Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.30.1 (S1 nuclease)
 3,660 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Murine complement protein H is encoded by a 100-kb gene on chromosome 1. A 3.2-kb fragment of the 5' flanking region of the H gene was sequenced, and two transcription start sites for this gene were identified by RNase protection and S1 nuclease analyses, each of which had upstream TATA and CAAT boxes. This region shares sequence homology with known regulatory elements, including the SV40 enhancer consensus, the Sp1 binding site, and two glucocorticoid-responsive core elements (GRE). Tissue and cell-line specificity has been examined by Northern analysis, and the 4.4-kb full-length H messenger RNA was identified in liver, kidney, spleen, thymus, liver cell line 1469, and L cells. IFN-gamma did not induce H mRNA expression in the macrophage cell line P388D.1 but had a positive effect on both the mRNA and protein levels of H in L cells. PMA, LPS, and vitamin D did not increase H mRNA levels in L cells. Pursuant to the discovery of two GRE in the 5' regulatory region of the H gene, we examined the effects of glucocorticoids on H mRNA expression. Dexamethasone (10(-7) M) was found to increase markedly the levels of H mRNA and protein after 24 h of incubation, and the effect on the mRNA was detectable by 30 min. The fact that H is a down-regulator of complement activation is consistent with the known immunosuppressive role of glucocorticoids. To our knowledge, this is the first time that dexamethasone has been shown to increase the levels of a complement protein.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Analysis of complement factor H mRNA expression: dexamethasone and IFN-gamma increase the level of H in L cells. 253 12

Vitamin D-dependent 28-kDa calcium-binding protein (CaBP28) cDNA clones were isolated from a chicken intestinal library. The nucleotide sequence analysis of the CaBP28 cDNA shows an open reading frame of 786 nucleotides, coding for a 262-amino acid 30.167-kDa protein. Interestingly, the protein contains six repeats of a domain with the feature of a calcium-binding site. In two of the six domains, oxygen-containing amino acids important for the positioning of calcium are absent, suggesting that these two sites have lost their calcium-binding capability and might have adopted a new function in evolution. In the chicken intestine, three different sized species of CaBP28 mRNA (2.0, 2.8, and 3.1 kilobases) are detected. Primer extension and S1 nuclease mapping show that the three CaBP28 mRNA species share a common 5' end but differ in the length of their 3' noncoding sequence. A similar triplet of CaBP28 mRNAs is identified in the rat kidney by the chicken probe, showing an interspecies conservation of the CaBP28. In the rat intestine, however, no CaBP28 mRNA could be detected. Instead, a vitamin D-dependent 9-kDa CaBP (CaBP9) is expressed, with an mRNA size of approximately equal to 0.7 kilobase that does not cross-hybridize with the CaBP28 probe. This indicates that the CaBP28 and CaBP9 are the product of two independent genes.
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PMID:The 28-kDa vitamin D-dependent calcium-binding protein has a six-domain structure. 346 88

The rate-limiting, hormonally regulated step in the biosynthesis of the biologically active form of vitamin D, 1,25(OH)2D, is its 1alpha-hydroxylation in the kidney by the mitochondrial P450 enzyme, P450c1alpha. We have recently cloned the human P450c1alpha cDNA and shown that this enzyme is the factor disrupted in vitamin D-dependent rickets, type 1 (VDDR-1). To facilitate the analysis of further patients with VDDR-1 and to permit studies of the regulation of the gene for P450c1alpha, we have used PCR-based tactics to clone the gene. Southern blotting studies indicate that there is only one copy of this gene in the human genome. The complete sequence of all exons and introns show that the gene consists of 9 exons spanning only 5 kb; the entire protein-coding region can be PCR-amplified as a single 4-kb fragment. The transcriptional start site, located by primer extension and S1 nuclease protection, lies 62-bp upstream from the ATG transitional start codon. Analysis of rodent/human somatic cell hybrid DNAs show that this gene lies on chromosome 12. Although the gene is substantially smaller than the human genes for other mitochondrial enzymes, its intron/exon organization is very similar, especially to that of P450scc. This indicates that although the mitochondrial P450 enzymes retain only 30%-40% amino acid sequence identity, they all belong to a single evolutionary lineage.
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PMID:Complete structure of the human gene for the vitamin D 1alpha-hydroxylase, P450c1alpha. 942 99