Showing posts sorted by relevance for query Glutamic Acid. Sort by date Show all posts
Showing posts sorted by relevance for query Glutamic Acid. Sort by date Show all posts

Wednesday, September 16, 2026

Glutamic Acid Helps Fresh-Cut Potatoes Stay Fresh by Silencing Browning Genes | Newswise

In continuation of my update on Glutamic acid 

The study identified a transcriptional regulatory module, StbZIP53-like2–StERF091, that suppresses the activity of key polyphenol oxidase genes linked to browning. By showing how glutamic acid activates this gene-control system, the work provides a clearer molecular basis for safer anti-browning strategies and may support the future development of quality-preserving treatments for fresh-cut potato products and other minimally processed vegetables.





Fresh-cut potatoes are increasingly popular because they fit modern food habits, but their shelf life is limited by rapid enzymatic browning after cutting. Existing methods to control browning include chemical, physical, and biological approaches, yet each has drawbacks. Some chemicals raise food-safety concerns, while physical treatments may cause off-flavors, and many biological methods are still difficult to commercialize. Earlier work had already shown that glutamic acid could reduce browning in fresh-cut potatoes, but the molecular mechanism remained unclear. That unresolved question made it necessary to investigate how glutamic acid regulates browning-related genes and upstream transcription factors in fresh-cut potato tissue.

A study (DOI:10.48130/ph-0026-0004) published in Plant Hormones on 20 March 2026 by Jingying Shi’s & Zunyang Song’s team, Shandong Agricultural University, demonstrates that glutamic acid-induced StbZIP53-like2 and StERF091 form a cooperative regulatory module that represses StPPO2 and StPPO3, thereby alleviating browning in fresh-cut potatoes.

The team first prepared fresh-cut potato shreds and compared untreated samples with samples immersed in a glutamic acid solution, then stored them at 4 °C and collected tissues across multiple time points. They measured ethylene production, performed RNA-seq and RT-qPCR analyses, and screened for transcription factors whose expression changed under glutamic acid treatment. Among 11 bZIP genes detected, StbZIP53-like2 stood out because its expression was strongly induced by glutamic acid. Subcellular localization assays showed that this protein is localized in the nucleus, consistent with its proposed role as a transcription factor. The researchers then examined whether StbZIP53-like2 directly controlled known browning-associated genes. Dual-luciferase assays showed that it repressed the promoter activity of StPPO3, while EMSA and yeast one-hybrid experiments confirmed direct binding to the C-box motif in the StPPO3 promoter. To identify interacting partners, the team screened a cDNA library and found StERF091, another glutamic acid-induced transcription factor. Yeast two-hybrid, GST pull-down, and co-immunoprecipitation assays together demonstrated that StbZIP53-like2 physically interacts with StERF091 both in vitro and in vivo. Like StbZIP53-like2, StERF091 was also localized in the nucleus. Next, the group tested the function of StERF091 in regulating browning genes. They found that StERF091 repressed the promoter activities of StPPO2 and StPPO3, but not StPPO7. EMSA and yeast one-hybrid assays further showed that StERF091 directly binds the GCC-box motifs in the StPPO2 and StPPO3 promoters. Most importantly, co-expression assays revealed that when StbZIP53-like2 and StERF091 acted together, repression of StPPO2 and StPPO3 became stronger than with either factor alone. This demonstrated that the two proteins form a functional inhibitory module that amplifies the anti-browning response triggered by glutamic acid.

Overall, the study shows that glutamic acid alleviates the browning of fresh-cut potatoes by inducing two transcriptional repressors, StbZIP53-like2 and StERF091, which cooperate to suppress StPPO2 and StPPO3. The findings move beyond a simple observation that glutamic acid works and explain why it works at the molecular level. This insight may help guide future preservation technologies aimed at extending the shelf life, visual quality, and commercial value of fresh-cut produce.


https://en.wikipedia.org/wiki/Glutamic_acid


Friday, August 24, 2012

Reformulated Copaxone Meets Goals........

Teva Pharmaceutical Industries Ltd. said that a new version of its multiple sclerosis drug Copaxone met its goals in a late-stage clinical trial.....

