scholarly journals The structure of polyamine analogues determines haemoglobin production and cytotoxicity in murine erythroleukaemia cells

1995 ◽  
Vol 309 (3) ◽  
pp. 787-791 ◽  
Author(s):  
S Clément ◽  
J G Delcros ◽  
H S Basu ◽  
G Quash ◽  
L J Marton ◽  
...  

The naturally occurring polyamine spermine induces haemoglobin synthesis in murine erythroleukaemia (MEL) cells. We have studied the ability of various polyamine analogues to inhibit cell growth and induce haemoglobin production. Polyamine analogues with free terminal amino groups were good inducers of haemoglobin production in MEL cells. Haemoglobin levels correlated with the number of positive charges: pentamines (five positive charges) were stronger inducers than tetramines (four positive charges). Compounds ethylated at their terminal amines were poor inducers of haemoglobin production but good inhibitors of MEL cell growth. These results provide evidence that polyamine analogues support specific biological functions of polyamines in MEL cells and suggest relationships between polyamine structure and function.

2021 ◽  
Author(s):  
Meng Wang ◽  
Yonggang Ren ◽  
Shaofan Hu ◽  
Keli Liu ◽  
Lu Qiu ◽  
...  

AbstractNrf1 and Nrf2, as two principal CNC-bZIP transcription factors, regulate similar but different targets involved in a variety of biological functions for maintaining cell homeostasis and organ integrity. Of note, the unique topobiological behavior of Nrf1 makes its functions more complicated than Nrf2, because it is allowed for alternatively transcribing and selectively splicing to yield multiple isoforms (e.g., TCF11, Nrf1α). Here, to gain a better understanding of their similarities and differences in distinct regulatory profiles, four distinct cell models for stably expressing TCF11, TCF11ΔN, Nrf1α or Nrf2 have been established by an Flp-In™ T-REx™-293 system and identified by transcriptomic sequencing. Further analysis revealed that Nrf1α and TCF11 have similar yet different regulatory profiles, though both contribute basically to positive regulation of their co-targets, which are disparate from those regulated by Nrf2. Such disparity in gene regulation by Nrf1 and Nrf2 was also corroborated by scrutinizing comprehensive functional annotation of their specific and/or common target genes. Conversely, the mutant TCF11ΔN, resulting from a deletion of the N-terminal amino acids 2-156 from TCF11, resembles Nrf2 with largely consistent structure and function. Interestingly, our further experimental evidence demonstrates that TCF11 acts as a potent tumour-repressor relative to Nrf1α, albeit both isoforms possess a congruous capability to prevent tumour growth and upregulate those genes critical for improving the survival of patients with hepatocellular carcinoma.


2020 ◽  
Vol 27 (31) ◽  
pp. 5159-5174 ◽  
Author(s):  
Xinjie Lu

Background:Angiopoietin-Like Proteins (ANGPTLs) are structurally related to the angiopoietins. A total of eight ANGPTLs (from ANGPTL1 to ANGPTL8) have been identified so far. Most ANGPTLs possess multibiological functions on lipid metabolism, atherosclerosis, and cancer. Among them, ANGPTL3 has been shown to regulate the levels of Very Low-Density Lipoprotein (VLDL) made by the liver and play a crucial role in human lipoprotein metabolism.Method:A systematic appraisal of ANGPTLs was conducted, focusing on the main features of ANGPTL3 that has a significant role in atherosclerosis.Results:Angiopoietins including ANGPTL3 are vascular growth factors that are highly specific for endothelial cells, perform a variety of other regulatory activities to influence inflammation, and have been shown to possess both pro-atherosclerotic and atheroprotective effects.Conclusion:ANGPTL3 has been demonstrated as a promising target in the pharmacological management of atherosclerosis. However, many questions remain about its biological functions.


IUBMB Life ◽  
2012 ◽  
Vol 64 (4) ◽  
pp. 346-353 ◽  
Author(s):  
Alexander Vargas-Hernández ◽  
Gabriela López-Herrera ◽  
José L. Maravillas-Montero ◽  
Felipe Vences-Catalán ◽  
Dolores Mogica-Martínez ◽  
...  

Metallomics ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 23-33 ◽  
Author(s):  
Jelena Habjanič ◽  
Serge Chesnov ◽  
Oliver Zerbe ◽  
Eva Freisinger

Naturally occurring Ser/Cys variations in Pseudomonas metallothioneinss affect intra-cluster dynamics rather than binding capacity.


2019 ◽  
Vol 116 (10) ◽  
pp. 4037-4043 ◽  
Author(s):  
Maria I. Freiberger ◽  
A. Brenda Guzovsky ◽  
Peter G. Wolynes ◽  
R. Gonzalo Parra ◽  
Diego U. Ferreiro

Conflicting biological goals often meet in the specification of protein sequences for structure and function. Overall, strong energetic conflicts are minimized in folded native states according to the principle of minimal frustration, so that a sequence can spontaneously fold, but local violations of this principle open up the possibility to encode the complex energy landscapes that are required for active biological functions. We survey the local energetic frustration patterns of all protein enzymes with known structures and experimentally annotated catalytic residues. In agreement with previous hypotheses, the catalytic sites themselves are often highly frustrated regardless of the protein oligomeric state, overall topology, and enzymatic class. At the same time a secondary shell of more weakly frustrated interactions surrounds the catalytic site itself. We evaluate the conservation of these energetic signatures in various family members of major enzyme classes, showing that local frustration is evolutionarily more conserved than the primary structure itself.


Blood ◽  
1983 ◽  
Vol 62 (1) ◽  
pp. 133-140 ◽  
Author(s):  
MP Croissant ◽  
M Zuzel ◽  
JP Allain

The interference of antibodies to factor VIII coagulant protein (VIII:C) of 9 nonhemophilic patients with the binding to factor VIII coagulant antigen (VIII:CAg) of a reference hemophilic 125I-Fab' reagent, used in a liquid phase VIII:CAg assay, was studied. The binding competition was estimated from immunoradiometric assay (IRMA) dose-response slope of VIII:CAg present in patient plasma, interference of antibodies with the 125I-Fab' binding to VIII:CAg in normal plasma, and the displacement of antibody from the complexes with VIII:CAg by the 125I Fab'. Antibody populations from three patients were studied in detail; in the VIII:CAg assay, two of them interfered with the 125I- Fab' binding, and one did not (patient 1). The formation of stable complexes between antibodies of each patient and VIII:CAg was demonstrated by protein-A-Sepharose adsorption. The 125I-Fab' binding to VIII:CAg-anti-VIII:CAg IgG complexes indicated that patient 1 antibodies and the 125I-Fab' recognized different antigenic determinants, whereas the other two patient antibodies and 125I-Fab' recognized closely related or identical VIII:CAg determinants. These results demonstrate an apparently selective recognition of at least two distinct VIII:CAg determinants by naturally occurring antibodies, suggesting a possibility of a wider use of these antibodies in studies of the structure and function of factor VIII.


Biochemistry ◽  
1983 ◽  
Vol 22 (9) ◽  
pp. 2068-2076 ◽  
Author(s):  
Grazyna Faure ◽  
Jean Claude Boulain ◽  
Francoise Bouet ◽  
Therese Montenay-Garestier ◽  
Pierre Fromageot ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document