scholarly journals Involvement of DNase II-Like Acid DNase in the Cataract Formation of the UPL Rat and the Shumiya Cataract Rat

2006 ◽  
Vol 29 (12) ◽  
pp. 2367-2371 ◽  
Author(s):  
Noriaki Nagai ◽  
Noriko Takeuchi ◽  
Akira Kamei ◽  
Yoshimasa Ito
Keyword(s):  
Cataract Formation ◽  
Dnase Ii ◽  
Acid Dnase

Drosophila acid DNase is a homolog of mammalian DNase II

Gene ◽  
2002 ◽  
Vol 295 (1) ◽  
pp. 61-70 ◽  
Author(s):  
Cory J. Evans ◽  
John R. Merriam ◽  
Renato J. Aguilera
Keyword(s):  
Dnase Ii ◽  
Acid Dnase

scholarly journals Degradation of nuclear DNA by DNase II-like acid DNase in cortical fiber cells of mouse eye lens

FEBS Journal ◽  
2007 ◽  
Vol 274 (12) ◽  
pp. 3055-3064 ◽  
Author(s):  
Masaki Nakahara ◽  
Akiomi Nagasaka ◽  
Masato Koike ◽  
Kaori Uchida ◽  
Kohki Kawane ◽  
...  
Keyword(s):  
Nuclear Dna ◽  
Eye Lens ◽  
Dnase Ii ◽  
Fiber Cells ◽  
Acid Dnase

scholarly journals Severe Defects in Proliferation and Differentiation of Lens Cells in Foxe3 Null Mice

2005 ◽  
Vol 25 (20) ◽  
pp. 8854-8863 ◽  
Author(s):  
Olga Medina-Martinez ◽  
Isaac Brownell ◽  
Felipe Amaya-Manzanares ◽  
Qiyong Hu ◽  
Richard R. Behringer ◽  
...  
Keyword(s):  
Lens Epithelium ◽  
Abnormal Development ◽  
Distinct Region ◽  
Lens Development ◽  
Forkhead Transcription Factor ◽  
Surface Ectoderm ◽  
Dnase Ii ◽  
Lens Cells ◽  
Acid Dnase ◽  
Normal Lens

ABSTRACT During mouse eye development, the correct formation of the lens occurs as a result of reciprocal interactions between the neuroectoderm that forms the retina and surface ectoderm that forms the lens. Although many transcription factors required for early lens development have been identified, the mechanism and genetic interactions mediated by them remain poorly understood. Foxe3 encodes a winged helix-forkhead transcription factor that is initially expressed in the developing brain and in the lens placode and later restricted exclusively to the anterior lens epithelium. Here, we show that targeted disruption of Foxe3 results in abnormal development of the eye. Cells of the anterior lens epithelium show a decreased rate of proliferation, resulting in a smaller than normal lens. The anterior lens epithelium does not properly separate from the cornea and frequently forms an unusual, multilayered tissue. Because of the abnormal differentiation, lens fiber cells do not form properly, and the morphogenesis of the lens is greatly affected. The abnormally differentiated lens cells remain irregular in shape, and the lens becomes vacuolated. The defects in lens development correlate with changes in the expression of growth and differentiation factor genes, including DNase II-like acid DNase, Prox1, p57, and PDGFα receptor. As a result of abnormal lens development, the cornea and the retina are also affected. While Foxe3 is also expressed in a distinct region of the embryonic brain, we have not observed abnormal development of the brain in Foxe3 −/− animals.

Cloning of a cDNA Encoding a Rat DNase II-like Acid DNase

1999 ◽  
Vol 265 (2) ◽  
pp. 395-399 ◽  
Author(s):  
Sei-ichi Tanuma ◽  
Daisuke Shiokawa
Keyword(s):  
Dnase Ii ◽  
Acid Dnase

scholarly journals An auxiliary mode of apoptotic DNA fragmentation provided by phagocytes

2000 ◽  
Vol 14 (5) ◽  
pp. 549-558 ◽  
Author(s):  
Dorian McIlroy ◽  
Masato Tanaka ◽  
Hideki Sakahira ◽  
Hidehiro Fukuyama ◽  
Misao Suzuki ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Dna Fragmentation ◽  
Apoptotic Cells ◽  
Wild Type ◽  
Chromosomal Dna ◽  
Γ Irradiation ◽  
Dnase Ii ◽  
Striking Increase ◽  
Resistant Form ◽  
Acid Dnase

