16 results on '"Kalinski H"'
Search Results
2. Mutation Profile of All 49 Exons of the Human Myosin VIIA Gene, and Haplotype Analysis, in Usher 1B Families from Diverse Origins
- Author
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Adato, A., primary, Weil, D., additional, Kalinski, H., additional, Pel-Or, Y., additional, Ayadi, H., additional, Petit, C., additional, Korostishevsky, M., additional, and Bonne-Tamir, B., additional
- Published
- 1997
- Full Text
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3. Two species of Rev proteins, with distinct N termini, are expressed by caprine arthritis encephalitis virus
- Author
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Gazit, A, primary, Mashiah, P, additional, Kalinski, H, additional, Gast, A, additional, Rosin-Abersfeld, R, additional, Tronick, S R, additional, and Yaniv, A, additional
- Published
- 1996
- Full Text
- View/download PDF
4. 386 DYNAMICS OF SKELETAL HUSCLE PHOSPHODIESTERASE ACTIVITY DURING THE FIRST 24 HOURS OF RECOVERY FROM MILD EXERCISE: EFFECTS OF A PHOSPHODIESTERASE INHIBITOR
- Author
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Kalinski, H. I., primary, Dunbar, C. C., additional, and Michielli, D. W., additional
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- 1994
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5. Amphiphilic poly(α)glutamate polymeric micelles for systemic administration of siRNA to tumors.
- Author
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Krivitsky A, Polyak D, Scomparin A, Eliyahu S, Ofek P, Tiram G, Kalinski H, Avkin-Nachum S, Feiner Gracia N, Albertazzi L, and Satchi-Fainaro R
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- Animals, Antineoplastic Agents chemistry, Breast Neoplasms genetics, Cell Cycle Proteins antagonists & inhibitors, Cell Cycle Proteins genetics, Cell Proliferation drug effects, Female, Humans, Mice, Protein Serine-Threonine Kinases antagonists & inhibitors, Protein Serine-Threonine Kinases genetics, Proto-Oncogene Proteins antagonists & inhibitors, Proto-Oncogene Proteins genetics, RNA, Small Interfering chemistry, RNA, Small Interfering genetics, Surface-Active Agents chemistry, Tumor Cells, Cultured, Xenograft Model Antitumor Assays, rac1 GTP-Binding Protein antagonists & inhibitors, rac1 GTP-Binding Protein genetics, Polo-Like Kinase 1, Antineoplastic Agents administration & dosage, Breast Neoplasms therapy, Micelles, Polyglutamic Acid chemistry, Polymers chemistry, RNA, Small Interfering administration & dosage, RNAi Therapeutics
- Abstract
RNAi therapeutics carried a great promise to the area of personalized medicine: the ability to target "undruggable" oncogenic pathways. Nevertheless, their efficient tumor targeting via systemic administration had not been resolved yet. Amphiphilic alkylated poly(α)glutamate amine (APA) can serve as a cationic carrier to the negatively-charged oligonucleotides. APA polymers complexed with siRNA to form round-shaped, homogenous and reproducible nano-sized polyplexes bearing ~50 nm size and slightly negative charge. In addition, APA:siRNA polyplexes were shown to be potent gene regulators in vitro. In light of these preferred physico-chemical characteristics, their performance as systemically-administered siRNA nanocarriers was investigated. Intravenously-injected APA:siRNA polyplexes accumulated selectively in tumors and did not accumulate in the lungs, heart, liver or spleen. Nevertheless, the polyplexes failed to induce specific mRNA degradation, hence neither reduction in tumor volume nor prolonged mice survival was seen., (Copyright © 2017 Elsevier Inc. All rights reserved.)
- Published
- 2018
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6. Systemic delivery of siRNA by aminated poly(α)glutamate for the treatment of solid tumors.
