Tissue-Specific Expression and Androgen Regulation of Different Genes Encoding Rat Prostatic 22-Kilodalton Glycoproteins Homologous to Human and Rat Cystatin

Winderickx, Joris; Hemschoote, K; Clercq, Norbert De; Dijck, Patrick Van; Peeters, Benjamin; Rombauts, Wilfried; Verhoeven, Guido; Heyns, Walter

doi:10.1210/mend-4-4-657

Cited by 59 publications

(29 citation statements)

References 29 publications

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“…Androgens have been reported to stimulate the expression of several regulatory proteins, including the prostatic binding protein also called prostatein (Vercaeren et al 1992), cystatin-related protein (Winderickx et al 1990) and proliferating cell nuclear antigen (Perry & Tindall 1996). Androgens also induce stimulation of neutral lipid synthesis, including triglyceride and cholesterol esters in the prostate gland (Swinnen et al 1990).…”

Section: Introductionmentioning

confidence: 99%

Regulation of the gap junction connexin 43 gene by androgens in the prostate

Huynh

Alpert²,

Laird³

et al. 2001

Journal of Molecular Endocrinology

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Androgens play an important role in prostate gland development and function, and have been implicated in prostate carcinogenesis. We report the regulation of the gap junctional intercellular communication gene connexin 43 (Cx43) by androgens in the prostate gland. In rat ventral prostate tissue, only trace levels of Cx43 mRNA were detected. Castration, however, resulted in a high increase in Cx43 mRNA and protein. Cx32 was unchanged. Castration-induced Cx43 mRNA and protein were abolished by administration of dihydrotestosterone (DHT). Following castration, prostate weights were approximately 16% of shamtreated controls. However, DHT replacement resulted in prostate weights which were not different from sham-treated controls. Under similar castration conditions, Cx43 induction coincided with pronounced apoptosis in the prostate gland cells, and DHT prevented the induction of apoptosis. Given the physiological role of gap junctions and androgens in the regulation of prostate tissue homeostasis, our observations are relevant to the understanding of androgendependent prostate carcinogenesis.

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Section: Introductionmentioning

confidence: 99%

Regulation of the gap junction connexin 43 gene by androgens in the prostate

Huynh

Alpert²,

Laird³

et al. 2001

Journal of Molecular Endocrinology

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“…These proteins include fetuin [17], cystatin-related proteins [18] and, most recently, testatin [19]. The identification of these proteins has led to the premise that new cystatin families or subgroups of families exist that have evolved to perform tissue-specific functions distinct from the housekeeping-type functions of the classic cystatin proteins.…”

Section: Introductionmentioning

confidence: 99%

Structure, alternative splicing and chromosomal localization of the cystatin-related epididymal spermatogenic gene

Hsia

Sutton

1999

Biochemical Journal

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The cystatin superfamily of cysteine protease inhibitors consists of three major families, including the stefins, cystatins and kininogens. However, the recent identification of several genes that possess sequence similarity with the cystatins but have different gene or protein structures indicates that several new cystatin families or subgroups of families might exist. We previously identified the cystatin-related epididymal spermatogenic (Cres) gene, which is related to the family 2 cystatins but exhibits highly tissue-specific expression in the reproductive tract. In the studies presented here, an analysis of gene structure as well as chromosomal mapping studies suggest that the Cres gene might represent a new subgroup within the family 2 cystatins. Although the Cres gene possesses an additional exon encoding 5ʹ untranslated sequences, its coding exons are similar in size to the three coding exons of the cystatin family 2 genes, and the Cres exon/intron splice junctions occur in identical locations as in the cystatin C gene. Furthermore, chromosomal mapping studies show that the Cres gene co-segregates with the cystatin C gene on mouse chromosome 2. Similar to the cystatin family 2 proteins, the Cres protein possesses the type A and B disulphide loops that are necessary for cystatin folding. Interestingly, Cres protein also possesses half of a type C disulphide loop. Although probably related to the cystatin genes, the Cres gene is distinct in that its promoter contains consensus motifs typical of regulated genes. Finally, reverse transcriptase-mediated PCR studies and the identification of new Cres cDNA clones indicate that the Cres mRNA is alternatively spliced, resulting in two Cres

