Sperm-specific expression of angiotensin-converting enzyme (ACE) is mediated by a 91-base-pair promoter containing a CRE-like element.

Howard, Tom E.; Balogh, R; Overbeek, Paul A.; Bernstein, Kenneth E.

doi:10.1128/mcb.13.1.18

Cited by 110 publications

(72 citation statements)

References 43 publications

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“…The template DNA for in vitro transcription was a linear fragment containing the mouse testis ACE promoter from -91 to -9 followed by a 380-bp G-free cassette. Each reaction contained 50 ,ug rat testis nuclear extract, 300 ng testis ACE template, 200 ng pADML(190) as an internal control, and 300 ng doublestranded poly(dI-dC) in a total volume of 20 gl (11,12). In the indicated experiments, 1-5 pkg of anti-CREM antibody (Santa Cruz Biotechnology) or rabbit IgG (Sigma) was preincubated with the rat testis nuclear extract for 1 hr on ice before the addition of templates.…”

Section: Methodsmentioning

confidence: 99%

“…Whole testis nuclear extracts were prepared from adult Sprague Dawley rats as described (11). The oligonucleotides used to generate a double-stranded fragment containing the testis ACE-55 element were: ACE.327 5'-ACATTGCTCTATGAGGTCACACTGCAG-GCTTG-3' and ACE.328 5'-CAAGCCTGCAGTGTGAC-CTCATAGAGCAAT-3'.…”

Section: Methodsmentioning

confidence: 99%

“…Previous studies have identified a germ cell-specific testis ACE promoter located within the 12th intron of the somatic ACE gene; as few as 91 bp of this promoter can target the expression of a reporter gene to round and elongating spermatids in transgenic mice (10,11). In vitro analyses of the testis ACE promoter have identified two important transcriptional motifs within the 91-bp promoter (12).…”

mentioning

confidence: 99%

“…There are two isozymes of ACE in mammals (2). Somatic ACE is produced by endothelium and other somatic tissues and is responsible for the conversion of angiotensin I into the potent vasoconstrictor angiotensin 11 (3). A second isozyme, testis ACE, is a tissue-specific gene product made only by round and elongating spermatids (4).…”

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confidence: 99%

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cAMP-response element modulator tau is a positive regulator of testis angiotensin converting enzyme transcription.

Zhou

Sun²,

Means³

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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Testis angiotensin-converting enzyme (ACE) is a unique form of ACE, only produced by male germ cells, and results from a testis-specific promoter found within the ACE gene. We have investigated the role of cAMP-response element modulator (CREM)T in testis ACE transcription. In gel shift experiments, testes nuclear proteins retard an oligonucleotide containing the cAMP-response element (CRE) found at position -55 in the testis ACE promoter. Anti-CREM antibody supershifts this complex. Competitive gel shift shows that recombinant CREMT protein and testes nuclear proteins have a similar specificity of binding to the testis ACE CRE. Functional analysis using in vitro transcription and transfection studies also demonstrate that CREMT protein is a transcriptional activator of the testis ACE promoter. Western blot analysis identifies CREMT protein in the protein-DNA complex formed between nuclear proteins and the testis ACE CRE motif. This analysis also identified other CREM isoforms in the gel-shifted complex, which are thought to be CREMT1/2, CREMci/j3, and S-CREM. These data indicate that CREMT isoforms play an important role as a positive regulator in the tissue-specific expression of testis ACE.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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cAMP-response element modulator tau is a positive regulator of testis angiotensin converting enzyme transcription.

Zhou

Sun²,

Means³

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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“…This site has been located from Ϫ55 to Ϫ48 relative to the transcriptional start site and has been shown to be a binding site for CREM (17). A small portion of the angiotensin-converting enzyme promoter from Ϫ91 to ϩ17 can efficiently target a reporter construct to step 4 -14 spermatids (38,39).…”

Section: Figmentioning

confidence: 99%

Germ Cell Nuclear Factor Relieves cAMP-response Element Modulator τ-mediated Activation of the Testis-specific Promoter of Human Mitochondrial Glycerol-3-phosphate Dehydrogenase