- Author
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Polyak D, Krivitsky A, Scomparin A, Eliyahu S, Kalinski H, Avkin-Nachum S, and Satchi-Fainaro R
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- Amination, Animals, Cell Line, Tumor, HeLa Cells, Humans, Mice, Mice, Inbred BALB C, Neoplasms genetics, RNA, Small Interfering genetics, RNA, Small Interfering therapeutic use, RNAi Therapeutics, rac1 GTP-Binding Protein genetics, Gene Transfer Techniques, Neoplasms therapy, Polyglutamic Acid chemistry, RNA, Small Interfering administration & dosage
- Abstract
Small interfering RNA (siRNA) can silence the expression of a targeted gene in a process known as RNA interference (RNAi). As a consequence, RNAi has immense potential as a novel therapeutic approach in cancer targeted therapy. However, successful application of siRNA for therapeutic purposes is challenging due to its rapid renal clearance, degradation by RNases in the bloodstream, poor cellular penetration, immunogenicity and aggregation in the blood. In addition, the few oligonucleotide-based nanomedicines that reached clinical trials either go to the liver following systemic administration or are applied topically. Treatment of solid tumors requires selective distribution of siRNA to the target tissue, hence there is an unmet medical need for an efficacious and safe nano-sized delivery system for their clinical use. To overcome these hurdles, we have designed, synthesized and physico-chemically characterized a novel nanocarrier based on aminated poly(α)glutamate (PGAamine). This cathepsin B-biodegradable polymer interacts electrostatically with the siRNA to form a nano-sized polyplex stable in plasma. Treatment with PGAamine-Rac1 siRNA polyplex (siRac1-polyplex) caused specific gene silencing by 80% in HeLa and SKOV-3 human ovarian adenocarcinoma cells as opposed to PGAamine-control non-targeting siRNA polyplex (siCtrl-polyplex) leading to inhibition of cell migration and wound healing abilities. A stepwise dose escalation was performed in order to determine the in vivo maximum tolerated dose (MTD). This was followed by intraperitoneal administration of siRac1-polyplex to mCherry-labeled ovarian adenocarcinoma-bearing mice leading to preferred tumor accumulation of siRac1 (8-fold) which resulted in 38% Rac1 knockdown. Furthermore, the polyplex was administered intravenously to lung carcinoma-bearing mice in which it caused 33% Rac1 knockdown. These promising results led to efficacy studies administering systemic treatment with an anticancer siRNA, siPlk1-polyplex, which inhibited tumor growth by 73% and 87% compared with siCtrl-polyplex or saline-treated mice, respectively, leading to prolonged overall survival. These findings represent the first time that a polyaminated poly(α)glutamate polymer is used for an efficacious and safe tumor delivery of RNAi following systemic administration., (Copyright © 2017 Elsevier B.V. All rights reserved.)
- Published
- 2017
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7. siRNA-Mediated Knockdown of the mTOR Inhibitor RTP801 Promotes Retinal Ganglion Cell Survival and Axon Elongation by Direct and Indirect Mechanisms.
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Morgan-Warren PJ, O'Neill J, de Cogan F, Spivak I, Ashush H, Kalinski H, Ahmed Z, Berry M, Feinstein E, Scott RA, and Logan A
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- Animals, Cell Survival physiology, Disease Models, Animal, Enzyme-Linked Immunosorbent Assay, Gene Knockdown Techniques, Immunohistochemistry, Immunosuppressive Agents pharmacology, Intravitreal Injections, Male, Nerve Crush, Nerve Growth Factors metabolism, Optic Nerve Injuries etiology, Optic Nerve Injuries prevention & control, Rats, Rats, Wistar, Retinal Ganglion Cells metabolism, Sirolimus pharmacology, TOR Serine-Threonine Kinases metabolism, Transcription Factors, Transfection, Axons physiology, Gene Expression Regulation physiology, Nerve Regeneration physiology, RNA, Small Interfering pharmacology, Repressor Proteins genetics, Retinal Ganglion Cells cytology, TOR Serine-Threonine Kinases antagonists & inhibitors
- Abstract
