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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/11/05 00:22:38」(JST)
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Similar to the cytoplasm of a cell, the nucleus contains 'nucleoplasm' (nucleus sap) or karyoplasm. The nucleoplasm is one of the types of protoplasm, and it is enveloped by the nuclear membrane or nuclear envelope. The nucleoplasm is a highly viscous liquid that includes the chromosomes and nucleoli. Many substances such as nucleotides (necessary for purposes such as the replication of DNA) and enzymes (which direct activities that take place in the nucleus) are dissolved in the nucleoplasm. The soluble, liquid portion of the nucleoplasm is called the nucleosol or nuclear hyaloplasm.
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Structures of the cell nucleus / nuclear protein
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Envelope (membrane)/
nuclear lamina |
- Pore complex:
- Nucleoporin
- NUP35
- NUP37
- NUP43
- NUP50
- NUP54
- NUP62
- NUP85
- NUP88
- NUP93
- NUP98
- NUP107
- NUP133
- NUP153
- NUP155
- NUP160
- NUP188
- NUP205
- NUP210
- NUP214
- AAAS
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Nucleolus |
- Cajal (coiled) body
- GEMIN4
- GEMIN5
- GEMIN6
- GEMIN7
- GEMIN8
- SMN/SIP1
- COIL
- Perinucleolar compartment
- TCOF
- ATXN7
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Other |
- Chromatin
- Dot (PML body)
- Paraspeckle
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SMC protein: |
- Cohesin
- Condensin
- NCAPD2
- NCAPD3
- NCAPG
- NCAPG2
- NCAPH
- NCAPH2
- SMC2
- SMC4
- DNA repair
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Transition nuclear protein: |
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- Nuclear matrix (Nucleoskeleton)
- Nucleoplasm
- Nucleosol
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- see also transcription factors and intracellular receptors
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see also nucleus diseases
Index of cells
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Description |
- Structure
- Organelles
- peroxisome
- cytoskeleton
- centrosome
- epithelia
- cilia
- mitochondria
- Membranes
- Membrane transport
- ion channels
- vesicular transport
- solute carrier
- ABC transporters
- ATPase
- oxidoreduction-driven
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Disease |
- Structural
- peroxisome
- cytoskeleton
- cilia
- mitochondria
- nucleus
- scleroprotein
- Membrane
- channelopathy
- solute carrier
- ATPase
- ABC transporters
- other
- extracellular ligands
- cell surface receptors
- intracellular signalling
- Vesicular transport
- Pore-forming toxins
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English Journal
- Identification of the PKR Nuclear Interactome Reveals Roles in Ribosome Biogenesis, mRNA Processing and Cell Division.
- Blalock WL1, Piazzi M, Bavelloni A, Raffini M, Faenza I, D'Angelo A, Cocco L.Author information 1CNR-NationalResearch Council of Italy, Institute of Molecular Genetics, Bologna, Italy; SC Laboratory of Musculoskeletal Cell Biology, Rizzoli Orthopedic Institute, Bologna, Italy.AbstractThe double-strand RNA-dependent protein kinase, PKR, plays a central role in inflammatory/chronic stress-mediated pathologies such as cancer, diabetes, and neuro/muscular degenerative diseases. Although a significant amount of research has been conducted to elucidate the role of PKR signaling in the cytosol, only recently has attention been paid to the role of PKR in the nuclear compartment. Previously our group reported that phosphorylated forms of PKR are present in the nucleus of acute leukemic cell lines, representing a reservoir of active kinase that responds to stress. Using the CCRF-CEM acute T-cell leukemia cell line, a PKR-specific inhibitor, co-immunoprecipitation and a proteomics approach, which included affinity purified mass spectrometry analysis (AP/MS), we identified the proteins present in active and inactive PKR nuclear complexes. Of the proteins identified in the PKR complexes, sixty-nine (69) were specific to the active complex, while thirty-eight (38) were specific to the inactive complex. An additional thirteen (13) proteins associated specifically with both complexes. The majority of the proteins identified are involved in, ribosome biogenesis, RNA splicing, mRNA stability, gene expression, cell cycle, or chromatin organization, including several with known significance to normal hematopoiesis and/or hematological disease. In agreement with the AP/MS data, basal- or over-expression of PKR under normal growth conditions favored cell proliferation in the tested cell lines, whereas pharmacological inhibition of PKR or shRNA-mediated knock-down did not. PKR was also found to influence the isoform and the level of expression of the proto-oncogene MYC. J. Cell. Physiol. 229: 1047-1060, 2014. © 2013 Wiley Periodicals, Inc.
- Journal of cellular physiology.J Cell Physiol.2014 Aug;229(8):1047-60. doi: 10.1002/jcp.24529.
- The double-strand RNA-dependent protein kinase, PKR, plays a central role in inflammatory/chronic stress-mediated pathologies such as cancer, diabetes, and neuro/muscular degenerative diseases. Although a significant amount of research has been conducted to elucidate the role of PKR signaling in the
- PMID 24347309
- Krüppel-Like Factor 4 Regulates Blood-Tumor Barrier Permeability via ZO-1, Occludin and Claudin-5.
