Human 25-hydroxyvitamin D-1α-hydroxylase: cloning, mutations, and gene expression
Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene e...
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E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2000 |
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| Umfang: |
6 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Pediatric nephrology - 1987, 14(2000) vom: Juli, Seite 620-625 |
| Übergeordnetes Werk: |
volume:14 ; year:2000 ; month:07 ; pages:620-625 ; extent:6 |
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| 520 | |a Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene encoding this enzyme were cloned from mouse, rat, and human tissue in late 1997. The human gene encoding the 1α-hydroxylase is 5 kb in length, located on chromosome 12, and comprises nine exons and eight introns; its intron/exon organization is very similar to that of the other four mitochondrial P450 enzymes cloned to date. Mutations in P450c1α cause 1α-hydroxylase deficiency, also known as vitamin D- dependent rickets type 1, a rare autosomal recessive disease characterized by rickets and impaired growth due to failure of renal synthesis of 1,25(OH)2D. To date, 31 patients have been studied and 20 distinct mutations in the gene identified, including 13 mis-sense mutations, none of which encode a protein with significant enzyme activity. Recent studies in animals demonstrate that regulation of P450c1α gene expression by parathyroid hormone (PTH), low calcium diet, low phosphorus diet, and 1,25(OH)2D occurs at the level of its mRNA. Transcriptional activity of the mouse and human P450c1α gene promoters can be stimulated by PTH, cAMP, and forskolin and suppressed by 1,25(OH)2D. | ||
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(DE-627)NLEJ205948995 DE-627 ger DE-627 rakwb eng Human 25-hydroxyvitamin D-1α-hydroxylase: cloning, mutations, and gene expression 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene encoding this enzyme were cloned from mouse, rat, and human tissue in late 1997. The human gene encoding the 1α-hydroxylase is 5 kb in length, located on chromosome 12, and comprises nine exons and eight introns; its intron/exon organization is very similar to that of the other four mitochondrial P450 enzymes cloned to date. Mutations in P450c1α cause 1α-hydroxylase deficiency, also known as vitamin D- dependent rickets type 1, a rare autosomal recessive disease characterized by rickets and impaired growth due to failure of renal synthesis of 1,25(OH)2D. To date, 31 patients have been studied and 20 distinct mutations in the gene identified, including 13 mis-sense mutations, none of which encode a protein with significant enzyme activity. Recent studies in animals demonstrate that regulation of P450c1α gene expression by parathyroid hormone (PTH), low calcium diet, low phosphorus diet, and 1,25(OH)2D occurs at the level of its mRNA. Transcriptional activity of the mouse and human P450c1α gene promoters can be stimulated by PTH, cAMP, and forskolin and suppressed by 1,25(OH)2D. Springer Online Journal Archives 1860-2002 Portale, A. A. oth Miller, W. L. oth in Pediatric nephrology 1987 14(2000) vom: Juli, Seite 620-625 (DE-627)NLEJ188983775 (DE-600)1463004-7 1432-198X nnns volume:14 year:2000 month:07 pages:620-625 extent:6 http://dx.doi.org/10.1007/PL00009639 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 14 2000 7 620-625 6 |
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(DE-627)NLEJ205948995 DE-627 ger DE-627 rakwb eng Human 25-hydroxyvitamin D-1α-hydroxylase: cloning, mutations, and gene expression 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene encoding this enzyme were cloned from mouse, rat, and human tissue in late 1997. The human gene encoding the 1α-hydroxylase is 5 kb in length, located on chromosome 12, and comprises nine exons and eight introns; its intron/exon organization is very similar to that of the other four mitochondrial P450 enzymes cloned to date. Mutations in P450c1α cause 1α-hydroxylase deficiency, also known as vitamin D- dependent rickets type 1, a rare autosomal recessive disease characterized by rickets and impaired growth due to failure of renal synthesis of 1,25(OH)2D. To date, 31 patients have been studied and 20 distinct mutations in the gene identified, including 13 mis-sense mutations, none of which encode a protein with significant enzyme activity. Recent studies in animals demonstrate that regulation of P450c1α gene expression by parathyroid hormone (PTH), low calcium diet, low phosphorus diet, and 1,25(OH)2D occurs at the level of its mRNA. Transcriptional activity of the mouse and human P450c1α gene promoters can be stimulated by PTH, cAMP, and forskolin and suppressed by 1,25(OH)2D. Springer Online Journal Archives 1860-2002 Portale, A. A. oth Miller, W. L. oth in Pediatric nephrology 1987 14(2000) vom: Juli, Seite 620-625 (DE-627)NLEJ188983775 (DE-600)1463004-7 1432-198X nnns volume:14 year:2000 month:07 pages:620-625 extent:6 http://dx.doi.org/10.1007/PL00009639 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 14 2000 7 620-625 6 |
