Tag Archives: Proteins

Study: Cardamom Seed Extract Enhances Production of Antiviral Proteins

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Cardamom (Elettaria cardamom) seed extract, notably its primary bioactive element, 1,8-cineole, has been highlighted in recent research for its potential as an antiviral agent by enhancing the production of antiviral proteins known as type I interferons.

Cardamom (Elettaria cardamom) seed. Image credit: Karina Panchenko.

Herbal remedies have long been utilized to address various health conditions, including viral infections.

Medicinal herbs and plants are abundant sources of bioactive substances and have been incorporated into antiviral products by pharmaceutical companies.

These substances interfere with different stages of various viruses’ life cycles and help modulate the body’s immune response to viral threats.

Recent research by Takeshi Kawahara and his team at Shinshu University suggests that cardamom seed extract might possess formidable antiviral properties.

“Even prior to the emergence of the recent coronavirus, we were investigating substances that could help prevent viral infections in daily life,” Dr. Kawahara stated.

“The pandemic has amplified public interest in the antiviral qualities of food, providing us more avenues to pursue this research.”

In earlier investigations, the researchers discovered that cardamom seed extract effectively prevented influenza virus infections.

The latest study involved conducting experiments on human lung cells, specifically A549 cells, treated with cardamom seed extract to simulate viral infection processes and better understand its effects on the production of antiviral molecules.

They found that cardamom seed extract, along with its key bioactive component, 1,8-cineole, activates intracellular nucleic acid sensors that recognize viral DNA and RNA.

These sensors trigger the production of various cytokines, which impact the virus at different phases of infection.

In this instance, treatment with cardamom seed extract or 1,8-cineole resulted in increased production of a specific type of cytokine known as type I interferon, which is crucial for the body’s defense against viral infections, facilitated by the intracellular nucleic acid sensors.

Given these findings, the researchers expressed significant interest in the potential therapeutic applications of their results.

“Traditionally, cardamom has been widely recognized as a medicinal spice, and based on our findings, we aspire to explore its use as an antiviral agent to combat various viral infections,” Dr. Kawahara noted.

“We hope this research sheds new light on the antiviral properties of foods and inspires further exploration of various food components that may aid in preventing viral infections in everyday life.”

These findings were published in the August 2025 issue of Foods.

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Abdullah Al Sufian Shuvo et al. 2025. Type I interferon-enhancing effect of cardamom seed extract via intracellular nucleic acid sensor regulation. Foods 14(15):2744; doi: 10.3390/Food14152744

Source: www.sci.news

Cancer Cells Manipulate Immune Proteins to Evade Treatment – Sciworthy

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Cancer arises from the proliferation of abnormal, uncontrolled cells that create dense masses, known as Solid Tumors. These cancer cells possess unique surface markers called antigens that can be identified by immune cells. A crucial component of our immune system, T cells, carry a protective protein known as FASL, which aids in destroying cancer cells. When T cells encounter cancer antigens, they become activated and initiate an attack on the tumor.

One form of immunotherapy, referred to as chimeric antigen receptor T cell therapy or CAR-T therapy, involves reprogramming a patient’s T cells to recognize cancer cell antigens. However, CAR-T therapy often struggles with solid tumors due to the dense, hostile environment within these tumors, which obstructs immune cells from infiltrating and functioning effectively.

Another significant hurdle that clinicians encounter when treating solid tumors is their heterogeneous composition of various cancer cell types. Some of these cells exhibit antigens recognizable by CAR-T cells, while others do not, complicating the design of CAR-T therapies that can target all tumor cells without harming healthy cells. Solid tumors also produce the protein Plasmin, which further impairs the immune system’s ability to break down FASL and eliminate cancer cells.

Researchers from the University of California, Davis investigated whether shielding FASL from plasmin could preserve its cancer-killing capabilities and enhance the efficacy of CAR-T therapy. They found that the human FASL protein contains a unique amino acid compared to other primates, making it more susceptible to degradation by plasmin. Their observations suggested that when FASL was cleaved, it lost its ability to kill tumor cells. However, after injecting an antibody that prevents plasmin from cleaving FASL, it remained intact and preserved its cancer-killing function.

Since directly studying cell behavior in the human body poses challenges, scientists culture tumor cells and cell lines in Petri dishes under controlled laboratory environments. To gain insights into plasmin’s role, the team examined ovarian cancer cell lines obtained from patients, discovering that CAR-T resistant cancer cells exhibited high plasmin activity.

