Reverse Zymography Studies of Protease Inhibitors in the Secretions of Different Lobes of Rat Prostate

Wilson, Michael J.; Casey, Carol A.; Woodson, Mildred; Sinha, Akhouri A.

doi:10.1080/014850199262959

Cited by 3 publications

(3 citation statements)

References 28 publications

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“…The rat's main different semen components present a nearly lobe-specific production, with prostatin and serine proteases by VP, zinc by LP, spermine by DP, and fructose by AP (Gerhardt et al, 1983;Wilson et al, 1993a;Sorensen et al, 1997). MMPs and serine protease inhibitors are also secreted in a lobe-specific manner (Wilson et al, 1992(Wilson et al, , 1993b(Wilson et al, , 1999. Here, we use immunocytochemistry to investigate whether TIMP-2 is produced by rat prostate epithelial cells and if expression may have a lobespecific pattern.…”

Section: Introductionmentioning

confidence: 99%

Tissue inhibitor of metalloproteinase‐2 (TIMP‐2) location in the ventral, lateral, dorsal and anterior lobes of rat prostate by immunohistochemistry

Delella

Justulin

Felisbino

2007

Cell Biology International

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Matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) play a major role in extracellular matrix component degradation in several normal and abnormal tissue situations; they are also found in human seminal plasma. MMPs have been found in rat prostate secretions and are nearly lobe specific in expression pattern. The aim of this study was to evaluate whether TIMP-2, like other semen components, is expressed differently from different rat prostatic lobes. Immunohistochemical staining was performed in both young and adult rat ventral (VP), lateral (LP), dorsal (DP), and anterior (AP) prostatic lobes and confirmed by western blotting. TIMP-2 expression was found in the epithelial cells in the following sequence: LP>AP>DP>VP, in both young and adult rats. In this study, 100% of adult LP presented histological signs of prostatitis, where TIMP-2 immunostaining was positive in normal epithelium even with intraluminal neutrophils, but was reduced or absent in the epithelium with intraepithelial leukocytes or with periductal stroma disorganization associated with mononuclear cell infiltration. However, TIMP-2 expression in LP was not induced by prostatitis, since younger rat LPs were also strongly TIMP-2 positive. The distal and intermediate VP regions were TIMP-2 negative, but the proximal regions were strongly stained. Western blotting results confirmed the high TIMP-2 expression in the LP lobe. Thus, TIMP-2 is expressed differently between the prostatic lobes and is another nearly lobe-specific protein, which plays a role in the regulation of MMP activity in seminal plasma and glandular homeostasis. TIMP-2 is also another regional ductal variation of VP. Further studies should address whether TIMP-2 expression is related to the highest incidence of rat LP prostatitis and adenocarcinoma.

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Section: Introductionmentioning

confidence: 99%

Tissue inhibitor of metalloproteinase‐2 (TIMP‐2) location in the ventral, lateral, dorsal and anterior lobes of rat prostate by immunohistochemistry

Delella

Justulin

Felisbino

2007

Cell Biology International

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“…There are also clear-cut differences in the level of expression of non-gastric H + /K + -ATPase-· and endothelin receptor density (17,18), and in the secretion of prostate secretory protein (PSP94) and protease inhibitors (19,20). Moreover, angiographic studies demonstrated that the prostate ventral lobe is better irrigated than the dorsal one (21).…”

Section: Introductionmentioning

confidence: 97%

Real-time PCR analysis of leptin and leptin receptor expression in the rat prostate, and effects of leptin on prostatic acid phosphatase release

Malendowicz¹,

Ruciński²,

Belloni³

et al. 2006

Int J Mol Med

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Abstract.We have recently demonstrated the expression of leptin and leptin receptor (Ob-R) isoforms a, b, c, e and f in the rat seminal vesicles and prostate. The aim of the present study was to provide a semiquantitative real-time PCR estimation of leptin/Ob-R isoform mRNA expression in the seminal vesicles and individual components of rat prostate, and to ascertain the in vitro effects of leptin on prostate acid phosphatase release. The highest expression of the leptin and Ob-R genes was in the seminal vesicles and lateral prostate lobe, respectively. Of the various isoforms, Ob-Rb displayed the highest and Ob-Re the lowest expression. Leptin (10 -8 and 10 -6 M) enhanced acid phosphate release from seminal vesicles, and (10 -6 M) decreased it from the coagulating lobe. Taken together, our findings support the contention that leptin may be involved in the autocrine-paracrine functional regulation of rat seminal vesicles and prostate. The physiological relevance of the marked heterogeneity of the different prostate lobes in both their leptin/Ob-R expression and functional response to leptin remains to be addressed.

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“…Here, we note that proMMP is unable to cleave peptide chains, which implies that proMMP cannot be a marker for cancer diagnosis due to its incapability of ECM degradation. To overcome the limitation of these bioassays based on antibody, the bioassays using zymography 9 , 16 , 17 or fluorogenic nanosensor 18 - 20 have been employed to sense only MMP by detecting the cleavage (i.e. proteolysis) of peptide chains due to MMP.…”

Section: Introductionmentioning

confidence: 99%

Blood Droplet-Based Cancer Diagnosis via Proteolytic Activity Measurement in Cancer Progression

Choi¹,

Lee²,

Lee³

et al. 2017

Theranostics

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Matrix metalloproteinase (MMP) is a key marker and target molecule for cancer diagnosis, as MMP is able to cleave peptide chains resulting in degradation of extracellular matrix (ECM), a necessary step for cancer development. In particular, MMP2 has recently been recognized as an important biomarker for lung cancer. Despite the important role of detecting MMP molecules in cancer diagnosis, it is a daunting task to quantitatively understand a correlation between the status of cancer development and the secretion level of MMP in a blood droplet. Here, we demonstrate a nanoscale cancer diagnosis by nanomechanical quantitation of MMP2 molecules under cancer progression with using a blood droplet of lung cancer patients. Specifically, we measured the frequency dynamics of nanomechanical biosensor functionalized with peptide chains mimicking ECM in response to MMP2 secreted from tumors in lung with different metastasis level. It is shown that the frequency shift of the biosensor, which exhibits the detection sensitivity below 1 nM, enables the quantitation of the secretion level of MMP2 molecules during the progression of cancer cells or tumor growth. More importantly, using a blood droplet of lung cancer patients, nanomechanical biosensor is shown to be capable of depicting the correlation between the secretion level of MMP2 molecules and the level of cancer metastasis, which highlights the cantilever-based MMP2 detection for diagnosis of lung cancer. Our finding will broaden the understanding of cancer development activated by MMP and allow for a fast and point-of-care cancer diagnostics.

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Reverse Zymography Studies of Protease Inhibitors in the Secretions of Different Lobes of Rat Prostate

Cited by 3 publications

References 28 publications

Tissue inhibitor of metalloproteinase‐2 (TIMP‐2) location in the ventral, lateral, dorsal and anterior lobes of rat prostate by immunohistochemistry

Tissue inhibitor of metalloproteinase‐2 (TIMP‐2) location in the ventral, lateral, dorsal and anterior lobes of rat prostate by immunohistochemistry

Real-time PCR analysis of leptin and leptin receptor expression in the rat prostate, and effects of leptin on prostatic acid phosphatase release

Blood Droplet-Based Cancer Diagnosis via Proteolytic Activity Measurement in Cancer Progression

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