Copper- and Zinc-Binding Protein Fractions in the Soluble Cytoplasm of Rat Tissues

1977 ◽  
Vol 5 (2) ◽  
pp. 425-427 ◽  
Author(s):  
DEREK S. NORTON ◽  
FRANK W. HEATON
Keyword(s):  
Binding Protein ◽  
Protein Fractions ◽  
Zinc Binding ◽  
Rat Tissues ◽  
Copper And Zinc

scholarly journals The Native Copper- and Zinc- Binding Protein Metallothionein Blocks Copper-Mediated Aβ Aggregation and Toxicity in Rat Cortical Neurons

PLoS ONE ◽  
2010 ◽  
Vol 5 (8) ◽  
pp. e12030 ◽  
Author(s):  
Roger S. Chung ◽  
Claire Howells ◽  
Emma D. Eaton ◽  
Lana Shabala ◽  
Kairit Zovo ◽  
...  
Keyword(s):  
Cortical Neurons ◽  
Binding Protein ◽  
Zinc Binding ◽  
Native Copper ◽  
Copper And Zinc ◽  
Aβ Aggregation ◽  
Rat Cortical Neurons

Ecl1 is a zinc-binding protein involved in the zinc-limitation-dependent extension of chronological life span in fission yeast

2017 ◽  
Vol 292 (2) ◽  
pp. 475-481 ◽  
Author(s):  
Takafumi Shimasaki ◽  
Hokuto Ohtsuka ◽  
Chikako Naito ◽  
Kenko Azuma ◽  
Takeshi Tenno ◽  
...  
Keyword(s):  
Life Span ◽  
Fission Yeast ◽  
Binding Protein ◽  
Zinc Binding ◽  
Chronological Life Span

Studies on the Appearance of a Zinc-Binding Protein in Rat Pancreas

1974 ◽  
Vol 2 (4) ◽  
pp. 654-656 ◽  
Author(s):  
NEILL T. DAVIES ◽  
IAN BREMNER
Keyword(s):  
Binding Protein ◽  
Zinc Binding ◽  
Rat Pancreas

Zinc- and copper-binding proteins in the plasma of winter flounder (Pseudopleuronectes americanus)

1980 ◽  
Vol 58 (4) ◽  
pp. 609-613 ◽  
Author(s):  
P. E. Fletcher ◽  
G. L. Fletcher
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Binding Protein ◽  
Gel Filtration ◽  
Protein S ◽  
Egg Yolk ◽  
Winter Flounder ◽  
Zinc Binding ◽  
Copper Binding ◽  
Copper Binding Proteins

Zinc- and copper-binding proteins were isolated from the plasma of winter flounder using gel filtration chromatography. A single copper-binding protein fraction of molecular weight 170 000 was isolated from the plasma of both sexes.In male and female flounder over 95% of the plasma zinc was associated with a zinc-binding protein(s) with a molecular weight of 76 000. In male flounder the remaining zinc appeared to be bound to a protein(s) of molecular weight 186 000. In female flounder the remaining 5% of the zinc was associated with two zinc-binding fractions with apparent molecular weights of 186 000 and 340 000 – 370 000.Extracts of plasma vitellogenin and egg yolk proteins revealed significant quantities of zinc and copper. It is hypothesized that the female specific zinc-binding protein (340 000 – 370 000) was vitellogenin.

Characteristics of a somatostatin-binding protein

1978 ◽  
Vol 56 (1) ◽  
pp. 48-53 ◽  
Author(s):  
N. Ogawa ◽  
T. Thompson ◽  
H. G. Friesen
Keyword(s):  
Diabetes Mellitus ◽  
Binding Protein ◽  
Gel Filtration ◽  
The Other ◽  
Rat Tissues ◽  
Cytoplasmic Protein ◽  
Disulfide Bridges ◽  
Thiol Groups ◽  
Tissue Extracts ◽  
Streptozotocin Induced Diabetes

The concentrations of a somatostatin-binding protein, found in the cytosol of a number of rat tissues, are similar in both sexes, and hypophysectomy has little or no effect on the level of binding protein in tissue extracts. On the other hand, streptozotocin-induced diabetes mellitus causes a modest decrease. The somatostatin-binding proteins obtained from extracts of several rat tissues are not only similar in molecular weight but also exhibit a similar isoelectric point and electrophoretic mobility. Agents that block thiol groups or prevent the formation of disulfide bridges markedly decrease the binding of somatostatin to the cytoplasmic protein. Studies using thiol reagents and gel filtration suggest that free thiol groups in somatostatin-binding protein are important for the binding of somatostatin.

Isolation and characterization of a new zinc-binding protein from albacore tuna plasma

Biochemistry ◽  
1987 ◽  
Vol 26 (11) ◽  
pp. 3228-3234 ◽  
Author(s):  
Bruce Dyke ◽  
Jack Hegenauer ◽  
Paul Saltman ◽  
R. Michael Laurs
Keyword(s):  
Binding Protein ◽  
Zinc Binding ◽  
Albacore Tuna ◽  
Isolation And Characterization

scholarly journals Structural basis of the zinc-induced cytoplasmic aggregation of the RNA-binding protein SFPQ

2020 ◽  
Vol 48 (6) ◽  
pp. 3356-3365 ◽  
Author(s):  
Jie Huang ◽  
Mitchell Ringuet ◽  
Andrew E Whitten ◽  
Sofia Caria ◽  
Yee Wa Lim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cortical Neurons ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Zinc Binding ◽  
Structural Basis ◽  
Rna Biogenesis ◽  
Cytoplasmic Accumulation ◽  
Nucleocytoplasmic Distribution

Abstract SFPQ is a ubiquitous nuclear RNA-binding protein implicated in many aspects of RNA biogenesis. Importantly, nuclear depletion and cytoplasmic accumulation of SFPQ has been linked to neuropathological conditions such as Alzheimer's disease (AD) and amyotrophic lateral sclerosis (ALS). Here, we describe a molecular mechanism by which SFPQ is mislocalized to the cytoplasm. We report an unexpected discovery of the infinite polymerization of SFPQ that is induced by zinc binding to the protein. The crystal structure of human SFPQ in complex with zinc at 1.94 Å resolution reveals intermolecular interactions between SFPQ molecules that are mediated by zinc. As anticipated from the crystal structure, the application of zinc to primary cortical neurons induced the cytoplasmic accumulation and aggregation of SFPQ. Mutagenesis of the three zinc-coordinating histidine residues resulted in a significant reduction in the zinc-binding affinity of SFPQ in solution and the zinc-induced cytoplasmic aggregation of SFPQ in cultured neurons. Taken together, we propose that dysregulation of zinc availability and/or localization in neuronal cells may represent a mechanism for the imbalance in the nucleocytoplasmic distribution of SFPQ, which is an emerging hallmark of neurodegenerative diseases including AD and ALS.

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