Purpose: To investigate, using in vivo and in vitro models, retinal ganglion cell (RGC) neuroprotective and axon regenerative effects and underlying mechanisms of siRTP801, a translatable small-interfering RNA (siRNA) targeting the mTOR negative regulator RTP801., Methods: Adult rats underwent optic nerve (ON) crush (ONC) followed by intravitreal siRTP801 or control siRNA (siEGFP) every 8 days, with Brn3a+ RGC survival, GFAP+ reactive gliosis, and GAP43+ regenerating axons analyzed immunohistochemically 24 days after injury. Retinal cultures, prepared from uninjured animals or 5 days after ONC to activate retinal glia, were treated with siRTP801/controls in the presence/absence of rapamycin and subsequently assessed for RGC survival and neurite outgrowth, RTP801 expression, glial responses, and mTOR activity. Conditioned medium was analyzed for neurotrophin titers by ELISA., Results: Intravitreal siRTP801 enabled 82% RGC survival compared to 45% with siEGFP 24 days after ONC, correlated with greater GAP43+ axon regeneration at 400 to 1200 μm beyond the ONC site, and potentiated the reactive GFAP+ Müller glial response. In culture, siRTP801 had a direct RGC neuroprotective effect, but required GFAP+ activated glia to stimulate neurite elongation. The siRTP801-induced neuroprotection was significantly reduced, but not abolished, by rapamycin. The siRTP801 potentiated the production and release of neurotrophins NGF, NT-3, and BDNF, and prevented downregulation of RGC mTOR activity., Conclusions: The RTP801 knockdown promoted RGC survival and axon elongation after ONC, without increasing de novo regenerative sprouting. The neuroprotection was predominantly direct, with mTORC1-dependent and -independent components. Enhanced neurite/axon elongation by siRTP801 required the presence of activated retinal glia and was mediated by potentiated secretion of neurotrophic factors.
- Published
- 2016
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8. Delayed intrathecal delivery of RhoA siRNA to the contused spinal cord inhibits allodynia, preserves white matter, and increases serotonergic fiber growth.
- Author
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Otsuka S, Adamson C, Sankar V, Gibbs KM, Kane-Goldsmith N, Ayer J, Babiarz J, Kalinski H, Ashush H, Alpert E, Lahav R, Feinstein E, and Grumet M
- Subjects
- Animals, Disease Models, Animal, Female, Hyperalgesia genetics, Injections, Spinal, Nerve Regeneration genetics, RNA, Small Interfering genetics, Rats, Rats, Sprague-Dawley, Spinal Cord Injuries genetics, Up-Regulation physiology, rhoA GTP-Binding Protein antagonists & inhibitors, rhoA GTP-Binding Protein genetics, Genetic Therapy methods, Hyperalgesia therapy, RNA, Small Interfering administration & dosage, Serotonin physiology, Spinal Cord Injuries therapy, rhoA GTP-Binding Protein administration & dosage
- Abstract
RhoA is a key regulator of the actin cytoskeleton that is upregulated after spinal cord injury (SCI). We analyzed different methods for siRNA delivery and developed siRNAs targeting RhoA (siRhoA) for SCI treatment. Cy 3.5-labeled siRNA delivered at the time of SCI yielded fluorescence in several cell types in the injury site. Intraspinal injections of chemically stabilized siRhoA into the spinal cord of injured rats reduced RhoA protein levels after 1 week and improved hindlimb walking over 6 weeks. To explore a less invasive route, we tested intrathecal injection of Cy 3.5-labeled siRNA via lumbar puncture 1 day after SCI, which resulted in robust uptake in the T9-T10 injury site. Lumbar injection of siRhoA 1 day after SCI reduced RhoA mRNA and protein levels 3 days after injection. Although siRhoA treatment did not yield significant improvement in locomotion, it decreased tactile hypersensitivity significantly compared to controls. Histological analysis at 8 weeks showed significant improvement in white matter sparing with siRhoA compared to control siRNA. siRhoA treatment also resulted in less accumulation of ED1+macrophages, increased PKC-γ immunoreactivity in the corticospinal tract rostral to the injury site, and increased serotonergic fiber growth 12 mm caudal to the contusion site. The ability of siRhoA to preserve white matter and promote serotonergic axonal regrowth caudal to the injury site is likely to suppress allodynia. This provides justification for considering clinical development of RhoA inhibitors to treat SCI sub-acutely to reduce allodynia, which occurs frequently in SCI patients.
- Published
- 2011
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9. siRNA targeted to p53 attenuates ischemic and cisplatin-induced acute kidney injury.