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“…CRP, originally described as androgen-regulated 20-or 22-kDa glycoprotein (60,61), has been called CRP because of its marked sequence homology to cystatin (62,63). The function of CRP is still unknown, and no protease inhibitory activity has yet been demonstrated.…”

Section: Discussionmentioning

confidence: 99%

Molecular Targets for Diabetes Mellitus-associated Erectile Dysfunction

Yohannes

Chang

Tar

et al. 2010

Molecular & Cellular Proteomics

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Protein expression profiles in rat corporal smooth muscle tissue were compared between animal models of streptozotocin-induced diabetes mellitus (STZ-DM) and agematched controls (AMCs) at 1 week and 2 months after induction of hyperglycemia with STZ treatment. At each time point, protein samples from four STZ-DM and four AMC rat corpora tissues were prepared independently and analyzed together across multiple quantitative twodimensional gels using a pooled internal standard sample to quantify expression changes with statistical confidence. A total of 170 spots were differential expressed among the four experimental groups. A subsequent mass spectrometry analysis of the 170 spots identified a total of 57 unique proteins. Network analysis of these proteins using MetaCore TM suggested altered activity of transcriptional factors that are of too low abundance to be detected by the two-dimensional gel method. The proteins that were down-regulated with diabetes include isoforms of collagen that are precursors to fibril-forming collagen type 1; Hsp47, which assists and mediates the proper folding of procollagen; and several proteins whose abundance is controlled by sex hormones (e.g. CRP1 and A2U). On the other hand, proteins seen or predicted to be up-regulated include proteins involved in cell apoptosis (e.g. p53, 14-3-3-␥, Serpinf1, Cct4, Cct5, and Sepina3n), proteins that neutralize the biological activity of nerve growth factor (e.g. anti-NGF 30), and proteins involved in lipid metabolism (e.g. apoA-I and apoA-IV). Subsequent Western blot validation analysis of p53, 14-3-3-␥, and Hsp47 confirmed increased p53 and 14-3-3-␥ and decreased Hsp47 levels in separate samples. According to the results from the Western blot analysis, Hsp47 protein showed a ϳ3-fold decrease at 1 week and was virtually undetectable at 2 months in diabetic versus control. Taken together, our results identify novel candidate proteins playing a role in erectile dysfunction in diabetes resulting from STZ treatment. Molecular & Cellular Proteomics 9:565-578, 2010. Erectile dysfunction (ED)1 is one of the many complications caused by diabetes mellitus. About 52% of men between the age of 40 and 70 years suffer from ED due to various causes, such as pathophysiological changes in nerves, blood vesicles, corporal smooth muscle tissue, and endothelial cells as well as psychological problems (such as stress) (1-3). As most of these risk factors for development of ED are inherent to diabetes mellitus, men with diabetes have a greater prevalence of ED and early onset of the disease compared with men without diabetes (4 -6). The current estimates suggest that as many as 75% of men with diabetes will develop some degree of ED at an earlier age (7). In addition, men with diabetes present with more severe dysfunction and are less responsive to current pharmacological therapies for ED (8 -10). Although ED is considered a disease impacting the "quality of life" of patients, it is often associated with depression, low self-esteem, and lower overall quality of ma...

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Tissue-Specific Expression and Androgen Regulation of Different Genes Encoding Rat Prostatic 22-Kilodalton Glycoproteins Homologous to Human and Rat Cystatin

Cited by 59 publications

References 29 publications

Regulation of the gap junction connexin 43 gene by androgens in the prostate

Regulation of the gap junction connexin 43 gene by androgens in the prostate

Structure, alternative splicing and chromosomal localization of the cystatin-related epididymal spermatogenic gene

Molecular Targets for Diabetes Mellitus-associated Erectile Dysfunction

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