Faculty Opinions recommendation of COVID-19: Attacks the 1-Beta Chain of Hemoglobin and Captures the Porphyrin to Inhibit Human Heme Metabolism.

2020 ◽  
Author(s):  
Paul B Fisher ◽  
Luni Emdad
Keyword(s):  
Beta Chain ◽  
Heme Metabolism

scholarly journals COVID-19:Attacks the 1-Beta Chain of Hemoglobin and Captures the Porphyrin to Inhibit Human Heme Metabolism

2021 ◽  
Author(s):  
liu wenzhong ◽  
li hualan
Keyword(s):  
Binding Sites ◽  
Cell Function ◽  
Viral Infections ◽  
Immune Cell ◽  
Viral Proteins ◽  
Heme Iron ◽  
The Novel ◽  
Beta Chain ◽  
Heme Metabolism ◽  
Novel Coronavirus

The novel coronavirus pneumonia is a contagious acute respiratory disease caused by the SARS-COV-2 coronavirus. The pathogenic mechanism of the novel coronavirus is unknown, which presents a significant impediment to the patient rescue. A conserved domain search strategy was utilized in this work to determine that a large number of viral proteins could bind to hemoglobin. S could bind to extracellular hemoglobin. SARS-COV-2 virus proteins interacted with porphyrins. SARS-COV-2 viruses could synthesize heme from porphobilinogen and encode all the similar enzymes required for the process. Both E and ORF3a contained heme-binding sites. ORF3a's Arg134 and E's Cys44 were the heme-iron binding sites, respectively. ORF3a also contained homologous domains to human cytochrome C reductase and bacterial EFeB protein. The molecular docking analysis revealed that ORF3a and ORF8 proteins were shown to be capable of attacking hemoglobin's 1-beta chain, whereas ORF3a was found to be effective in capturing heme for dissociation to iron and porphyrin. Deoxyhemoglobin was more susceptible to viral attack than oxidized hemoglobin. In summary, the combination of viral proteins to porphyrins and their metal compounds would improve the ability to permeate cell membranes and generate oxygen free radicals (ROS). It may be associated with viral infections and epidemic transmission. Viral proteins regulated the production and function of NO, CO and CO2 by inhibiting the activity of hemoglobin, thereby affecting immune cell function. Viral proteins' attack on hemoglobin could result in symptoms such as respiratory distress and blood clotting, damage to numerous organs and tissues, and disruption of normal human heme metabolism.

Hemoglobin beta chain fragments in bile correspond with restoration of liver function early after liver transplantation

2007 ◽  
Vol 45 (01) ◽  
Author(s):  
CW Strey ◽  
K Zamprakou ◽  
T Beckhaus ◽  
E Oppermann ◽  
WO Bechstein
Keyword(s):  
Liver Transplantation ◽  
Liver Function ◽  
Beta Chain

Effect of cadmium chloride on some parameters of heme metabolism in rats under modulation of NO radicals level

2008 ◽  
Vol 21 (2) ◽  
pp. 243-246
Author(s):  
Pavlo Kaliman ◽  
Iryna Nikitchenko ◽  
Olga pavychenko
Keyword(s):  
Cadmium Chloride ◽  
Heme Metabolism

Identification of binding partners of CsaA - an archaeal chaperonic pro-tein of Picrophilus torridus

2020 ◽  
Vol 27 ◽  
Author(s):  
Neelja Singhal ◽  
Archana Sharma ◽  
Manisha Aswal ◽  
Nirpendra Singh ◽  
Manish Kumar ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Citrate Synthase ◽  
Elongation Factor ◽  
Trna Synthetase ◽  
Strong Interactions ◽  
Beta Chain ◽  
Protein Protein Interactions ◽  
Uncharacterized Protein ◽  
Binding Partners ◽  
Picrophilus Torridus