- Author
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Molitoris BA, Dagher PC, Sandoval RM, Campos SB, Ashush H, Fridman E, Brafman A, Faerman A, Atkinson SJ, Thompson JD, Kalinski H, Skaliter R, Erlich S, and Feinstein E
- Subjects
- Acute Kidney Injury chemically induced, Acute Kidney Injury metabolism, Animals, Antineoplastic Agents adverse effects, Apoptosis drug effects, Cisplatin adverse effects, Kidney Tubules, Proximal injuries, Male, RNA, Small Interfering pharmacology, Rats, Rats, Sprague-Dawley, Rats, Wistar, Reperfusion Injury metabolism, Tumor Suppressor Protein p53 metabolism, Up-Regulation drug effects, Acute Kidney Injury drug therapy, Kidney Tubules, Proximal metabolism, RNA, Small Interfering therapeutic use, Reperfusion Injury drug therapy, Tumor Suppressor Protein p53 antagonists & inhibitors
- Abstract
Proximal tubule cells (PTCs), which are the primary site of kidney injury associated with ischemia or nephrotoxicity, are the site of oligonucleotide reabsorption within the kidney. We exploited this property to test the efficacy of siRNA targeted to p53, a pivotal protein in the apoptotic pathway, to prevent kidney injury. Naked synthetic siRNA to p53 injected intravenously 4 h after ischemic injury maximally protected both PTCs and kidney function. PTCs were the primary site for siRNA uptake within the kidney and body. Following glomerular filtration, endocytic uptake of Cy3-siRNA by PTCs was rapid and extensive, and significantly reduced ischemia-induced p53 upregulation. The duration of the siRNA effect in PTCs was 24 to 48 h, determined by levels of p53 mRNA and protein expression. Both Cy3 fluorescence and in situ hybridization of siRNA corroborated a short t(1/2) for siRNA. The extent of renoprotection, decrease in cellular p53 and attenuation of p53-mediated apoptosis by siRNA were dose- and time-dependent. Analysis of renal histology and apoptosis revealed improved injury scores in both cortical and corticomedullary regions. siRNA to p53 was also effective in a model of cisplatin-induced kidney injury. Taken together, these data indicate that rapid delivery of siRNA to proximal tubule cells follows intravenous administration. Targeting siRNA to p53 leads to a dose-dependent attenuation of apoptotic signaling, suggesting potential therapeutic benefit for ischemic and nephrotoxic kidney injury.
- Published
- 2009
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10. Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer.
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May D, Itin A, Gal O, Kalinski H, Feinstein E, and Keshet E
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- Animals, Apoptosis, Brain Neoplasms pathology, Carcinoma, Hepatocellular pathology, Cell Proliferation, Glioma pathology, Helix-Loop-Helix Motifs, Humans, Hypoglycemia, Hypoxia-Inducible Factor 1, Hypoxia-Inducible Factor 1, alpha Subunit, Liver Neoplasms pathology, Membrane Glycoproteins genetics, Mice, Mice, Nude, Neovascularization, Pathologic, Oxidoreductases genetics, Tumor Cells, Cultured, Up-Regulation, Vascular Endothelial Growth Factor A biosynthesis, Vascular Endothelial Growth Factor A genetics, Cell Hypoxia, DNA-Binding Proteins pharmacology, Membrane Glycoproteins biosynthesis, Membrane Glycoproteins pharmacology, Nuclear Proteins pharmacology, Oxidoreductases biosynthesis, Oxidoreductases pharmacology, Transcription Factors pharmacology, Vascular Endothelial Growth Factor A metabolism
- Abstract
Oxygen is the ultimate source of oxidizing power for disulfide bond formation, suggesting that under limiting oxygen proper protein folding might be compromised. We show that secretion of vascular endothelial growth factor (VEGF), a protein with multiple disulfide bonds, was indeed impeded under hypoxia and was partially restored by artificial increase of oxidizing equivalents with diamide. Physiologically, the oxireductase endoplasmic reticulum oxidoreductin-1 (Ero1)-L alpha, but not other proteins in the relay of disulfide formation, was strongly upregulated by hypoxia and independently by hypoglycemia, two known accompaniments of tumors. Further, we provide genetic evidence that induction of Ero1-L alpha by hypoxia and hypoglycemia is mediated by the transcription factor hypoxia-inducible factor 1 (HIF-1) but is independent of p53. In natural human tumors, Ero1-L alpha mRNA was specifically induced in hypoxic microenvironments coinciding with that of upregulated VEGF expression. To establish a physiological relevance to modulations in Ero1-L alpha levels, we showed that even a modest, two- to three-fold reduction in Ero1-L alpha production via siRNA leads to significant inhibition of VEGF secretion, a compromised proliferation capacity and enhanced apoptosis. Together, these findings demonstrate that hypoxic induction of Ero1-L alpha is the key adaptive response in a previously unrecognized HIF-1-mediated pathway that operates to improve protein secretion under hypoxia and might be harnessed for inhibiting tumor growth via inhibiting VEGF-driven angiogenesis.