They noted that combining ovarian cancer cells with elevated plasmin levels with normal cells displaying surface FASL diminished FASL levels in the normal cells. When they added FASL-protecting antibodies, CAR-T cells effectively eliminated not only the targeted cancer cells but also nearby cancer cells lacking the specific target antigen. These findings indicated that plasmin can cleave FASL in T cells and undermine CAR-T therapy, suggesting that safeguarding FASL may enhance CAR-T treatment’s effectiveness.

To assess whether tumor-generated plasmin can deactivate human FASL in more natural settings, researchers examined its function in live tumors within an active immune system. They implanted ovarian, mammary, and colorectal tumor cell lines from mice into genetically matched mice to elicit a natural immune response. When human FASL protein was directly injected into mouse tumors, the cancer cells remained intact. In contrast, injecting a drug that inhibits plasmin resulted in cancer cell death. Additionally, administering FASL-protecting antibodies also led to the elimination of cancer cells.

As a final experiment, the team aimed to determine whether activated T cells from the mice’s immune systems could penetrate the tumors and kill cancer cells. They implanted mice with both plasmin-positive and plasmin-negative tumors, treating both with drugs to enhance immune cell activity and boost FASL production.

They discovered that in tumors with low plasmin levels, mouse immune cells expressed high amounts of FASL on their surfaces, while in tumors with elevated plasmin levels, FASL was significantly reduced. Once again, injecting FASL-protected antibodies into these tumors increased FASL levels. The researchers concluded that plasmin can diminish the immune system’s ability to eliminate cancer cells by depleting FASL from immune cells.

In summary, the team found that tumors exploit plasmin to break down the protective protein FASL, evading immune system attacks. Based on their findings, they proposed that plasmin inhibitors or FASL-protected antibodies could augment the effectiveness of immunotherapy in treating cancer.


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Source: sciworthy.com

Paleontologists Discover Ancient Proteins in Mammalian Tooth Enamel from 18 Million Years Ago

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Researchers have identified protein sequences within the dense enamel tissues of ancient nasal cavities and materials collected from the Burg and Lopelot sites in the Turkana Basin, Kenya.

The Turkana Basin within the East African lift system preserves fossil communities dating back more than 66 million years. Green et al. Powder samples were collected for paleontological skin analysis from the early Pleistocene back to the Oligocene (29 million years ago) from large herbivores. Image credit: Green et al., doi: 10.1038/s41586-025-09040-9.

“Teeth are the rocks in our mouths,” stated Dr. Daniel Green, a researcher at Harvard and Columbia University.

“They represent the most complex structures created by animals; hence, it’s possible to find teeth that are 100 million years old, offering geochemical records of animal life.”

“This includes insights into their diets, hydration, and habitats.”

“Previously, we believed that mature enamel, being the hardest part of teeth, should contain very little protein.”

Yet, by employing a novel proteomic technique known as liquid chromatography tandem mass spectrometry (LC-MS/MS), the researchers uncovered remarkable protein diversity in various biological tissues.

“The method comprises multiple stages where peptides are sorted according to size or chemistry, enabling detailed sequential analysis at unprecedented resolution,” explains Dr. Kevin Uno from Harvard and Columbia University.

“Recent findings indicate that there are dozens, potentially hundreds, of different proteins present in tooth enamel,” remarked Dr. Green.

Recognizing that many proteins exist in modern teeth, researchers pivoted towards studying fossils of nasal mesentery and related materials.

As herbivores, these creatures exhibited large teeth to crush their plant-based diets.

“These mammals could have enamels measuring 2-3 millimeters in thickness, providing ample material for investigation,” Dr. Green noted.

“Our discovery — peptide fragments and amino acid chains representing proteins spanning around 18 million years — stands to transform the field.”

“No one has previously identified peptide fragments of such antiquity.”

The oldest published findings to date date back around 3.5 million years.

“The newly identified peptides encompass a diverse array of proteins, representing what is known as the proteome,” Dr. Green remarked.

“One reason we are thrilled about these ancient teeth is that we lack a complete proteome for all proteins that could potentially be extracted from the bodies of these extinct elephants and rhinos, yet we can identify distinct groups.”

“Such collections could yield more information from these groups than from a single protein alone.”

“This research opens a new chapter for paleontology, enabling scientists to reconstruct the molecular and physiological traits of extinct species, moving beyond just bones and morphology,” stated Dr. Emmanuel Nudiemma, a researcher at the National Museum of Kenya.

