Isolation of Ca, Mg-dependent nuclear endonuclease as a principal component of the nuclease complex of human lymphocyte chromatin

Khodarev, Nikolai N.; Соколова, И. А.; Александрова, С. С.; Volgina, Veronica V.; Votrin, I. I.

doi:10.1007/bf00840558

Cited by 2 publications

(3 citation statements)

References 10 publications

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“…Both Mg 2+ and Mg 2+/ Ca 2+ endonucleases have been isolated from rat liver nuclei, while several nuclear nucleases have been isolated from rat thymocytes − Physiological concentrations of Zn 2+ known to inhibit apoptosis also inhibit the activity of these Ca 2+ /Mg 2+ nucleases, which are found extensively in lymphocyte tissue. Other than inhibition by zinc, the activity of these nucleases may be regulated at the transcriptional level.…”

Section: E General Nucleasesmentioning

confidence: 99%

“…105 These nuclear Ca 2+ /Mg 2+ -dependent endonucleases have been implicated in the extensive internucleosomal DNA fragmentation arising during programmed cell death (apoptosis) and are potential targets for drug design. [106][107][108][109][110] Physiological concentrations of Zn 2+ known to inhibit apoptosis also inhibit the activity of these Ca 2+ /Mg 2+ nucleases, which are found extensively in lymphocyte tissue. Other than inhibition by zinc, the activity of these nucleases may be regulated at the transcriptional level.…”

Section: E General Nucleasesmentioning

confidence: 99%

See 1 more Smart Citation

Metal Activation of Enzymes in Nucleic Acid Biochemistry

1998

Chem. Rev.

391

267

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Section: E General Nucleasesmentioning

confidence: 99%

Section: E General Nucleasesmentioning

confidence: 99%

Metal Activation of Enzymes in Nucleic Acid Biochemistry

1998

Chem. Rev.

391

267

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“…For example, it is well known that Ca2+/Mg2+-dependent nuclease can be poly(ADP-ribosy1)ated and that this modification inhibits its activity [31,401. A lot of preparations of enzymes belonging to this group of nucleases have been described [22,23,[25][26][27][28][29][30][41][42][43]. They are variable, in their affinity to different ion exchangers, molecular mass and some other properties but differ from DNase-I-like nucleases by showing the maximum activity in the presence of a combination of Ca2+ and Mg2+ or Mn2+, insensitivity to G-actin, inhibition of their activity by iodacetamide and N-ethylmaleimide [25,26,301.…”

Section: Discussionmentioning

confidence: 99%

Properties of some nuclear nucleases of rat thymocytes and their changes in radiation‐induced apoptosis

Nikonova

Beletsky

Umansky

1993

European Journal of Biochemistry

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Three nuclease activites have been found and characterized in rat thymocyte nuclear extracts. A Mn2+-dependent nuclease is loosely bound to nuclear components and can be extracted with 0.35 M NaCI. The enzyme is activated by MnZ+ but not by Mg", Ca2+, or both. Its molecular mass is 36-40 kDa when measured by gel filtration and 37 kDa by SDSPAGE. An acidic nuclease is independent of divalent ions, produces DNA strand breaks with 5'-OH ends, its molecular mass is about 37 kDa. Two fractions of Ca2+Nn2+-dependent nuclease, differing in binding to CM-Sepharose but identical in other respects, are active in the presence of Mn2+ but can be additionally activated by Ca2+. They are inactive in the presence of Mg'' or Ca2+ but cleave DNA in Ca2'/Mg2'-containing medium. The molecular mass of the enzyme is 22 kDa as determined by both gel filtration and electrophoresis. The dependence of nuclease activities on pH, ions, and sulfhydryl reagents is described. Cycloheximide injection to both control and irradiated animals strongly inhibits the activities of Ca2+/Mn2+-dependent nuclease from thymocyte nuclei separated by chromatography on CMSepharose and does not change the activities of Mn2+-dependent and acidic nucleases. Nuclease activity in thymocyte nuclei from irradiated rats is increased in CaZ+Ng2'-containing and Ca2+/ Mn"-containing media whereas there is no change in the activity of acidic nuclease. CaZ+/Mn2+-dependent nuclease is extracted from thymocyte nuclei of irradiated rats with 0.35 M NaCl but from control nuclei only with 0.5 M NaCl. Possible reasons of labilization of Ca*+Nn*+-dependentnuclease binding to the nuclear structures in dying thymocytes are discussed.In the past decade the concept has been formulated that in most cases the death of cells is the result of their active response to physiological or damaging factors [ 1 -31. This type of cell death was called apoptosis [l] and the recent literatur data suggests that, besides the programmed and physiological cell death [l -31, cell death [5-81. Data indicate the involvement of nuclear nucleases, particularly, Ca2+Ng2+-dependent endonuclease [7, 21 -241 but the mechanism of itdtheir activation in dying cells remain unclear. A number of preparations of this enzyme were purified from different sources but they usually differed in molecular mass, substrate specificity, binding to ion-exchange columns and so on [25-301. Ca2+/Mg2+-nucleases with molecular masses in the range 25-120 kDa with preference for single-stranded or double-stranded DNA are described. The mechanisms of regulation of the nuclease activity are poorly understood. Even the ion dependence of the nuclease differs between various studies. The enzyme is normally inactive in the presence of Mg2+ or Ca" only but is activated by addition of both ions. At the same time the nuclease is normally active in the presence of Mn2+ and the maximal activity is manifested with Mn' + and Caz+ [25, 301. Previously it has been shown that there are different nucleases in rat thymus nuclei but only a CaZ...

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Isolation of Ca, Mg-dependent nuclear endonuclease as a principal component of the nuclease complex of human lymphocyte chromatin

Cited by 2 publications

References 10 publications

Metal Activation of Enzymes in Nucleic Acid Biochemistry

Metal Activation of Enzymes in Nucleic Acid Biochemistry

Properties of some nuclear nucleases of rat thymocytes and their changes in radiation‐induced apoptosis

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