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- 2005
- Full Text
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11. CMF608-a novel mechanical strain-induced bone-specific protein expressed in early osteochondroprogenitor cells.
- Author
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Segev O, Samach A, Faerman A, Kalinski H, Beiman M, Gelfand A, Turam H, Boguslavsky S, Moshayov A, Gottlieb H, Kazanov E, Nevo Z, Robinson D, Skaliter R, Einat P, Binderman I, and Feinstein E
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- Amino Acid Sequence, Animals, Base Sequence, Blotting, Northern, Blotting, Western, Cells, Cultured, Fractures, Bone genetics, Humans, In Situ Hybridization, Molecular Sequence Data, Oligonucleotide Array Sequence Analysis, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Skull physiology, Stress, Mechanical, Up-Regulation, Bone and Bones physiology, Chondrocytes physiology, Osteocytes physiology, Protein Biosynthesis, Stem Cells physiology
- Abstract
Microarray gene expression analysis was utilized to identify genes upregulated in primary rat calvaria cultures in response to mechanical force. One of the identified genes designated CMF608 appeared to be novel. The corresponding full-length cDNA was cloned and characterized in more details. It encodes a putative 2597 amino acid protein containing N-terminal signal peptide, six leucine-rich repeats (LRRs), and 12 immunoglobulin-like repeats, 10 of which are clustered within the C-terminus. Expression of CMF608 is bone-specific and the main type of CMF608-positive cells is mesenchymal osteochondroprogenitors with fibroblast-like morphology. These cells reside in the perichondral fibrous ring of La Croix, periosteum, endosteum of normal bone as well as in the activated periosteum and early fibrous callus generated postfracture. Expression of CMF608 is notably absent from the regions of endochondral ossification. Mature bone cell types do not produce CMF608 with the exception of chondrocytes of the tangential layer of the articular cartilage, which are thought to be under constant mechanical loading. Ectopic expression of CMF608 in HEK293T cells shows that the protein is subjected to post-translational processing and its N-terminal approximately 90 kDa polypeptide can be found in the conditioned medium. Ectopic expression of either the full-length cDNA of CMF608 or of its N-terminal region in CMF608-negative ROS17/2.8 rat osteosarcoma cells results in transfected clones displaying increased proliferation rate and the characteristics of less-differentiated osteoblasts compared to the control cells. Our data indicate that CMF608 is a unique marker of early osteochondroprogenitor cells. We propose that it could be functionally involved in maintenance of the osteochondroprogenitor cells pool and its down-regulation precedes terminal differentiation.
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- 2004
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12. Identification of a novel stress-responsive gene Hi95 involved in regulation of cell viability.