Background:: CsaA is among the few chaperones which are present in both bacteria and archaea, but absent in eukaryotes. There are no reports on interactome analysis of CsaA from archaea, till date. Identification of binding partners of CsaA might be helpful in understanding CsaA-associated processes in Picrophilus torridus– an extreme thermoaci-dophilic euryarchaeon. Objectives:: The present study was conducted to identify the binding partners of CsaA of P. torridus (PtCsaA). Methods:: The binding partners of PtCsaA were isolated and identified using a pull down assay and liquid chromatography-mass spectrometry (LC-MS). Results:: The results revealed twelve potential binding partners of CsaA. These were thermosome subunits (Q6KZS2 and Q6L132), nascent polypeptide-associated complex protein (Q6L1N3), elongation factor 1-alpha (Q6L202), uncharacterized protein (Q6L0Y6), citrate synthase (Q6L0M8), asparaginyl-tRNA synthetase (Q6L0M5), succinyl-CoA synthetase beta chain (Q6L0B4), pyruvate ferredoxin oxidoreductase alpha and beta chain proteins (Q6KZA7 and Q6KZA6, respectively), malate dehydrogenase (Q6L0C3) and reversed fumarylacetoacetase (Q6KZ97). Functional categorization revealed that of these, six proteins were involved in energy metabolic pathways, three were archaeal chaperones, two were involved in trans-lation and one might be a transcription regulator. STRING-based analysis of the protein-protein interactions of the experi-mental interactome revealed strong interactions among them. Conclusion:: PtCsaA might be a multifaceted protein which besides translation might also play important role in metabolic processes of P. torridus. However, further experiments investigating the binding partners of CsaA in other archaea are re-quired for a better understanding of CsaA-associated processes in archaea.

A Review on Noscapine, and its Impact on Heme Metabolism

2013 ◽  
Vol 14 (3) ◽  
pp. 351-360 ◽  
Author(s):  
Harpal Singh ◽  
Prashant Singh ◽  
Kamlesh Kumari ◽  
Ankush Chandra ◽  
Sujata K. Dass ◽  
...  
Keyword(s):  
Heme Metabolism

scholarly journals A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction.

1994 ◽  
Vol 14 (11) ◽  
pp. 7404-7413 ◽  
Author(s):  
S Takaki ◽  
H Kanazawa ◽  
M Shiiba ◽  
K Takatsu
Keyword(s):  
Signal Transduction ◽  
Protein Tyrosine Kinase ◽  
Cytoplasmic Domain ◽  
Beta Chain ◽  
Cytoplasmic Domains ◽  
Interleukin 5 ◽  
Alpha Chain ◽  
Gm Csf ◽  
Response Expression ◽  
And Function

Interleukin-5 (IL-5) regulates the production and function of B cells, eosinophils, and basophils. The IL-5 receptor (IL-5R) consists of two distinct membrane proteins, alpha and beta. The alpha chain (IL-5R alpha) is specific to IL-5. The beta chain is the common beta chain (beta c) of receptors for IL-3 and granulocyte-macrophage colony-stimulating factor (GM-CSF). The cytoplasmic domains of both alpha and beta chains are essential for signal transduction. In this study, we generated cDNAs of IL-5R alpha having various mutations in their cytoplasmic domains and examined the function of these mutants by expressing them in IL-3-dependent FDC-P1 cells. The membrane-proximal proline-rich sequence of the cytoplasmic domain of IL-5R alpha, which is conserved among the alpha chains of IL-5R, IL-3R, and GM-CSF receptor (GM-CSFR), was found to be essential for the IL-5-induced proliferative response, expression of nuclear proto-oncogenes such as c-jun, c-fos, and c-myc, and tyrosine phosphorylation of cellular proteins including JAK2 protein-tyrosine kinase. In addition, analysis using chimeric receptors which consist of the extracellular domain of IL-5R alpha and the cytoplasmic domain of beta c suggested that dimerization of the cytoplasmic domain of beta c may be an important step in activating the IL-5R complex and transducing intracellular growth signals.

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