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Where does monochlorobimane bins onto GSH? 


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Monochlorobimane (MCB) binds onto glutathione (GSH) primarily through interactions with glutathione S-transferase enzymes . Studies have shown that MCB has a high affinity for rat neutral transferases, with a Km of 2.6 microM, indicating excellent substrate reactivity. In contrast, human transferases, especially the pi isoform prevalent in human tumor cell lines, exhibit reduced affinity for MCB, with a Km of 264 microM, resulting in lower labeling efficiency at lower concentrations (<50 microM) in human cell lines. Additionally, the nuclear/cytoplasmic distribution of MCB-GSH conjugates in rat hepatocytes suggests that MCB diffuses into the nucleus and accumulates there, limiting its value in estimating GSH concentrations in the nucleus and cytoplasm.

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Monochlorobimane binds onto glutathione (GSH) primarily through interactions with different glutathione S-transferase isozymes, showing varying affinities for human and rodent enzymes.
Monochlorobimane binds onto GSH via S-glutathionylation in the developing zebrafish embryo, allowing visualization of GSH changes at a suborganism level.
Monochlorobimane (MCB) binds onto glutathione (GSH) in living cells, allowing for the assessment of cell redox status through relative GSH content and responsiveness to various factors.
Monochlorobimane binds onto GSH in the nucleus and cytosol of isolated hepatocytes, diffusing and accumulating primarily in the nucleus, affecting accurate GSH concentration estimations.
Monochlorobimane binds onto glutathione S-transferase, causing challenges in labeling GSH in certain human tumor cell lines, requiring higher dye concentrations and longer staining times for adequate staining.

Related Questions

What are the potential benefits of using GSTs as an antioxidant in patients with high blood pressure?5 answersGlutathione S-transferases (GSTs) play a crucial role as antioxidants in patients with high blood pressure. Studies have shown that hypertensive patients exhibit alterations in their antioxidant defense systems. Specifically, GSTM1 deficiency may lead to increased susceptibility to kidney disease progression due to impaired handling of oxidative stress. Furthermore, research suggests that GST gene polymorphisms are associated with oxidative stress in hypertensive individuals, with potential benefits observed from interventions like yoga. Antioxidant therapy, including compounds like alpha tocopherol and ascorbic acid, has been highlighted as important in managing hypertension-induced oxidative stress. Therefore, utilizing GSTs as antioxidants can potentially help mitigate the oxidative stress burden in hypertensive patients, offering a promising avenue for therapeutic intervention.
Please what is the relationship between intracellular cysteine and GSH ?7 answersThe relationship between intracellular cysteine and glutathione (GSH) is fundamental to cellular health and function, as evidenced by research across various biological contexts. Cysteine is a critical amino acid that serves as a precursor for the synthesis of GSH, a major intracellular antioxidant. GSH plays a central role in scavenging free radicals and detoxifying harmful substances, thereby protecting cells from oxidative stress and damage. The synthesis of GSH from cysteine is crucial for maintaining the redox balance within cells, as demonstrated in studies where the promotion of cysteine uptake leads to increased GSH synthesis, highlighting the direct relationship between cysteine availability and GSH levels. Research involving acute lymphoblastic leukemia (ALL) patients has shown significant differences in GSH levels based on the presence or absence of certain alleles, indicating that genetic factors influencing cysteine metabolism can impact GSH synthesis and, consequently, cellular antioxidant capacity. Furthermore, nutrient availability, including that of cysteine, has been shown to influence cell differentiation and the life cycle through the modulation of GSH levels, underscoring the importance of cysteine in GSH-dependent cellular processes. Experimental manipulation of GSH synthesis pathways, through either the variation of cystine supply or direct inhibition, has further elucidated the relationship between cysteine and GSH. These manipulations affect cellular processes such as the tricarboxylic acid cycle and protein secretion, demonstrating the interconnected roles of cysteine and GSH in cellular metabolism and function. Additionally, the development of fluorescent probes for detecting intracellular GSH has highlighted the significance of rapidly and sensitively monitoring GSH levels, indirectly pointing to the importance of cysteine in cellular health. The cooperative roles of cysteine and GSH in regulating cell signaling pathways, such as the mechanistic target of rapamycin complex 1 (mTORC1) and the integrated stress response (ISR), further illustrate the intertwined relationship between cysteine availability and GSH function. This cooperation is essential for the suppression of ferroptosis, a form of cell death linked to oxidative stress, thereby highlighting the protective roles of cysteine and GSH against cellular damage. Intriguingly, the chemical reactivity of certain proteins can be modulated by intracellular factors like GSH, suggesting that the cysteine-GSH axis may influence protein function and cellular conductance through redox mechanisms. The role of intracellular GSH in mitigating toxicity, as observed in studies on human hepatocytes, underscores the importance of GSH in cellular defense mechanisms, which is directly influenced by cysteine availability and metabolism. Finally, the development of probes for detecting cellular cysteine in the presence of high GSH concentrations further emphasizes the distinct yet interconnected roles of these two molecules in cellular physiology. Collectively, these studies illuminate the intricate relationship between intracellular cysteine and GSH, showcasing their pivotal roles in maintaining cellular health, metabolism, and defense against oxidative stress and toxicity.
Are GSLs in urine present on cell?5 answersGSLs (glomerular segmental lesions) in urine are present on cells. Parietal epithelial cells (PECs) and podocytes are the two types of epithelial cells in the glomerulus. PDX-positive PECs have been found to be excreted in the urine of patients with focal segmental glomerulosclerosis (FSGS). Additionally, single-cell RNA sequencing analysis of urine samples from FSGS subjects identified immune cells, predominantly monocytes, and renal epithelial cells, including podocytes. These findings suggest that GSLs in urine are associated with cellular components, such as PECs and podocytes, which are involved in the pathogenesis of FSGS.
How does GSTM affect signaling pathway?3 answersGSTM inhibits LPS-stimulated TNF-α production through the ceramide pathway and inhibits NF-κB activation.
How gstm1 relation with nfkb?5 answersGSTM1 is not mentioned in any of the provided abstracts. Therefore, there is no information available regarding the relationship between GSTM1 and NFkB in the abstracts provided.
What is the GST rate on cell phones?3 answers

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