New Findings about IL-33 You May Want to Know

A team of researchers from the French Scientific Research Center and the National Institute of Health and Medical Research discovered that a protein acts like a sensor can detect asthma-inducing allergens in the respiratory tract. Their research, co-led by Corinne Cayrol and Jean-Philippe Girard, was recently published in Nature Immunology and has brought new breakthroughs in the treatment of allergic diseases.

What are the common features of mold, pollen, and wolfberry? Although they belong to three different organisms, they all can cause allergies in susceptible people. Although the composition varies greatly, they all contain enzymes called proteases.

The team found a human protein that reacts with environmental allergens: interleukin-33 (IL-33). When allergens enter the human respiratory tract, they release proteases that activate IL-33 to become extremely active. This triggers an allergic chain reaction.

At the same time, this mechanism has led to allergic reactions to various allergens. IL-33 can detect 14 different allergens, including environmental air (such as pollen, indoor aphids, fungal spores, etc.) and occupational asthma-related (like subtilisin found in detergents) allergens.

These findings are important because they find a direct relationship between genes and the environment. In fact, the gene encoding IL-33 is indeed one of the major genes that cause people to easily develop asthma. In addition, clinical trials targeting IL-33 are ongoing. Inhibiting the production of activated IL-33 after exposure to allergens may be an effective way to control severe allergic reactions in allergic patients.

Collected by Creative BioMart.

The Amaryllidaceae Alkaloid Helps Repress Cancer Cell Growth

Daffodil can quickly cure cancer? Scientists from the Laboratory of RNA Molecular Biology at the Liberal University School of Science and Cancer Research Center in Brussels, Belgium, conducted a preliminary exploration in this direction, and this study was published in Cell's Structure recently.

The study, led by Denis Lafontaine, extracted a natural anticancer compound from daffodil (Amaryllidaceae). They found that the compound is an alkaloid called tennis amine, which binds ribosomes. Ribosomes are nanodevices necessary for the survival of our cells because they synthesize all of our proteins. In order to maintain their own unrestricted growth, cancer cells rely on enhanced protein synthesis, so cancer cells are very sensitive to therapies that inhibit ribosome formation or inhibit ribosomal function.

In the new study, researchers also found that tennis amine can inhibit ribosome-forming proteins and therefore slow cancer cell growth. Peracetamol also inhibits the production of such nanodevices in the nucleus: the pressure on the nucleolus activates the anti-cancer watchdog pathway, leading to increased stability of the p53 protein, thereby eliminating cancer cells.

This study, for the first time, reveals the molecular mechanism of antitumor activity of daffodils, which has been used in folk medicine for hundreds of years. Pedigree is a member of a large group of natural therapeutic molecules: Many of the other alkaloids used in human care are extracted from plants such as morphine (potent analgesics), quinine (anti-malaria drugs), and ephedrine (anti-asthma Medicine) and so on.

In the near future, Denis Lafontaine's team will work with Veronique Mathieu's team to examine the effects of four Amaryllid alkaloids on ribosome formation and function. Their goal is to quickly find the most promising chemical framework, and then further develop anticancer drugs.

Collected by Creative BioMart.