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(DE-627)NLEJ205948995 DE-627 ger DE-627 rakwb eng Human 25-hydroxyvitamin D-1α-hydroxylase: cloning, mutations, and gene expression 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene encoding this enzyme were cloned from mouse, rat, and human tissue in late 1997. The human gene encoding the 1α-hydroxylase is 5 kb in length, located on chromosome 12, and comprises nine exons and eight introns; its intron/exon organization is very similar to that of the other four mitochondrial P450 enzymes cloned to date. Mutations in P450c1α cause 1α-hydroxylase deficiency, also known as vitamin D- dependent rickets type 1, a rare autosomal recessive disease characterized by rickets and impaired growth due to failure of renal synthesis of 1,25(OH)2D. To date, 31 patients have been studied and 20 distinct mutations in the gene identified, including 13 mis-sense mutations, none of which encode a protein with significant enzyme activity. Recent studies in animals demonstrate that regulation of P450c1α gene expression by parathyroid hormone (PTH), low calcium diet, low phosphorus diet, and 1,25(OH)2D occurs at the level of its mRNA. Transcriptional activity of the mouse and human P450c1α gene promoters can be stimulated by PTH, cAMP, and forskolin and suppressed by 1,25(OH)2D. Springer Online Journal Archives 1860-2002 Portale, A. A. oth Miller, W. L. oth in Pediatric nephrology 1987 14(2000) vom: Juli, Seite 620-625 (DE-627)NLEJ188983775 (DE-600)1463004-7 1432-198X nnns volume:14 year:2000 month:07 pages:620-625 extent:6 http://dx.doi.org/10.1007/PL00009639 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 14 2000 7 620-625 6 |
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(DE-627)NLEJ205948995 DE-627 ger DE-627 rakwb eng Human 25-hydroxyvitamin D-1α-hydroxylase: cloning, mutations, and gene expression 2000 6 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene encoding this enzyme were cloned from mouse, rat, and human tissue in late 1997. The human gene encoding the 1α-hydroxylase is 5 kb in length, located on chromosome 12, and comprises nine exons and eight introns; its intron/exon organization is very similar to that of the other four mitochondrial P450 enzymes cloned to date. Mutations in P450c1α cause 1α-hydroxylase deficiency, also known as vitamin D- dependent rickets type 1, a rare autosomal recessive disease characterized by rickets and impaired growth due to failure of renal synthesis of 1,25(OH)2D. To date, 31 patients have been studied and 20 distinct mutations in the gene identified, including 13 mis-sense mutations, none of which encode a protein with significant enzyme activity. Recent studies in animals demonstrate that regulation of P450c1α gene expression by parathyroid hormone (PTH), low calcium diet, low phosphorus diet, and 1,25(OH)2D occurs at the level of its mRNA. Transcriptional activity of the mouse and human P450c1α gene promoters can be stimulated by PTH, cAMP, and forskolin and suppressed by 1,25(OH)2D. Springer Online Journal Archives 1860-2002 Portale, A. A. oth Miller, W. L. oth in Pediatric nephrology 1987 14(2000) vom: Juli, Seite 620-625 (DE-627)NLEJ188983775 (DE-600)1463004-7 1432-198X nnns volume:14 year:2000 month:07 pages:620-625 extent:6 http://dx.doi.org/10.1007/PL00009639 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 14 2000 7 620-625 6 |
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Human 25-hydroxyvitamin D-1α-hydroxylase: cloning, mutations, and gene expression |
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Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene encoding this enzyme were cloned from mouse, rat, and human tissue in late 1997. The human gene encoding the 1α-hydroxylase is 5 kb in length, located on chromosome 12, and comprises nine exons and eight introns; its intron/exon organization is very similar to that of the other four mitochondrial P450 enzymes cloned to date. Mutations in P450c1α cause 1α-hydroxylase deficiency, also known as vitamin D- dependent rickets type 1, a rare autosomal recessive disease characterized by rickets and impaired growth due to failure of renal synthesis of 1,25(OH)2D. To date, 31 patients have been studied and 20 distinct mutations in the gene identified, including 13 mis-sense mutations, none of which encode a protein with significant enzyme activity. Recent studies in animals demonstrate that regulation of P450c1α gene expression by parathyroid hormone (PTH), low calcium diet, low phosphorus diet, and 1,25(OH)2D occurs at the level of its mRNA. Transcriptional activity of the mouse and human P450c1α gene promoters can be stimulated by PTH, cAMP, and forskolin and suppressed by 1,25(OH)2D. |
