anti-Superoxide dismutase copper chaperone (CCS) Antikörper

Arabidopsis thaliana Copper Chaperone For Superoxide Dismutase (CCS) Interaktionspartner

1. Data indicate that transgenic plants expressing miR398-resistant forms of CSD1, CSD2 (zeige TGFB1 Antikörper) and CCS under the control of their native promoters are more sensitive to heat stress.

2. miR398 links expression of the three major chloroplast copper proteins, plastocyanin, CCS1 and Csd2 (zeige TGFB1 Antikörper), to copper availability.

3. CCS1 gene encodes both a cytosolic and a chloroplastic form of CCS1. miR398 directs the post-transcriptional regulation of CCS1 mRNAs by cleavage and AGO10-mediated translational repression. [CCS1]

4. Arabidopsis thaliana gene AtCCS encodes a functional homolog to yeast Ccs1p/Lys7p, a copper chaperone for SOD [AtCCS]

5. The structure and function of the CCS gene of A. thaliana, including its copper and protein binding domains, are reported.

Human Copper Chaperone For Superoxide Dismutase (CCS) Interaktionspartner

1. In addition to Atox1 (zeige ATOX1 Antikörper), the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (zeige SOD1 Antikörper) (i.e. CCS) and cytochrome c (zeige CYCS Antikörper) oxidase in mitochondria (i.e. Cox17 (zeige COX17 Antikörper)). [review]

2. Human cytoplasmic copper chaperones Atox1 (zeige ATOX1 Antikörper) and CCS exchange copper ions in vitro

3. Coexpression of hCCS (zeige HCCS Antikörper) in the presence of copper restores the correct maturation of the SOD1 (zeige SOD1 Antikörper) mutants and prevents the formation of the unstructured species, confirming that hCCS (zeige HCCS Antikörper) also acts as a molecular chaperone (zeige HSP90AA1 Antikörper).

4. CCS mRNA and protein levels in the serum are not correlated with inflammatory processes.

5. CTR1 (zeige SLC31A1 Antikörper) silencing increased the protein levels of copper chaperone ATOX1 (zeige ATOX1 Antikörper) and copper chaperone for superoxide dismutase 1 (zeige SOD1 Antikörper) (CCS-1), but decreased copper chaperone for cytochrome c (zeige CYCS Antikörper) oxidase (COX17 (zeige COX17 Antikörper)).

6. CCS1 serves as a specialized import receptor in mitochondria that facilitates the import and folding of SOD1 (zeige SOD1 Antikörper) and CCS1.

7. CCS-dependent copper acquisition and distribution largely occur at membrane interfaces and that this emerging role of the bilayer may reflect a general mechanistic aspect of cellular transition metal ion acquisition.

8. CCS-1 facilitates copper trafficking to the mitochondria, but does not affect the transfer of copper to the cytochrome c (zeige CYCS Antikörper) oxidase.

9. The CCS mutation, p.Arg163Trp, causes reduced SOD1 (zeige SOD1 Antikörper) activity and may impair other mechanisms important for normal Cu homeostasis.

10. analysis of human superoxide dismutase 1 (hSOD1 (zeige SOD1 Antikörper)) maturation through interaction with human copper chaperone for SOD1 (hCCS (zeige HCCS Antikörper))

Mouse (Murine) Copper Chaperone For Superoxide Dismutase (CCS) Interaktionspartner

1. results suggest that a SOD1 (zeige SOD1 Antikörper) supplement to healthy mice may not be necessary to modulate cell proliferation and neuroblast differentiation in the dentate gyrus

2. Small interfering RNA (siRNA) targeting CCS was introduced into metallothionein (zeige MT Antikörper)-knockout mouse fibroblasts (MT-KO cells) and their wild type cells (MT-WT cells) to reveal the interactive role of CCS with other Cu-regulating proteins.

3. CCS is necessary for the efficient incorporation of copper into SOD1 (zeige SOD1 Antikörper) in motor neurons, but it does not modify the onset and progression of motor neuron disease in SOD1 (zeige SOD1 Antikörper)-mutant mice.

4. CCS-independent activation of mammalian SOD1 (zeige SOD1 Antikörper) involves glutathione

5. Associated with copper deficiency were higher levels of Ccs in erythrocytes.

6. A mechanism determining the abundance of CCS that is competitive with the process of copper delivery to SOD1 (zeige SOD1 Antikörper) is described, revealing a unique post-translational component of intracellular copper homeostasis.

7. These results establish that CCS/G93A SOD1 (zeige SOD1 Antikörper) mice manifest an isolated complex IV deficiency which may underlie a substantial part of mutant SOD1 (zeige SOD1 Antikörper)-induced mitochondrial cytopathy.

8. Study finds that as expected, CCS over-expression promotes oxidation of a wild-type SOD1 (zeige SOD1 Antikörper) disulfide; however, in the diseased G93A/CCS mouse, there was no increased oxidation of the mutant SOD1 (zeige SOD1 Antikörper) disulfide.

9. effects of copper chaperone for SOD1 on mitochondrial dysfunction are SOD1 (zeige SOD1 Antikörper) mutation dependent and correlate with SOD1 (zeige SOD1 Antikörper) redox susceptibility