The molecular basis for genetic polymorphism of human deoxyribonuclease I: identification of the nucleotide substitution that generates the fourth allele

Yasuda, Toshihiro; Nadano, Daita; Takeshita, Hitoshi; Tenjo, Etsuko; Sawazaki, Kazumi; Ootani, Masahiro; Kishi, Koichiro

doi:10.1016/0014-5793(95)00037-a

Cited by 23 publications

(7 citation statements)

References 17 publications

(27 reference statements)

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“…350 bp and 300 bp respectively) to be amplified separately and identified. Each PCR and RACE product was directly subcloned into TA cloning vector pCR II (Invitrogen, San Diego, CA, U.S.A.) and sequenced [31,32]. Sequence analysis of each fragment was performed at least three times.…”

Section: Designationmentioning

confidence: 99%

“…However, a full-length cDNA encoding DNase I has not yet been isolated from any mammal. With regard to the genomic structure of the DNase I gene, we have isolated and sequenced the structural gene encoding human DNase I [30] and elucidated the complete molecular basis for its genetic polymorphism [30][31][32]. The DNase I gene comprises at least nine exons, spanning approx.…”

Section: Introductionmentioning

confidence: 99%

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Rabbit DNase I: purification from urine, immunological and proteochemical characterization, nucleotide sequence, expression in tissues, relationships with other mammalian DNases I and phylogenetic analysis

Yasuda

Takeshita

Nakajima

et al. 1997

Biochemical Journal

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DNase I from rabbit urine was purified approx. 3600-fold to apparent homogeneity with a 41% yield by affinity chromatography utilizing DNA-cellulose; the purity of the final preparation was assessed by SDS/PAGE, lack of contamination by other nucleases and production of a monospecific antibody against the enzyme. Although the proteochemical and enzymological properties of the purified enzyme resembled those of other mammalian DNases I, the enzymic activity of rabbit DNase I was less efficiently inhibited by monomeric actin than was that of human DNase I, probably due to substitution of an amino acid residue involved in actin binding (Tyr-65 to Phe). The effects of specific antibodies to human, rabbit and rat DNases I on the activities of the corresponding purified enzymes revealed that human DNase I lies between the rat and rabbit enzymes with regard to its immunological properties. An 1158 bp full-length cDNA encoding rabbit DNase I was constructed from the total RNA of rabbit pancreas using a combination of reverse transcriptase-PCR and rapid amplification of cDNA ends, followed by sequencing. This identified a 17- or 21-amino-acid signal sequence, with the mature enzyme containing 260 amino acids and a single N-glycosylation site at Asn-18. The amino acid sequence deduced from the cDNA sequence exactly matched that determined proteochemically from the purified enzyme up to residue 20. A systematic survey of DNase I distribution as measured by both enzymic activity and DNase I gene transcripts in 12 rabbit tissues showed the pancreas and parotid gland to produce equivalent levels, higher than those in other tissues. Enzymic activity and DNase I gene expression levels in each tissue correlated well. The results of phylogenetic and sequence identity analysis, immunological properties and tissue-distribution patterns of DNase I indicated a closer relationship between the rabbit and human enzymes than for other mammalian DNases I. Furthermore, differences between the enzymic activities expressed in mammalian parotid gland and pancreas suggest that the distribution of DNase I in mammalian tissue is species-specific.

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Section: Designationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Rabbit DNase I: purification from urine, immunological and proteochemical characterization, nucleotide sequence, expression in tissues, relationships with other mammalian DNases I and phylogenetic analysis

Yasuda

Takeshita

Nakajima

et al. 1997

Biochemical Journal

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“…Our recent studies [6][7][8][9] have elucidated the complete molecular basis for the genetic poly morphism of DNase 1. and on the basis of this, a new DNase I-genotyping system using the polymerase chain reaction (PCR) has been developed [10].…”

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confidence: 99%

Population Studies of Human Deoxyribonuclease I Polymorphism

et al. 1997

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We have improved the resolution of the conventional method for phenotyping deoxyribonuclease I (DNase I), which makes use of isoelectric focusing, by the addition of amphoteric separators. The distribution of DNase I phenotypes was extensively examined using this improved method in 1,212 unrelated individuals from a Japanese population. In order to investigate a possible difference in phenotype distribution between different populations, DNA samples from Germans and African Americans were genotyped using the polymerase chain reaction. The DNASE 1*2 allele in the German population was found to be predominant among the four alleles of DNase I, in contrast to the Japanese population. These results are the first to demonstrate a wide distribution of DNase I polymorphism in the Japanese population as well as in two other populations.

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“…A pI in the range of 3.5-4.3 has been reported for the human enzyme (25,27,29), and is similar to the range of 4.7-5.2 for the ladder of bands of bDNase in IEF analysis (22). The IEF pattern of desialylated human DNase (hDNase) has been extensively investigated in conjunction with studies of the genetic basis for charge heterogeneity of hDNase isoforms (27)(28)(29)(30)(31)(32)(33)(34)73). The cDNA sequence of human DNase I and characteristics of the recombinant protein expressed in mammalian cells have been reported by Shak et al (35).…”

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confidence: 72%

Human DNase I Contains Mannose 6-Phosphate and Binds the Cation-Independent Mannose 6-Phosphate Receptor

Cacia¹,

Quan²,

Pai³

et al. 1998

Biochemistry

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DNase I isolated from human urine (hDNase) or expressed in Chinese hamster ovary (CHO) cells contains mannose-phosphorylated oligosaccharides. hDNase binds to a column of immobilized cation-independent mannose 6-phosphate receptor, with the strongest binding exhibited by the protein bearing diphosphorylated oligosaccharides. The binding is inhibited by 5 mM mannose 6-phosphate, and can be prevented by prior treatment of hDNase with alkaline phosphatase. Phosphorylated high-mannose oligosaccharides were observed at both sites of glycosylation in hDNase by high-performance liquid chromatography-mass spectrometry of a tryptic digest. These results indicate that hDNase, though not an acid hydrolase, may enter the lysosomal trafficking pathway, and may have evolved from a lysosomal enzyme.

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The molecular basis for genetic polymorphism of human deoxyribonuclease I: identification of the nucleotide substitution that generates the fourth allele

Cited by 23 publications

References 17 publications

Rabbit DNase I: purification from urine, immunological and proteochemical characterization, nucleotide sequence, expression in tissues, relationships with other mammalian DNases I and phylogenetic analysis

Rabbit DNase I: purification from urine, immunological and proteochemical characterization, nucleotide sequence, expression in tissues, relationships with other mammalian DNases I and phylogenetic analysis

Population Studies of Human Deoxyribonuclease I Polymorphism

Human DNase I Contains Mannose 6-Phosphate and Binds the Cation-Independent Mannose 6-Phosphate Receptor

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