“These peptide fragments can be utilized to delve into the relationships among ancient animals, much like contemporary methods that map human DNA relations.”

“Though a few animals analyzed in studies are completely extinct without living descendants, in theory, proteins could be extracted from their teeth and added to a phylogenetic tree,” Dr. Green elaborated.

“This information may clarify long-standing debates among paleontologists concerning the relationships among various mammalian lineages, utilizing molecular evidence.”

Survey results Today, I will be featured in the journal Nature.

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Dr. Green et al. Diverse enamel proteomes from rifts of East Africa over 108 million years. Nature Published online on July 9, 2025. doi:10.1038/s41586-025-09040-9

Source: www.sci.news

Ancient Enamel Proteins Uncover Biological and Genetic Diversity in Paranthropus robustus

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Paranthropus robustus is a well-documented species within the Hominin group that has yet to be associated with genetic evidence. This species thrived in what is now South Africa between 2 million and 1.2 million years ago. In a recent study, paleontologists extracted enamel protein sequences from a dental specimen, believed to be 2 million years old, discovered at the Swartkrans site in South Africa. The results indicate a greater diversity than previously recognized for Paranthropus robustus and support the potential existence of multiple species within the genus.

Paranthropus Boisei. Image credit: ©Roman Yevseyev.

Advancements in ancient DNA (aDNA) sequencing have provided essential insights into the evolutionary connections among mid- to late Pleistocene hominins. However, our understanding of the earlier Pliocene-Pleistocene species, including Paranthropus robustus, remains limited.

This limitation is primarily due to the poor preservation of aDNA in African hominin fossils older than 20,000 years.

Paranthropus robustus has traditionally been regarded as a singular evolutionary line.

Yet, morphological overlaps between Paranthropus robustus and Australopithecus raise questions about their possible evolutionary links.

Moreover, variations in dental morphology suggest either an undiscovered diversity within Paranthropus robustus or the existence of multiple distinct species.

In this study, researchers from the University of Copenhagen, the University of Cape Town, and Dr. Paresa Madupe employed more durable ancient proteins to explore the variation within this ancient human species.

Four tooth enamel proteins were analyzed using high-resolution mass spectrometry and paleontological techniques, focusing on Paranthropus robustus fossils from the Swartkrans cave.

These specimens, dating from 2.2 to 1.8 million years ago, are among the earliest known hominins.

Molecular analysis of the protein sequences revealed significant variation at the molecular level among Paranthropus robustus individuals, including evidence from both male and female fossils, challenging the reliability of tooth size as a sole indicator of sexual dimorphism and suggesting that this variance cannot be attributed exclusively to sexual differences.

Notably, one individual appears to be genetically distinct from the others, highlighting considerable intraspecies variability within Paranthropus robustus.

The results align with recent morphological evidence, indicating previously unrecognized taxonomic diversity within the genus, including the proposed species Paranthropus capensis.

“Our study illustrates how paleobiological traits can assist in distinguishing sexual dimorphism from other forms of variation in the early Pleistocene human lineage in Africa,” the authors concluded.

The study is published in the journal Science.

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Paresa P. Madupe et al. 2025. Enamel proteins reveal biological and genetic variation in southern Africa Paranthropus robustus. Science 388 (6750): 969-973; doi: 10.1126/science.adt953

Source: www.sci.news

Tiny proteins that repair tooth enamel

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Over 50% of the world’s population experiences at least one cavity in childhood, increasing to over 90% in adults. Using a fluoride gagging agent, brushing and flossing twice daily and getting fillings as needed is a standard practice to maintain good dental hygiene. Still, dentists fill more than 100 million cavities around the world each year, on average. What if there is a way to prevent it? and Reverse cavity? Dental researchers recently tested a new method of restoring the structure of teeth before major damage occurs.

Our teeth are made up of minerals made up of calcium and phosphates. When the acids and bacteria in our mouth break down these minerals, our teeth experience Demineralisation. When dechlorination drills holes in the protective layer outside the tooth, a cavity forms; enamel. If left untreated, these holes will deepen and slowly collapse over time the enamel and remaining teeth.

Brushing teeth and using mouthwash can clean acids and bacteria from the mouth to prevent the initial cavity, but dental researchers want to demineralize and therefore reverse the cavity. Tooth-like minerals line themselves up in shapes similar to snowflakes and diamonds. Crystal-like structure. They also tend to complete their own patterns by fusing firmly with the surrounding minerals. Therefore, researchers hope to use this natural process to reconstruct dental minerals into their crystal-like structures.

