Sweat. Where Does it Come From?

The majority of the fluids in our body reside within cells and in the spaces between cells. Broadly, the fluids in our body can be divided into two main compartments:

Intracellular fluid (ICF): This is the fluid that is contained inside our cells. It accounts for about two-thirds (roughly 66%) of the total body water in a typical human.

Extracellular fluid (ECF): This is the fluid that exists outside of our cells. It accounts for about one-third (roughly 33%) of the total body water. The extracellular fluid can be further broken down into:

Interstitial fluid: The fluid that lies between cells (in the “interstitial” spaces) and accounts for most of the ECF.
Plasma(Circulatory System): The liquid component of blood where the blood cells are suspended.
Transcellular fluid: These are small amounts of fluid contained in specific spaces, such as synovial fluid in joints, cerebrospinal fluid in the brain and spinal cord, and intraocular fluid in the eyes.

Sweat consists primarily of water (90% by volume), with 1-3% salt and 0.5-2% urea.

In a typical adult human, total body water might comprise about 60% of the body’s total weight (though this can vary based on factors like age, sex, and body composition). So, around 40% of the body’s weight is from intracellular fluid, and around 20% is from extracellular fluid.

Urea derivatives have a wide range of biological activities, including anticancer, antibacterial, and antiviral. Some urea derivatives, such as N-phenyl-N’-(2-chloroethyl)ureas (CEUs) and benzoylureas (BUs), have shown good anticancer activity. These compounds are tubulin ligands that inhibit the polymerization of tubulin.

Diarylurea is a prominent pharmacophore in anticancer drugs. This activity is due to its near-perfect binding with certain acceptors. The NH moiety acts as a hydrogen bond donor, and the urea oxygen atom acts as an acceptor.

Urea derivatives have also shown anticonvulsant, analgesic, and high-density lipoprotein (HDL) elevating activities.

Sweat originates from both intracellular and extracellular fluids. Here’s how the process works:

1. Initial Formation in Sweat Glands: Sweat is primarily formed in sweat glands, which are distributed across the skin. Initially, sweat glands produce a fluid that is similar to plasma (i.e., the fluid portion of blood without the cells) but without the proteins. This initial sweat is derived from the extracellular fluid, especially the plasma.

2. Modification of Sweat: As the sweat passes through the ducts of the sweat gland, the composition of the sweat is modified. Specifically, cells in the ducts of the sweat glands reabsorb sodium and chloride ions, making the sweat hypotonic relative to plasma. To achieve this reabsorption, cells use energy and move ions against their concentration gradient. In the process, water from inside the cells (intracellular fluid) can also be drawn into the duct due to osmotic forces.

So, while the initial formation of sweat is primarily from the extracellular fluid, the modification of sweat as it passes through the sweat gland ducts can involve intracellular fluid. However, in terms of volume, the majority of the sweat comes from the extracellular compartment.

It’s worth noting that sweating is an essential mechanism for thermoregulation. As sweat evaporates from the surface of the skin, it cools the body down. Additionally, sweat also plays a role in excreting certain waste products. For those that are less active, that is, those that don’t sweat because of inactivity, the kidneys are the primary organs for excretion in the body from the body’s fluid storage.

-Michael J. Loomis & ChatGPT

And It All Starts With Giving a Shit

Nobody ever got shit to stick to a wall without first getting their hands a little dirty. And nobody ever got their hands dirty doing this without first giving a shit.

“Throwing shit at a wall until it sticks” is a common Australian saying that means if you try to attack a problem long enough and with enough varied methods, then eventually, you must make some progress.

Not everyone can be as lucky as Gary Dahl and his Pet Rock.

His idea for the Pet Rock came to him in a bar while he was listening to friends complain about their pets. Dahl joked that he had a pet that required no care or attention because it was a rock. The rock would not need to be fed, walked, bathed, or groomed, and it would not die, become sick, or be disobedient.

Dahl, an American businessman and advertising director, created the collectible toy Pet Rock in the mid-1970s. The Pet Rock was a smooth stone from Rosarito, Baja California, Mexico. Each rock came on a bed of straw with a carrying case and an instruction manual. The Pet Rock retailed for $3.95 and made Dahl a millionaire.

For the rest of us, sometimes that means that we first gotta give a shit and be willing to get our hands a little dirty.

-Michael J. Loomis

Cancer: Why Are We Scared Of It?

Cancer is a scary word for most people. Most at least know or have lost a loved one to cancer. As a result, it engenders a lot of mixed emotions. One of the biggest is fear, which is understandable because it is typically associated with physical pain in the individual experiencing it, but also in the friends and loved ones through emotional pain.

Over the last six(6) years, I have studied human physiology and disease pathology because of my own experiences and interactions with this BIG, scary word, cancer. As a result, I no longer fear cancer to the same level that some or most do. Fear does not fare well in the light of knowledge and understanding.

A cancer diagnosis is not the end of the world, and it is not something that happens to us as if we are a victim of it. It is a condition connected with or rooted in a biological process that has been taking place over a long period of time, usually without our knowledge.

What we call cancer is not something that is attacking us. On the contrary, it is something that is happening within us with our body’s full knowledge and wilful intent. What we call cancer is a result of our body’s continual efforts to maintain homeostasis for the overall good of us as a wonderfully created creature of creation. However, to most people, it doesn’t feel that way because we have been taught something different for many generations. I would like to dispel that myth and bring light and comfort to a world where fear has taken over in the darkness of ignorance.

Please continue to follow along with me. I’ve got a lot more to say about this…

Zinc, A Little Something to Make You Think

The incessant dance of atoms and molecules around us unfolds an undeniably beautiful ballet of nature. Among these, a wondrous metal with the atomic number 30 makes a remarkable appearance – zinc. Many of us, in the thrall of our sophisticated digital age, remain oblivious to this humble metallic actor’s cosmic journey and its vital role in the grand opera of human existence.