- Author
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Budanov AV, Shoshani T, Faerman A, Zelin E, Kamer I, Kalinski H, Gorodin S, Fishman A, Chajut A, Einat P, Skaliter R, Gudkov AV, Chumakov PM, and Feinstein E
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- Amino Acid Sequence, Animals, Antineoplastic Agents pharmacology, Base Sequence, Blotting, Northern, Blotting, Western, Brain Neoplasms metabolism, Brain Neoplasms pathology, Breast Neoplasms genetics, Breast Neoplasms metabolism, Breast Neoplasms pathology, Cell Division, Cell Survival, Cloning, Molecular, DNA Primers chemistry, Doxorubicin pharmacology, Glioma metabolism, Glioma pathology, Humans, Hydrogen Peroxide pharmacology, Hypoxia metabolism, In Situ Nick-End Labeling, Mice, Mice, Nude, Molecular Sequence Data, Oligonucleotide Array Sequence Analysis, RNA, Messenger metabolism, Rats, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Tumor Cells, Cultured, Tumor Suppressor Protein p53 genetics, Tumor Suppressor Protein p53 metabolism, Brain Neoplasms genetics, Glioma genetics, Nuclear Proteins genetics, Nuclear Proteins metabolism
- Abstract
cDNA microarray hybridization was used in an attempt to identify novel genes participating in cellular responses to prolonged hypoxia. One of the identified novel genes, designated Hi95 shared significant homology to a p53-regulated GADD family member PA26. In addition to its induction in response to prolonged hypoxia, the increased Hi95 transcription was observed following DNA damage or oxidative stress, but not following hyperthermia or serum starvation. Whereas induction of Hi95 by prolonged hypoxia or by oxidative stress is most likely p53-independent, its induction in response to DNA damaging treatments (gamma- or UV-irradiation, or doxorubicin) occurs in a p53-dependent manner. Overexpression of Hi95 full-length cDNA was found toxic for many types of cultured cells directly leading either to their apoptotic death or to sensitization to serum starvation and DNA damaging treatments. Unexpectedly, conditional overexpression of the Hi95 cDNA in MCF7-tet-off cells resulted in their protection against cell death induced by hypoxia/glucose deprivation or H(2)O(2). Thus, Hi95 gene seems to be involved in complex regulation of cell viability in response to different stress conditions.
- Published
- 2002
- Full Text
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13. Identification of a novel hypoxia-inducible factor 1-responsive gene, RTP801, involved in apoptosis.
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Shoshani T, Faerman A, Mett I, Zelin E, Tenne T, Gorodin S, Moshel Y, Elbaz S, Budanov A, Chajut A, Kalinski H, Kamer I, Rozen A, Mor O, Keshet E, Leshkowitz D, Einat P, Skaliter R, and Feinstein E
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- Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Apoptosis drug effects, Base Sequence, Cell Differentiation, Cloning, Molecular, DNA-Binding Proteins chemistry, Humans, Hydrogen Peroxide pharmacology, Hypoxia genetics, Hypoxia-Inducible Factor 1, Hypoxia-Inducible Factor 1, alpha Subunit, In Situ Hybridization, Liposomes metabolism, Lung cytology, Lung drug effects, Lung metabolism, Mice, Molecular Sequence Data, PC12 Cells, RNA, Messenger genetics, RNA, Messenger metabolism, Rats, Reactive Oxygen Species metabolism, Repressor Proteins, Sequence Homology, Amino Acid, Stroke genetics, Transcription Factors chemistry, Tumor Cells, Cultured, Up-Regulation, Apoptosis genetics, DNA-Binding Proteins genetics, DNA-Binding Proteins metabolism, Gene Expression Regulation, Nuclear Proteins metabolism, Transcription Factors genetics, Transcription Factors metabolism
- Abstract
Hypoxia is an important factor that elicits numerous physiological and pathological responses. One of the major gene expression programs triggered by hypoxia is mediated through hypoxia-responsive transcription factor hypoxia-inducible factor 1 (HIF-1). Here, we report the identification and cloning of a novel HIF-1-responsive gene, designated RTP801. Its strong up-regulation by hypoxia was detected both in vitro and in vivo in an animal model of ischemic stroke. When induced from a tetracycline-repressible promoter, RTP801 protected MCF7 and PC12 cells from hypoxia in glucose-free medium and from H(2)O(2)-triggered apoptosis via a dramatic reduction in the generation of reactive oxygen species. However, expression of RTP801 appeared toxic for nondividing neuron-like PC12 cells and increased their sensitivity to ischemic injury and oxidative stress. Liposomal delivery of RTP801 cDNA to mouse lungs also resulted in massive cell death. Thus, the biological effect of RTP801 overexpression depends on the cell context and may be either protecting or detrimental for cells under conditions of oxidative or ischemic stresses. Altogether, the data suggest a complex type of involvement of RTP801 in the pathogenesis of ischemic diseases.
