Detection of deoxyribonucleases I and II (dnases I and II) activities in reproductive organs of male rabbits

Takeshita, Hitoshi; Yasuda, Toshihiro; Nadano, Daita; Tenjo, Etsuko; Sawazaki, Kazumi; Iida, Reiko; Kishi, Koichiro

doi:10.1016/0020-711x(94)90074-4

Cited by 30 publications

(17 citation statements)

References 22 publications

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“…DNase II was isolated directly from lysosomes in the porcine spleen (2) and from rat and monkey livers (3,4). DNase II activity is known to occur in various mammalian tissues (5)(6)(7)(8). Although the enzymological properties of DNase II from different tissues and species are very similar, inconsistencies in the chemical properties of these enzymes (for example, with regard to molecular mass or subunit structure) have been recognized.…”

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confidence: 99%

Molecular Cloning of the cDNA Encoding Human Deoxyribonuclease II

Yasuda¹,

Takeshita²,

Iida³

et al. 1998

Journal of Biological Chemistry

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confidence: 99%

Molecular Cloning of the cDNA Encoding Human Deoxyribonuclease II

Yasuda¹,

Takeshita²,

Iida³

et al. 1998

Journal of Biological Chemistry

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“…1988). I n addition to these findings, the presence of DNase I activity outside the digestive system (Nadano et al 1993;Yasuda et al 1993b;Takeshita et al 1994) suggests that it has biological functions other than just its digestive one. Genetic polymorphism of human DNase I has been demonstrated by differences among the PI values of type-specific isozymes .…”

Section: Introductionmentioning

confidence: 97%

“…Genetic polymorphism of human DNase I has been demonstrated by differences among the PI values of type-specific isozymes . The favourable distribution of its gene frequencies and availability of a highly sensitive phenotyping method (Yasuda et al , 1994 have enabled the enzyme to be used as an efficient marker for genetic, forensic and clinical studies (Sawazaki et al 1993;Tenjo et al 1993; Yasuda et al 1 9 9 3~) .…”

Section: Introductionmentioning

confidence: 99%

Molecular analysis of the third allele of human deoxyribonuclease I polymorphism

Yasuda

Nadano

Takeshita

et al. 1995

Annals of Human Genetics

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In addition to common phenotypes 1, 1-2 and 2 of human deoxyribonuclease I (DNase I), phenotypes 1-3 and 2-3, encoded by a third allele DNASE1*3, have been found by means of isoelectric focusing. The main objective of this study was to identify the mutation site(s) underlying phenotype 3. All eight exons covering the entire open reading frame of the human DNase I structural gene were amplified by the polymerase chain reaction (PCR) and subjected to direct DNA sequencing. When the entire 780-bp coding region and exon/intron junctions of the DNase I gene of two individuals with phenotypes 1-3 and 2-3 were sequenced, only one nucleotide substitution, a C-G transition (CCC-->GCC), in the codon for amino acid 132 of the mature enzyme located in exon VI was found that resulted in the replacement of proline with alanine (P132A). The mutation was confirmed by allele-specific amplification of genomic DNA. The replacement of the amino acid residue may reduce the hydrophobicity of the enzyme and thus increase the pI value of the type-3 isozyme compared with that of type 1, as increasing the hydrophobicity of a protein is known to decrease its pI value. The specific PCR-amplifications of exons and alleles developed in this study may provide a new tool suitable for rapid screening of DNase I variants.

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“…Deoxyribonuclease I (DNase I, EC 3.1.21.1) is an enzyme that preferentially attacks, by Ca 2+ ‐and Mg 2+ ‐dependent endonucleolytic cleavage, double‐stranded DNA to produce oligonucleotides with 5′‐phospho and 3′‐hydroxy termini [1]. It is considered to play a major role in digestion in the alimentary canal, because, in mammals, it is secreted by exocrine glands such as the pancreas and/or parotid gland [2–7]. However, DNase I also exists outside the alimentary tract [8–11], raising a doubt as to whether its major role in DNA metabolism in vivo is merely digestion.…”

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A single amino acid substitution of Leu130Ile in snake DNases I contributes to the acquisition of thermal stability

Takeshita

Yasuda²,

Nakajima

et al. 2003

European Journal of Biochemistry

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We purified pancreatic deoxyribonucleases I (DNases I) from three snakes, Elaphe quadrivirgata, Elaphe climacophora and Agkistrodon blomhoffii, and cloned their cDNAs. Each mature snake DNase I protein comprised 262 amino acids. Wild‐type snake DNases I with Leu130 were more thermally unstable than wild‐type mammalian and avian DNases I with Ile130. After substitution of Leu130Ile, the thermal stabilities of the snake enzymes were higher than those of their wild‐type counterparts and similar to mammalian wild‐type enzyme levels. Conversely, substituting Ile130Leu of mammalian DNases I made them more thermally unstable than their wild‐type counterparts. Therefore, a single amino acid substitution, Leu130Ile, might be involved in an evolutionally critical change in the thermal stabilities of vertebrate DNases I. Amphibian DNases I have a Ser205 insertion in a Ca2+‐binding site of mammalian and avian enzymes that reduces their thermal stabilities [Takeshita, H., Yasuda, T., Iida, R., Nakajima, T., Mori, S., Mogi, K., Kaneko, Y. & Kishi, K. (2001) Biochem. J.357, 473–480]. Thus, it is plausible that the thermally stable wild‐type DNases I of the higher vertebrates, such as mammals and birds, have been generated by a single Leu130Ile substitution of reptilian enzymes through molecular evolution following Ser205 deletion from amphibian enzymes. This mechanism may reflect one of the evolutionary changes from cold‐blooded to warm‐blooded vertebrates.

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Detection of deoxyribonucleases I and II (dnases I and II) activities in reproductive organs of male rabbits

Cited by 30 publications

References 22 publications

Molecular Cloning of the cDNA Encoding Human Deoxyribonuclease II

Molecular Cloning of the cDNA Encoding Human Deoxyribonuclease II

Molecular analysis of the third allele of human deoxyribonuclease I polymorphism

A single amino acid substitution of Leu130Ile in snake DNases I contributes to the acquisition of thermal stability

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