Literature DB >> 7679761

Gelatinolytic and caseinolytic proteinase activities in human prostatic secretions.

M J Wilson1, H Norris, D Kapoor, M Woodson, C Limas, A A Sinha.   

Abstract

Seminal fluid contains a number of proteinase activities, many of which are secreted by the prostate gland. Our objective was to determine proteinase activities in human prostatic secretions which can degrade gelatin and/or casein. Prostatic secretions were collected by prostate massage from men with benign prostatic hyperplasia prior to surgery to relieve obstruction. Significant proteinase activities towards gelatin of about 81, 86, 94, 111, 115 and 163 Kd as well as less active forms of 23, 36, 38, 132, 137, and 148 Kd were detected using protein substrate-polyacrylamide gel zymography. In addition, Ca2+ stimulated activities of approximately 64, 66, 71 and 76 Kd; however, EDTA and EGTA inhibited all activities but the 23, 36 and 38 Kd forms (these were inhibited by benzamidine and epsilon-amino caproic acid). This suggests that the gelatinolytic activities of 64 Kd and greater were metalloproteinases and those of 23, 36, and 38 Kd were serine proteinases. Significant caseinolytic activities of 22, 25, 35, 37, 57, 90, 96, 102 and 116 Kd were found as well as several less active forms and a 12 Kd activity stimulated by Ca2+. Caseinolytic activities of 12, 14, 16, 96, 102, 116, and 126 Kd were inhibited by EDTA and EGTA indicating they are metalloproteinases. The 35, 37, 57 and 58 Kd caseinolytic activities were inhibited by benzamidine, and the 57 and 58 Kd forms by epsilon-aminocaproic acid suggesting they were serine proteinases. There was considerable variability among individuals in the molecular forms of proteinase activity expressed as well as the level of their activity. A significant decrease in the frequency of expression of the 132 Kd gelatinolytic activity was found in secretions from men with atypia or adenocarcinoma, as compared with men with benign prostatic hyperplasia alone. Our results show that human prostatic secretion contains a variety of proteinase activities. The expression of the 132 Kd gelatinolytic activity could prove useful in further evaluation of neoplastic prostatic disease.

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Year:  1993        PMID: 7679761     DOI: 10.1016/s0022-5347(17)36173-6

Source DB:  PubMed          Journal:  J Urol        ISSN: 0022-5347            Impact factor:   7.450


  7 in total

1.  Identification of complexes of gelatinase A and tissue inhibitor of metalloproteinase-2 in human follicular fluid.

Authors:  Ken-Ichi Shimokawa; Masatoki Katayama; Yoshifumi Matsuda; Hidenobu Takahashi; Izumi Hara; Hirohisa Sato
Journal:  Reprod Med Biol       Date:  2003-09-26

2.  Matrix metalloproteinase (MMP)-2 and MMP-9 in seminal plasma.

Authors:  Ioannis Tentes; Byron Asimakopoulos; Efthimia Mourvati; Klaus Diedrich; Safaa Al-Hasani; Nikos Nikolettos
Journal:  J Assist Reprod Genet       Date:  2007-07-07       Impact factor: 3.412

3.  Matrix metalloproteinases (MMPs) in fresh human prostate tumour tissue and organ-cultured prostate tissue: levels of collagenolytic and gelatinolytic MMPs are low, variable and different in fresh tissue versus organ-cultured tissue.

Authors:  J Varani; Y Hattori; M K Dame; T Schmidt; H S Murphy; K J Johnson; K J Wojno
Journal:  Br J Cancer       Date:  2001-04-20       Impact factor: 7.640

4.  Semen levels of matrix metalloproteinase (MMP) and tissue inhibitor of metallorproteinases (TIMP) protein families members in men with high and low sperm DNA fragmentation.

Authors:  Larissa Berloffa Belardin; Mariana Pereira Antoniassi; Mariana Camargo; Paula Intasqui; Renato Fraietta; Ricardo Pimenta Bertolla
Journal:  Sci Rep       Date:  2019-01-29       Impact factor: 4.379

5.  Matrix metallopeptidase expression and modulation by transforming growth factor-β1 in equine endometrosis.

Authors:  Anna Szóstek-Mioduchowska; Mariola Słowińska; Joanna Pacewicz; Dariusz J Skarzynski; Kiyoshi Okuda
Journal:  Sci Rep       Date:  2020-01-24       Impact factor: 4.379

6.  Matrix metalloproteinase 9 expression in primary human prostatic adenocarcinoma and benign prostatic hyperplasia.

Authors:  F C Hamdy; E J Fadlon; D Cottam; J Lawry; W Thurrell; P B Silcocks; J B Anderson; J L Williams; R C Rees
Journal:  Br J Cancer       Date:  1994-01       Impact factor: 7.640

7.  MMP-2 and MMP-9 activities and TIMP-1 and TIMP-2 expression in the prostatic tissue of two ethanol-preferring rat models.

Authors:  Beatriz Aparecida Fioruci-Fontanelli; Luiz Gustavo A Chuffa; Leonardo O Mendes; Patricia Fernanda F Pinheiro; Flávia Karina Delella; Cilmery S Kurokawa; Sérgio Luis Felisbino; Francisco Eduardo Martinez
Journal:  Anal Cell Pathol (Amst)       Date:  2015-07-15       Impact factor: 2.916

  7 in total

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