CAD (caspase-activated DNase) can cause DNA fragmentation in apoptotic cells. Transgenic mice that ubiquitously express a caspase-resistant form of the CAD inhibitor (ICAD) were generated. Thymocytes prepared from the mice were resistant to DNA fragmentation induced by a variety of stimuli. However, similar numbers of TUNEL-positive cells were present in adult tissues of transgenic and wild-type mice. Exposure to γ-irradiation caused a striking increase in the number of TUNEL-positive cells in the thymus of wild-type, but not transgenic, mice. TUNEL-positive nuclei in transgenic mice were confined to thymic macrophages. When apoptotic thymocytes from the transgenic mice were cocultured with macrophages, the thymocytes underwent phagocytosis and their chromosomal DNA underwent fragmentation. This DNA fragmentation was sensitive to inhibitors that block the acidification of lysosomes. Hence, we conclude that the DNA fragmentation that occurs during apoptosis not only can result cell-autonomously from CAD activity but can also be attributed to a lysosomal acid DNase(s), most likely DNase II, after the apoptotic cells are engulfed.

Studies on acid deoxyribonuclease from brain

1969 ◽  
Vol 47 (11) ◽  
pp. 1081-1088 ◽  
Author(s):  
R. Rosenbluth ◽  
Shan-Ching Sung
Keyword(s):  
Dnase Ii ◽  
High Substrate ◽  
Beef Brain ◽  
Acid Dnase ◽  
Acid Deoxyribonuclease ◽  
Substrate Concentrations

An endonucleolytic acid DNase was purified from beef brain. It resembled spleen DNase II with respect to the properties studied: preference for double-strandedness, products of hydrolysis, pH optima, effects of some salts, and the effect of high substrate concentrations on the rate of release of acid-soluble nucleotides. The latter three points are discussed.

scholarly journals Role of nitric oxide and peroxynitrite in apoptosis - relation to endonuclease activity

2003 ◽  
Vol 22 (2) ◽  
pp. 93-100 ◽  
Author(s):  
Gordana Kocic ◽  
Dusica Pavlovic ◽  
Vidosava Djordjevic ◽  
Gordana Bjelakovic ◽  
Ivana Stojanovic
Keyword(s):  
Nitric Oxide ◽  
Biological Effects ◽  
Potential Interaction ◽  
Dnase Ii ◽  
Protective Function ◽  
Caspase Cleavage ◽  
Caspase Cleavage Site ◽  
Inflammatory Stimuli ◽  
Apoptotic Effect ◽  
Acid Dnase

Apoptosis is a form of cell death utilized physiologically to maintain tissue homeostasis, as well as in response to various toxic and inflammatory stimuli or anticancer drugs. Since the process of apoptosis is followed by phagocytosis, the cleavage of DNA to low molecular weight material may serve as a protective function limiting the probability of gene transfer to the nuclei of viable neighbor cells. Many different endonucleases have been proposed as candidates responsible for the internucleosomal cleavage of the genomic DNA observed during apoptosis. The main effect was attributed to the alkaline DNase I (Mg 2+ and caspase-dependent) and acid-DNase II. It was also documented that both of them contain a potential protease (caspase) cleavage site, but they can be also activated upon the influence of other "fragmentation factors", including nitric oxide (NO). The complexity of biological effects induced by NO may be the result of the cell redox state changes, due to its potential interaction with superoxide. The apoptotic effect of both, nitric oxide (NO) and peroxynitrite (ONOO) are dose-dependent and cell-specific may point out the existence of possible "inducible" form of endonuclease.

Secretion of Neutral and Acid DNases in Cultivated Human Lymphocytes after Incubation with DNA; Possible Consequences for Inhalation Anesthesia

1995 ◽  
Vol 50 (5-6) ◽  
pp. 419-424 ◽  
Author(s):  
Manfred Reitz ◽  
Günter Löber ◽  
Peter Kleemann ◽  
Wolfgang Dick
Keyword(s):  
Electrophoretic Mobility ◽  
Human Blood ◽  
Culture Medium ◽  
Human Lymphocytes ◽  
Cell Formation ◽  
Blast Cell ◽  
Dnase Activity ◽  
Inhalation Anesthesia ◽  
Dnase Ii ◽  
Acid Dnase

Abstract After incubation with DNA human lymphocytes release neutral and acid DNase activities into the culture medium; the release depends on DNA concentration and time of cultivation. The electrophoretic mobility of the released neutral DNase activity is in accordance with DNase I and the electrophoretic mobility of the released acid DNase activity with DNase II. The released DNase activities do not originate from dead cells and are not influenced by blast cell formation. The anesthetic halothane can inhibit the released neutral and acid DNase activities. Inhalation anesthesia can possibly disturb the correlation between DNA and DNases in human blood.

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