Rajković¹,

Middendorff

Wetzel³

et al. 2004

Journal of Biological Chemistry

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Mitochondrial glycerol-3-phosphate dehydrogenase (mGPDH) is an essential component of the glycerol phosphate shuttle that transfers reduction equivalents from the cytosol into the mitochondrion. Within the testis, immunohistological analysis localized human mG-PDH to late spermatids and to the midpiece of spermatozoa. The expression of human mGPDH is regulated by two somatic promoters, and here, we describe a third testis-specific promoter of human mGPDH. The usage of this testis-specific promoter correlates with the expression of a shortened mGPDH transcript of ϳ2.4 kb in length, which is solely detectable from testicular RNA. Within the testis-specific promoter, we detected a cAMPresponse element (CRE) site at ؊51, which binds the testis-specific transcriptional activator CRE modulator (CREM ) in electrophoretic mobility shift assays. This recognition site overlaps with a nuclear receptor binding half-site at ؊49, which binds the testis-specific transcriptional repressor germ cell nuclear factor (GCNF). Both factors compete for binding to the same DNA response element. Ectopic expression of CREM in HepG2 cells activated a promoter-driven luciferase construct in transient transfection experiments. Additional cotransfection of GCNF relieved this activity, suggesting a down-regulation of CREM -mediated activation by GCNF. This effect was preserved by introducing the CRE/nuclear receptor-binding element into a heterologous promoter context. Our data suggest a down-regulation of CREM -mediated gene expression by GCNF, which might be a general regulation mechanism for several postmeiotically expressed genes with a temporal expression peak during early spermatid development.Mitochondrial glycerol-3-phosphate dehydrogenase (mG-PDH) 1 is an essential component of the glycerol phosphate shuttle. In conjunction with the cytosolic glycerol-3-phosphate dehydrogenase, this shuttle uses the interconversion of glycerol-3-phosphate to dihydroxyacetone phosphate to oxidize cytosolic NADH by transferring reduction equivalents from the cytosol to the mitochondrion (1, 2). The expression of human and rat mGPDH is regulated by two somatic promoters in a tissue-specific manner (3-7), but rat mGPDH is additionally regulated by a third testis-specific promoter (8). The usage of the testis-specific promoter of mGPDH results in a shortened transcript length of ϳ2.4 kb containing an alternate first exon at its 5Ј end and a shortened 3Ј-untranslated region; however, the open reading frame remains unaffected (3,8). In rat testis, mGPDH transcripts have been detected in postmeiotic germ cells during early spermatid development, whereas mGPDH proteins have been detected during late spermatid development (8). The knockout of mGPDH in transgenic mice leads to reduced fertility (9, 10).Within the testis, spermatogenesis is a complex developmental process that includes the mitotic proliferation of spermatogonial stem cells, meiotic prophase, division of spermatocytes, and morphological changes of haploid spermatids to highly specialized spermato...

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Tissue-specific protein-DNA interactions of the mouse protamine 2 gene promoter

Wijnen

Hecht

1997

J. Cell. Biochem.

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During spermiogenesis, the haploid phase of spermatogenesis, the genome is packaged into a highly compacted form and this process requires replacement of histones by protamines. In the mouse, protamines are encoded by two genes, which are transcriptionally regulated in testis. To understand the regulation of transcription of the mouse protamine 2 (mP2) gene, the tissue-distribution of sequence-specific interactions between nuclear proteins and promoter DNA sequences have been analyzed. Protein binding to the promoter region from -370 to +65 was studied using DNase I footprinting and gel shift assays. Five protein binding sites were identified, which are recognized by nuclear proteins from either testis or liver. Site 1 from -64 to -48, contains part of a cAMP responsive element (CRE), which in testis is recognized by CREM tau, an activator of post-meiotic transcription. Testicular protein(s) also binds to three other promoter domains: site 2, -87 to -67, a region containing a CAAT box, and sites 4 and 5, -239 to -210 and -328 to -311, sequences with similarity to consensus steroid hormone responsive elements (HRE). In contrast, interactions between the mP2 promoter and nuclear factors from liver, a tissue in which the mP2 gene is not transcribed, are observed at sites 1, 2, and 4, as well as at an additional region at site 3, -202 to -175. Because occupancy at site 3 appears to correlate with inactivation of the gene in non-testicular tissues, whereas testicular protein binding at site 5 appears to be associated with active transcription, we conclude that the mP2 promoter displays intricate tissue-specific patterns of protein/DNA interactions at key regulatory elements.

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Sperm-specific expression of angiotensin-converting enzyme (ACE) is mediated by a 91-base-pair promoter containing a CRE-like element.

Cited by 110 publications

References 43 publications

cAMP-response element modulator tau is a positive regulator of testis angiotensin converting enzyme transcription.

cAMP-response element modulator tau is a positive regulator of testis angiotensin converting enzyme transcription.

Germ Cell Nuclear Factor Relieves cAMP-response Element Modulator τ-mediated Activation of the Testis-specific Promoter of Human Mitochondrial Glycerol-3-phosphate Dehydrogenase

Tissue-specific protein-DNA interactions of the mouse protamine 2 gene promoter

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