One way to encourage scientists to begin reconstructing teeth is to use small chains of molecules that form proteins. peptide. Scientists use a specific peptide called An Enamel-binding peptide Or EBP can help bind calcium and phosphate to crystallize. When you soak your teeth in a container filled with EBP, the minerals bind to it. Minerals from the solution do not stick to the teeth without EBPS. This makes these peptides an important component in crystal growth.

This knowledge led Japanese researchers to bind teeth with minerals, assuming that they could be soaked in EBP called wgnyayk and immersed in calcium and phosphate solutions. If this process works, build or effectively return the hard surface of the teeth. reminderalize Its enamel.

To test this idea, the researchers acquired 30 cow teeth and randomly separated them into three groups. They degrined the enamel of each tooth by placing it in a solution containing acetic acid at a pH of 4.5 for 7-9 days to mimic how natural tooth enamel fades. After this process, the scientists coated two groups of teeth with wgnyayk peptides and did not leave the other groups. They immersed them in a remineralization solution containing monopotasium phosphate and buffer at a pH of 7. The researchers also added a green pigment to the solution that brightens and brightens the harder the enamel surface. The more dense the minerals, the more intense the enamel and brighten the teeth.

Scientists analyzed teeth soaked in WGNYAYK peptide solution under a laser microscope. They found that the higher the concentration of the peptide solution that had soaked in the teeth, the brighter fluorescent green. They explained that this correlation means that the combination of peptide and mineral baths partially restored tooth enamel.

The researchers considered their experiment a success because the EBP they tested promoted dental remineralization. Next, they are trying to create a local application of this EBP for clinical research. They warned that before this EBP is brought to trial in humans, scientists should investigate the composition and potential adverse effects of reinserted teeth. Still, the researchers concluded that their success was a step in the right direction for dentistry. Future testing will check whether EBP treatment is effective in human teeth as well as in cow teeth.


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Source: sciworthy.com

The Age of the Brain: How 13 Types of Proteins in the Blood Can Give Clues

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Researchers trained artificial intelligence model to measure people's age from brain scans

Laboratory/Alamy

The abundance of 13 types of proteins in the blood appears to be a strong indicator of how quickly the brain is aging. This suggests that blood tests could one day help people track and even improve their brain health.

Most previous studies have looked at protein markers of brain aging in the blood. Less than 1000 peoplesay nicolas seyfried from Emory University in Atlanta, Georgia, was not involved in the new study.

To get a broader idea of ​​the effects of these proteins, Liu Weishi Researchers from Fudan University in China analyzed MRI brain scan data from around 11,000 adults (approximately 50 to 80 years old at the time of the images) who took part in the UK Biobank project.

Liu's team trained an artificial intelligence model using data from 70% of the participants to determine features of brain images, such as the size of different brain regions and how different parts are connected to each other. The age of the participants was predicted based on When the model was applied to the remaining 30% of participants, its predictions were accurate to within 2.7 years of their actual age.

The researchers then used the model to predict the age of another group of about 4,700 people, with an average age of 63, who also underwent brain imaging for UK Biobank. The researchers calculated the difference between these participants' actual ages and their AI-predicted ages, called the brain age gap. “The higher the age predicted by the AI ​​compared to the actual age, the faster the brain ages,” Liu says.

The group also provided blood samples around the same time as the brain imaging. From this, the research team identified eight proteins that appear to increase in abundance as brain age increases, and five proteins that appear to decrease in abundance.

In an analysis of data from previous studies, researchers confirmed that these proteins are produced by brain cells and that their levels can influence the risk of dementia and stroke.

This suggests that blood tests for these proteins may reveal how quickly the brain ages. “These markers may be canaries in the coal mine that say, 'Hey, look, let's start doing interventions that slow brain aging while there's still plenty of time,'” Seyfried said.

But for this to be helpful, we need to know that these proteins can change with lifestyle changes. “If I run this much, I'll lose this much weight, if I change my diet, [then] We can correct these levels and bring them back into normal range,” Seyfried says.

Because the study was conducted primarily among wealthy white people, Seyfried said more research is needed to see if the results hold true for other populations with more diverse ethnicities and income levels.

The research team now hopes to conduct studies in animals to determine exactly how the 13 proteins affect the brain. For example, researchers might test whether disrupting levels of these proteins affects cognition or even the development of neurodegenerative conditions, Liu says. “In the coming decades, this could open up ways to target proteins to slow aging and disease.”

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Source: www.newscientist.com