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Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene encoding this enzyme were cloned from mouse, rat, and human tissue in late 1997. The human gene encoding the 1α-hydroxylase is 5 kb in length, located on chromosome 12, and comprises nine exons and eight introns; its intron/exon organization is very similar to that of the other four mitochondrial P450 enzymes cloned to date. Mutations in P450c1α cause 1α-hydroxylase deficiency, also known as vitamin D- dependent rickets type 1, a rare autosomal recessive disease characterized by rickets and impaired growth due to failure of renal synthesis of 1,25(OH)2D. To date, 31 patients have been studied and 20 distinct mutations in the gene identified, including 13 mis-sense mutations, none of which encode a protein with significant enzyme activity. Recent studies in animals demonstrate that regulation of P450c1α gene expression by parathyroid hormone (PTH), low calcium diet, low phosphorus diet, and 1,25(OH)2D occurs at the level of its mRNA. Transcriptional activity of the mouse and human P450c1α gene promoters can be stimulated by PTH, cAMP, and forskolin and suppressed by 1,25(OH)2D. |
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Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene encoding this enzyme were cloned from mouse, rat, and human tissue in late 1997. The human gene encoding the 1α-hydroxylase is 5 kb in length, located on chromosome 12, and comprises nine exons and eight introns; its intron/exon organization is very similar to that of the other four mitochondrial P450 enzymes cloned to date. Mutations in P450c1α cause 1α-hydroxylase deficiency, also known as vitamin D- dependent rickets type 1, a rare autosomal recessive disease characterized by rickets and impaired growth due to failure of renal synthesis of 1,25(OH)2D. To date, 31 patients have been studied and 20 distinct mutations in the gene identified, including 13 mis-sense mutations, none of which encode a protein with significant enzyme activity. Recent studies in animals demonstrate that regulation of P450c1α gene expression by parathyroid hormone (PTH), low calcium diet, low phosphorus diet, and 1,25(OH)2D occurs at the level of its mRNA. Transcriptional activity of the mouse and human P450c1α gene promoters can be stimulated by PTH, cAMP, and forskolin and suppressed by 1,25(OH)2D. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ205948995</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230505183405.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070528s2000 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ205948995</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Human 25-hydroxyvitamin D-1α-hydroxylase: cloning, mutations, and gene expression</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2000</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">6</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The rate-limiting, hormonally regulated step in the bioactivation of vitamin D is the 1α-hydroxylation of 25-hydroxyvitamin D, which occurs in the kidney and other tissues and is catalyzed by the mitochondrial cytochrome P450 enzyme, P450c1α. After many years of effort, the cDNA and gene encoding this enzyme were cloned from mouse, rat, and human tissue in late 1997. The human gene encoding the 1α-hydroxylase is 5 kb in length, located on chromosome 12, and comprises nine exons and eight introns; its intron/exon organization is very similar to that of the other four mitochondrial P450 enzymes cloned to date. Mutations in P450c1α cause 1α-hydroxylase deficiency, also known as vitamin D- dependent rickets type 1, a rare autosomal recessive disease characterized by rickets and impaired growth due to failure of renal synthesis of 1,25(OH)2D. To date, 31 patients have been studied and 20 distinct mutations in the gene identified, including 13 mis-sense mutations, none of which encode a protein with significant enzyme activity. Recent studies in animals demonstrate that regulation of P450c1α gene expression by parathyroid hormone (PTH), low calcium diet, low phosphorus diet, and 1,25(OH)2D occurs at the level of its mRNA. Transcriptional activity of the mouse and human P450c1α gene promoters can be stimulated by PTH, cAMP, and forskolin and suppressed by 1,25(OH)2D.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Portale, A. A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Miller, W. L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Pediatric nephrology</subfield><subfield code="d">1987</subfield><subfield code="g">14(2000) vom: Juli, Seite 620-625</subfield><subfield code="w">(DE-627)NLEJ188983775</subfield><subfield code="w">(DE-600)1463004-7</subfield><subfield code="x">1432-198X</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:14</subfield><subfield code="g">year:2000</subfield><subfield code="g">month:07</subfield><subfield code="g">pages:620-625</subfield><subfield code="g">extent:6</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/PL00009639</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">14</subfield><subfield code="j">2000</subfield><subfield code="c">7</subfield><subfield code="h">620-625</subfield><subfield code="g">6</subfield></datafield></record></collection>
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