- Published
- 2002
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14. Possible interaction between USH1B and USH3 gene products as implied by apparent digenic deafness inheritance.
- Author
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Adato A, Kalinski H, Weil D, Chaib H, Korostishevsky M, and Bonne-Tamir B
- Subjects
- Dyneins, Female, Genes, Recessive, Genetic Markers, Humans, Male, Myosin VIIa, Myosins physiology, Pedigree, Polymorphism, Genetic, Syndrome, Hearing Loss, Sensorineural genetics, Myosins genetics
- Published
- 1999
- Full Text
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15. Characterization of cDNAs species encoding the Tat protein of caprine arthritis encephalitis virus.
- Author
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Kalinski H, Mashiah P, Rotem D, Orzech Y, Sherman L, Miki T, Yaniv A, Gazit A, and Tronick SR
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- Amino Acid Sequence, Animals, Base Sequence, Cell Line, DNA, Complementary chemistry, Gene Products, tat chemistry, Molecular Sequence Data, Open Reading Frames, Repetitive Sequences, Nucleic Acid, Transcriptional Activation, Arthritis-Encephalitis Virus, Caprine genetics, DNA, Complementary isolation & purification, Gene Products, tat genetics, Genes, Viral
- Abstract
Two distinct species of caprine arthritis encephalitis virus (CAEV) tat cDNAs were isolated early after infection of a Himalayan tahr cell line. Sequence analyses predicted that one cDNA (pCEV/e1) represented a polycistronic transcript that encodes Tat and Rev as well as an N-terminally truncated transmembrane protein and a protein, designated X, whose function is unknown; whereas the other cDNA (pCEV/f1) encodes Tat and the env gene products. pCEV/e1 trans-activated a CAEV LTR-chloramphenicol acetyltransferase reporter gene in goat synovial membrane cells. This activity was shown to be encoded by the Tat open reading frame by analysis of a deletion mutant. Because the pCAEV/f1 insert was unstable in plasmid form, its Tat activity could not be convincingly demonstrated. The target sequences for Tat within the CAEV LTR were localized to the U3 region which, when placed in either orientation upstream of heterologous promoters, was able to confer responsiveness to Tat.
- Published
- 1994
- Full Text
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16. rev-like transcripts of caprine arthritis encephalitis virus.
- Author
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Kalinski H, Yaniv A, Mashiah P, Miki T, Tronick SR, and Gazit A
- Subjects
- Amino Acid Sequence, Base Sequence, Blotting, Northern, Cell Line, DNA, Viral, Molecular Sequence Data, Nucleic Acid Conformation, Sequence Alignment, Transcription, Genetic, Arthritis-Encephalitis Virus, Caprine genetics, Genes, rev, RNA, Messenger genetics, RNA, Viral genetics
- Abstract
The pattern of expression of the caprine arthritis encephalitis virus genome (CAEV) in acutely infected tahr lung cells was found to be complex and temporally regulated. Employing Northern analysis, five CAEV-specific transcripts, 9, 6.5, 5.0, 2.5, and 1.4 kb, were detected. Nucleotide sequence analysis established the genetic structure of two species of cDNA, isolated from a library of CAEV-infected tahr cells, and suggested that they represent rev-like transcripts. One of these cDNA species was composed of three exons--the leader, an exon derived from the 5' region of env, and an exon which spanned the 3' orf. The second cDNA species consisted of four exons--three of which were identical with those of the former species. The additional exon (the second) was located at the 3' end of pol. These transcripts could potentially encode three proteins--a Rev-like protein, which is a fusion of 38 amino acids derived from the N-terminus of env and 91 residues from the 3' orf; a truncated form of the env transmembrane protein, and a novel protein, designated X composed of 73 amino acids. Thus, CAEV, like other lentiviruses, displays a complex pattern of gene expression, characterized by alternative splicing and the production of potentially polycistronic transcripts.
- Published
- 1991
- Full Text
- View/download PDF
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