Protein Aggregation in the Cell Nucleus: Structure, Function and Topology~!2009-04-10~!2009-06-05~!2010-01-02~!

2010 ◽  
Vol 2 (2) ◽  
pp. 193-199 ◽  
Author(s):  
Anna von Mikecz
Keyword(s):  
Protein Aggregation ◽  
Structure Function ◽  
Cell Nucleus ◽  
And Topology ◽  
Nucleus Structure

The Nucleus: Structure, Function, and Dynamics

1987 ◽  
Vol 56 (1) ◽  
pp. 535-565 ◽  
Author(s):  
J W Newport ◽  
D J Forbes
Keyword(s):  
Structure Function ◽  
Nucleus Structure

scholarly journals The Discovery and History of Animal and Human Physiology

2020 ◽  
Vol 1 (6) ◽  
pp. 19-27
Author(s):  
Guirad Oth ◽  
Yrick John
Keyword(s):  
Endoplasmic Reticulum ◽  
Human Physiology ◽  
Cell Nucleus ◽  
Membrane System ◽  
Eukaryotic Cells ◽  
History Of ◽  
Nucleus Structure

This study discusses Nucleus, history of the discovery of the cell nucleus Structure and parts of the cell nucleus. All of them is the phisiology of animal and human. The cell nucleus (nucleus) can be defined as an organelle found in eukaryotic cells. Nucleoplasm The nucleoplasm is the liquid that is in the nucleus which is thick and transparent. The cell nucleus has many genes from DNA which are arranged and form structures called chromosomes. The endoplasmic reticulum consists of tubules, vesicles and flattened pockets that occupy the cytoplasmic space. The endoplasmic reticulum is a part of the cell that consists of a membrane system, which has a structure that resembles a multi-layered sac. These sacs are called cisternae.

scholarly journals Amyloid domains in the cell nucleus controlled by nucleoskeletal protein lamin B1 reveal a new pathway of mercury neurotoxicity

2015 ◽  
Author(s):  
Florian Arnhold ◽  
Karl-Heinz Guehrs ◽  
Anna von Mikecz
Keyword(s):  
Protein Aggregation ◽  
Cell Nucleus ◽  
Ubiquitin Proteasome System ◽  
Confocal Imaging ◽  
Future Research ◽  
Organic Chemical ◽  
Protein Homeostasis ◽  
Lamin B1 ◽  
Neuronal Signalling ◽  
Amyloid Fibrillation

Mercury (Hg) is a bioaccumulating trace metal that globally circulates the atmosphere and waters in its elemental, inorganic and organic chemical forms. While Hg represents a notorious neurotoxicant, the underlying cellular pathways are insufficiently understood. We identify amyloid protein aggregation in the cell nucleus as a novel pathway of Hg-bio-interactions. By mass spectrometry of purified protein aggregates a subset of spliceosomal components and nucleoskeletal protein lamin B1 were detected as constituent parts of an Hg-induced nuclear aggregome network. The aggregome network was located by confocal imaging of amyloid-specific antibodies and dyes to amyloid cores within splicing-speckles that additionally recruit components of the ubiquitin-proteasome system. Hg significantly enhances global proteasomal activity in the nucleus suggesting that formation of amyloid speckles plays a role in maintenance of protein homeostasis. RNAi knock down showed that lamin B1 for its part regulates amyloid speckle formation and thus likewise participates in nuclear protein homeostasis. As the Hg-induced cascade of interactions between the nucleoskeleton and protein homeostasis reduces neuronal signalling, amyloid fibrillation in the cell nucleus is introduced as a feature of Hg-neurotoxicity that opens new avenues of future research. Similar to protein aggregation events in the cytoplasm that are controlled by the cytoskeleton, amyloid fibrillation of nuclear proteins may be driven by the nucleoskeleton.

scholarly journals Amyloid domains in the cell nucleus controlled by nucleoskeletal protein lamin B1 reveal a new pathway of mercury neurotoxicity