We know that, COPAXONE is the brand name for glatiramer acetate (formerly known as copolymer-1). Glatiramer acetate, the active ingredient of COPAXONE (glatiramer acetate) , consists of the acetate salts of synthetic polypeptides, containing four naturally occurring amino acids: L-glutamic acid, L-alanine, L-tyrosine, and L-lysine with an average molar fraction of 0.141, 0.427, 0.095, and 0.338, respectively. The average molecular weight of glatiramer acetate is 5,000 – 9,000 daltons. Glatiramer acetate is identified by specific antibodies.

Chemically, glatiramer acetate is designated L-glutamic acid polymer with L-alanine, L-lysine and L-tyrosine, acetate (salt). Its structural formula is:

(Glu, Ala, Lys, Tyr)x•xCH3COOH
(C5H9NO4•C3H7NO2•C6H14N2O2•C9H11NO3)x•xC2H4O2
CAS - 147245-92-9

COPAXONE (glatiramer acetate) is a clear, colorless to slightly yellow, sterile, nonpyrogenic solution for subcutaneous injection. Each 1 mL of solution contains 20 mg of glatiramer acetate and 40 mg of mannitol. The pH range of the solution is approximately 5.5 to 7.0. The  biological activity of COPAXONE (glatiramer acetate) is determined by its ability to block the induction of experimental autoimmune encephalomyelitis (EAE) in mice.


Monday, January 14, 2013

Melanomas that develop resistance to vemurafenib also become addicted to the drug

Vemurafenib (marketed as Zelboraf) is a B-Raf enzyme inhibitor developed by Plexxikon (now part of the Daiichi Sankyo group) and Hoffmann–La Roche for the treatment of late-stage melanoma. The name "vemurafenib" comes from V600E mutated BRAF inhibition.
Vemurafenib received FDA approval for the treatment of late-stage melanoma on August 17, 2011,  Health Canada approval on February 15, 2012 and on February 20, 2012, the European Commission approved vemurafenib as a monotherapy for the treatment of adult patients with BRAF V600 mutation positive unresectable or metastatic melanoma, the most aggressive form of skin cancer....

Mechanism : Vemurafenib has been shown to cause programmed cell death in melanoma cell lines. Vemurafenib interrupts the B-Raf/MEK step on the B-Raf/MEK/ERK pathway if the B-Raf has the common V600E mutation.
Vemurafenib only works in melanoma patients whose cancer has a V600E BRAF mutation (that is, at amino acid position number 600 on the B-Raf protein, the normal valine is replaced by glutamic acid). About 60% of melanomas have this mutation. It also has efficacy against the rarer BRAF V600K mutation. Melanoma cells without these mutations are not inhibited by vemurafenib; the drug paradoxically stimulates normal BRAF and may promote tumor growth in such cases. 

Monday, February 18, 2013

Breakthrough in ovarian cancer: Selumetinib

In continuation  of my update on Seumetinab


We know that, Selumetinib (AZD6244) is a drug being investigated for the treatment of various types of cancer, for example non-small cell lung cancer (NSCLC). 
Mode of action : The gene BRAF is part of the MAPK/ERK pathway, a chain of proteins in cells that communicates input from growth factors. Activating mutations in the BRAF gene, primarily V600E (meaning that the amino acid valine in position 600 is replaced by glutamic acid), are associated with lower survival rates in patients with papillary thyroid cancer. Another type of mutation that leads to undue activation of this pathway occurs in the gene KRAS and is found in NSCLC. A possibility of reducing the activity of the MAPK/ERK pathway is to block the enzyme MAPK kinase (MEK), immediately downstream of BRAF, with the drug selumetinib. More specifically, selumetinib blocks the subtypes MEK1 and MEK2 of this enzyme....



The study was initially developed in 2007, with 52 patients enrolled for the Phase II clinical trial between December 2007 and November 2009. Patients were given 50 milligrams of selumetinib orally twice daily. Of those participants, eight had a measurable decrease in tumor size, seven had partial responses and 34 patients saw their tumors stabilize. The findings suggest that inhibitors of the MAPK pathway warrant further investigation in patients with low-grade ovarian cancer.

"There just aren't very good treatments for low-grade ovarian cancer, so this discovery opens up a lot of new exciting possibilities for us," Dr. Farley said. He added that Phase III of this trial is scheduled to begin in the next few weeks, with that trial to be the "definitive test" before the treatment becomes available to the general population.


Ref : http://www.thelancet.com/journals/lanonc/article/PIIS1470-2045(12)70572-7/fulltext



Breakthrough in ovarian cancer: Selumetinib