- Ma J1, Wang P, Liu Y, Zhao L, Li Z, Xue Y.Author information 1Department of Neurobiology, College of Basic Medicine, China Medical University, Shenyang, People's Republic of China; Institute of Pathology and Pathophysiology, China Medical University, Shenyang, People's Republic of China.AbstractBlood-tumor barrier (BTB) constitutes an efficient organization of tight junctions which significantly reduce permeability for chemotherapy drugs. Krüppel-like factor 4 (KLF4), a member of the Krüppel-like family, has been documented in endothelial cells and may serve as an essential regulator of endothelial barrier function. However, our knowledge about the expression and function of KLF4 in the endothelial cells of BTB still remains unclear. In this study, we sought to investigate the role of KLF4 in regulation of BTB function as well as the potential molecular mechanisms. Quantitative RT-PCR, Western blot, and immunofluorescence assays demonstrated that KLF4 was down-regulated in the glioma endothelial cells (GECs) which were obtained through endothelial cells co-cultured with glioma cells. Short hairpin RNA targeting KLF4 impaired the integrity of BTB detected by trans-endothelial electric resistance assay, and meanwhile reduced the expression of ZO-1, occludin and claudin-5, demonstrated by quantitative RT-PCR, Western blot, and immunofluorescence assays. Depletion of KLF4 increased BTB permeability to small molecules detected by permeability assays. Furthermore, luciferase assays and chromatin immunoprecipitation assays showed that KLF4 up-regulated the promoter activities and interacted with "CACCC" DNA sequence presented in the promoters of ZO-1, occludin, and claudin-5. GATA-1, GATA-6, Sp1, and Sp3 factors participated in KLF4 regulation of promoter activities through binding to the promoters of tight junctions related proteins. Collectively, our results indicated that KLF4 is a key transcriptional regulator of BTB function by regulating expressions of tight junction related proteins, which would draw growing attention to KLF4 as a potential target for glioma therapy. J. Cell. Physiol. 229: 916-926, 2014. © 2013 Wiley Periodicals, Inc.
- Journal of cellular physiology.J Cell Physiol.2014 Jul;229(7):916-26. doi: 10.1002/jcp.24523.
- Blood-tumor barrier (BTB) constitutes an efficient organization of tight junctions which significantly reduce permeability for chemotherapy drugs. Krüppel-like factor 4 (KLF4), a member of the Krüppel-like family, has been documented in endothelial cells and may serve as an essential regulator of
- PMID 24318462
- Epigenetics and ocular diseases: from basic biology to clinical study.
- Yan B1, Yao J, Tao ZF, Jiang Q.Author information 1Eye Hospital, Nanjing Medical University, Nanjing, China.AbstractEpigenetics is an emerging field in ophthalmology and has opened a new avenue for understanding ocular development and ocular diseases related to aging and environment. Epigenetic mechanisms, including DNA methylation, histone modifications, chromatin remodeling, and deployment of non-coding RNAs, result in the heritable silencing of gene expression without any change in DNA sequence. Accumulating evidence suggests a potential link between gene expression, chromatin structure, non-coding RNAs, and cellular differentiation during ocular development. Disruption of the balance of epigenetic networks could become the etiology of several ocular diseases. Here, we summarized the current knowledge about epigenetic regulatory mechanisms in ocular development and diseases. J. Cell. Physiol. 229: 825-833, 2014. © 2013 Wiley Periodicals, Inc.
- Journal of cellular physiology.J Cell Physiol.2014 Jul;229(7):825-33. doi: 10.1002/jcp.24522.
- Epigenetics is an emerging field in ophthalmology and has opened a new avenue for understanding ocular development and ocular diseases related to aging and environment. Epigenetic mechanisms, including DNA methylation, histone modifications, chromatin remodeling, and deployment of non-coding RNAs, r
- PMID 24318407
Japanese Journal
- KARYOPLASM DIFFUSION DURING GERMINAL VESICLE BREAKDOWN IN STARFISH OOCYTES PROCEEDS IN TWO PHASES(Developmental Biology,Abstracts of papers presented at the 74^<th> Annual Meeting of the Zoological Society of Japan)
- Yokoi Jun-ya,Yamamoto Kenya,Sakai Takeru,Kani Satomi
- Zoological science 20(12), 1553, 2003-12-25
- NAID 110006166652
- Analysis of the Germinal Vesicle Requirement for the Activation of MPF in Maturation of Porcine Oocytes.
- , , , , ,
- Journal of Mammalian Ova Research 16(3), 130-134, 1999
- … These results indicate that the presence of GV is not required for normal protein synthesis during porcine oocyte maturation and that the generally suggested nucleus-cytoplasmic interactions, cyclin B movement into GV and the mixing of karyoplasm with cytoplasm, are not required for the MPF activation. …
- NAID 130004436622
- Plakophilins 2a and 2b : constitutive proteins of dual location in the karyoplasm and the desmosomal plaque
Related Links
- karyoplasm [-plaz′əm] noun nucleoplasm Origin: karyo- + plasm Related Forms: karyoplasmic adjective Webster's New World College Dictionary Copyright © 2010 by Wiley Publishing, Inc., Cleveland, Ohio. Used by ...
- karyoplasm / ˈkær i əˌplæz əm / Show Spelled [kar-ee-uh-plaz-uh m] Show IPA noun Cell Biology. nucleoplasm. Origin: karyo-+ -plasm Related forms karyoplasmic, karyoplasmatic / ˌkær i oʊ plæzˈmæt ɪk / Show Spelled [kar-ee ...
Related Pictures
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- 関
- karyoplasm、nucleoplasm