2015 ◽  
Author(s):  
Florian Arnhold ◽  
Karl-Heinz Guehrs ◽  
Anna von Mikecz
Keyword(s):  
Protein Aggregation ◽  
Cell Nucleus ◽  
Ubiquitin Proteasome System ◽  
Confocal Imaging ◽  
Future Research ◽  
Organic Chemical ◽  
Protein Homeostasis ◽  
Lamin B1 ◽  
Neuronal Signalling ◽  
Amyloid Fibrillation

Mercury (Hg) is a bioaccumulating trace metal that globally circulates the atmosphere and waters in its elemental, inorganic and organic chemical forms. While Hg represents a notorious neurotoxicant, the underlying cellular pathways are insufficiently understood. We identify amyloid protein aggregation in the cell nucleus as a novel pathway of Hg-bio-interactions. By mass spectrometry of purified protein aggregates a subset of spliceosomal components and nucleoskeletal protein lamin B1 were detected as constituent parts of an Hg-induced nuclear aggregome network. The aggregome network was located by confocal imaging of amyloid-specific antibodies and dyes to amyloid cores within splicing-speckles that additionally recruit components of the ubiquitin-proteasome system. Hg significantly enhances global proteasomal activity in the nucleus suggesting that formation of amyloid speckles plays a role in maintenance of protein homeostasis. RNAi knock down showed that lamin B1 for its part regulates amyloid speckle formation and thus likewise participates in nuclear protein homeostasis. As the Hg-induced cascade of interactions between the nucleoskeleton and protein homeostasis reduces neuronal signalling, amyloid fibrillation in the cell nucleus is introduced as a feature of Hg-neurotoxicity that opens new avenues of future research. Similar to protein aggregation events in the cytoplasm that are controlled by the cytoskeleton, amyloid fibrillation of nuclear proteins may be driven by the nucleoskeleton.

scholarly journals Protein Aggregation in the Cell Nucleus: Structure, Function and Topology

2009 ◽  
Vol 2 (1) ◽  
pp. 193-199 ◽  
Author(s):  
Anna von Mikecz
Keyword(s):  
Protein Aggregation ◽  
Control Unit ◽  
Ubiquitin Proteasome System ◽  
Nuclear Bodies ◽  
Dna And Rna ◽  
Ribonucleoprotein Complexes ◽  
Ubiquitin Proteasome ◽  
Nucleus Structure ◽  
Cellular Control ◽  
Nuclear Processes

The nucleus represents a cellular control unit that regulates all events concerning the storage and processing of DNA and RNA. It is organized by highly crowded, dynamic assemblies of proteins and nucleic acids in molecular machines, ribonucleoprotein complexes, clusters of ongoing nuclear processes, nuclear bodies, and chromatin. This review discusses the occurrence of nuclear protein aggregation with special emphasis on the functional architecture of the nucleus, and quality control by the ubiquitin-proteasome system.

An Ultra-Structural Study of Human Melanoma in Vivo and Vitro

1976 ◽  
Vol 34 ◽  
pp. 258-259
Author(s):  
James R. Gaylor ◽  
Fredda Schafer ◽  
Robert E. Nordquist
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Protein Aggregation ◽  
Structural Study ◽  
Human Melanoma ◽  
Protein Matrix ◽  
Early Form ◽  
Endoplasmic Reticulum Protein ◽  
Mitochondrial Origin

Several theories on the origin of the melanosome exist. These include the Golgi origin theory, in which a tyrosinase-rich protein is "packaged" by the Golgi apparatus, thus forming the early form of the melanosome. A second theory postulates a mitochondrial origin of melanosomes. Its author contends that the melanosome is a modified mitochondria which acquires melanin during its development. A third theory states that a pre-melanosome is formed in the smooth or rough endoplasmic reticulum. Protein aggregation is suggested by one author as a possible source of the melanosome. This fourth theory postulates that the melanosome originates when the protein products of several genetic loci aggregate in the cytoplasm of the melanocyte. It is this protein matrix on which the melanin is deposited. It was with these theories in mind that this project was undertaken.

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