acid 225kD, CS=chondroitin sulphate C 57kD, DS=dermatan sulphate 29kD, and H=heparin 11kD. Arrows on the right indicate mobility of prostate glycan populations: pG1, pG2, pG3, and pG4 (and their corresponding glycan populations following electrophoresis on cellulose acetate membranes).
European Urology  , DOI: ( /j.eururo )
Copyright © 2006 European Association of Urology Terms and Conditions

4. Fig. 3
Terazosin increases gelatinase activity in the ventral lobe of the rat prostate. (A) Representative gelatin zymography in aliquots of the 25–50% (NH4)2SO4 cut of prostate tissue homogenates (5μg protein) from rats treated with terazosin. Lane 3, normal prostate; lane 4, terazosin, 0.12mg/kg; lanes 5 and 6, terazosin, 1.2mg/kg; lane 7, normal prostate in the presence of Na2EDTA (20mM); lane 8, normal prostate in the presence of N-ethyl-maleimide (5mM); lane 9, normal prostate; lane 6: normal prostate incubated in the presence of APMA at 37°C for 24h and subjected to gelatin zymography. Arrows on the left and lane 1, prestained standard protein molecular weight markers: phosphorylase b (97.4kD), bovine serum albumin (66.2kD), l-glutamic dehydrogenase (55.0kD), ovalbumin (42.7kD), and aldolase (40.0kD); all were from Promega (Madison, WI). Arrows on the right and lane 2, migration of purified pro-matrix metalloproteinase (proMMP-9; 92kD) and proMMP-2 (72kD), and active MMP-2 (64kD) (Anawa Trading, Wangen). (B) Quantitative analysis of gelatinolytic activity rat prostate tissue using a computer-supported image analysis program. Each bar represents the mean±SD from 7–10 animals. Statistical significance: *p<0.05; **p<0.02; ***p<0.01. Parentheses indicate as compared to untreated animals (controls), which were regarded as 100% gelatinolytic activity. Brackets indicate as compared to lower dose.
European Urology  , DOI: ( /j.eururo )
Copyright © 2006 European Association of Urology Terms and Conditions

5. Fig. 4
Tissue inhibitor of matrix metalloproteinase 1 and 2 are expressed in prostate homogenates and are not influenced by terazosin treatment. Tissue inhibitors of matrix metalloproteinase (TIMP-1 and -2) were measured by enzyme-linked immunosorbent assay in aliquots of prostate homogenates (2μg protein) after oral treatment with terazosin (0.12, 1.2mg/kg, every second day for 120 d). Each bar represents the mean±SD of triplicate determinations from 8–10 animals.
European Urology  , DOI: ( /j.eururo )
Copyright © 2006 European Association of Urology Terms and Conditions

6. Fig. 5
Terazosin does not have a direct influence on pro-matrix metalloproteinase 2. Representative gelatin zymography of the effect of terazosin on purified pro-matrix metalloproteinase 2 (proMMP-2) isolated from pulmonary fibroblasts homogenates (2μg protein). Lane 3, proMMP-2 from pulmonary fibroblast; lane 4, plus terazosin 10−8M; lane 5, plus terazosin 10−7M; lane 6, plus terazosin 10−6M. Arrows on the left and lane 1, prestained standard protein molecular weight markers: phosphorylase b (97.4kD), bovine serum albumin (66.2kD), l-glutamic dehydrogenase (55.0kD), and ovalbumin (42.7kD). Arrows on the right and lane 2, migration of purified proMMP-9 (92kDa), and proMMP-2 (72kD), and active MMP-2 (64kD).
European Urology  , DOI: ( /j.eururo )
Copyright © 2006 European Association of Urology Terms and Conditions