Zinc, our protagonist, began its journey not on our azure host(Earth), but in the boundless vastness of the cosmos, forged in the stellar crucibles of supernovae. Cosmic winds, the grand maestros of the universe, orchestrated its journey towards our solar nebula, paving the way for the conception of our beautiful planet. Upon Earth’s formation, zinc nestled deep within her bosom, hidden beneath a crust of more glamorous elements. It took the inventive curiosity of mankind in the post-stone age, roughly 5000 years ago, to excavate and mold zinc into a useful ally. We learned to alloy zinc with copper, birthing brass, and thus, stepping into the age of metallurgy, unraveling a new chapter of civilization.

Zinc doesn’t merely belong in the annals of our human history; it is an intimate participant in the pulsating rhythm of life itself. This bluish-white metal, while not as ostentatious as gold or celebrated as iron, is fundamental to our health and well-being.

Deep within our bodies, hidden from the prying eyes of our consciousness, zinc plays an unassuming but powerful role. It slips into enzymes, becoming an integral part of over 300 different types, each performing a crucial task in the symphony of our biological processes. From the division of our cells, the orchestration of our immune response, to the expression of our DNA – zinc is there, in every note, in every beat, assisting, catalyzing, and enabling.

Imagine, for a moment, life without zinc. The music of our bodily functions would descend into a dissonant cacophony. Our cells would cease to divide, our wounds would refuse to heal, and our taste and smell would abandon us, leaving us in a world bereft of sensory pleasures. The vital process of growth and development in children would falter, casting a shadow over the vibrancy of youth. Zinc deficiency can transform life into an echo of its full expression, a symphony with its vital instruments missing.

Many of us, swept away by the glitz and glamour of modern life, forget the fundamentals. We forget how the subtle dance of elements like zinc orchestrates the drama of our existence. We neglect the importance of maintaining a balanced diet, rich in zinc, leading to an unfortunate deficiency of this vital nutrient.

While we engage in intellectual pursuits and explore the realm of the abstract, we must not lose touch with the primal. We must remain grounded in our physical existence, understanding the subtle interplay of the elements that maintain our well-being. And zinc, in all its humble glory, demands our attention.

Just as zinc has found its place in the cosmic order, becoming part of stars, planets, and living organisms, it has also found a home within us. This connection, this intimate dance between the human and the elemental, is a realization of our place in the cosmos. It is a beautiful reminder that we are not merely observers of the universe, but participants, intimately connected with the cosmic dance.

So, let us celebrate zinc, this unassuming yet vital element, not just for its role in human health but also for its cosmic journey and its place in the grand opera of existence. It serves as a gentle reminder of our interconnectedness with the universe, a profound illustration of the saying, “We are stardust.” By recognizing and acknowledging the importance of elements like zinc, we are not merely caring for our health but also acknowledging our intimate connection with the cosmos.

Ensure the presence of this humble element in your diet, not only as a step towards healthy living but also as a nod to your cosmic heritage. The zinc in us and the zinc in the stars are one and the same. We are all dancing to the same symphony of existence, an ode to the universe and life itself.

Michael J. Loomis & ChatGPT

The Loomis Lichen Epithelial Cancer Hypothesis: A Simplified Summary

The essay is about an idea called the “Loomis Lichen Cancer Hypothesis” which talks about the relationship between a kind of multipartner(multicellular, multispecies) organism called lichen and humans and how it might affect human health, especially what we call cancer.

For a fuller treatment of this summary.

Firstly, what is lichen? A lichen is like a super-team or grouping of two or more tiny organisms that help each other out. This includes a fungus and a kind of algae or bacteria. Algae are like plants that live in water-based environments and bacteria are tiny, single-celled organisms. Remember, the human body is about 60% water. The lichen team is very diverse, with potentially up to 30,000 different kinds!

One kind of algae that’s important in human lichens is called Prototheca. These algae are interesting because they lack chlorophyll, which most plants and algae use to make food through photosynthesis. Instead, Prototheca feed off the organic material around them, which lets them live in lots of different environments, throughout the human body.

Now, this is where it gets a bit more complex. Some Prototheca species can cause diseases in people, especially those with weaker immune systems. They can cause skin problems or more serious diseases affecting different organs in the body. This makes them an important area to research, especially since they’ve developed resistance to some medicines used to treat infections.

Prototheca algae have some harmful compounds too. Some of these can damage our liver or nerves or cause cell death. But remember, not all algae produce toxins and those that do might not always produce them.

We have lichen living on the human body. We’re talking about real lichen that live on the skin, adapting to the changing environment of the body. These lichens come in different forms, like flat leaf-like ones or more branched, bush-like ones.

Lichens on the body also have a way to reproduce. They produce little parts that can break off and grow into new lichens elsewhere on the body. They can even make special chemicals that help them fight off other bacteria or fungi, and survive the body’s immune responses.

So, while the idea of lichens on our body might seem a bit strange, it’s actually a fascinating area of study. Understanding how these tiny organisms live and interact with us could help us understand more about our health and potentially find new ways to treat diseases.

The Loomis Lichen Epithelial Cancer Hypothesis

The Loomis Lichen Cancer Hypothesis as specifically applied to, relating to, or denoting the thin tissue forming the outer layer of a body’s surface and lining the alimentary canal and other hollow structures on and in the human body.

An Overview of the Genus Prototheca: Intricate Characteristics and Interactions with the Human Body as a Foundation for What We Currently Call Cancer.

A Simplified Summary

Lichen Diversity. There is no global list of known lichen species, but estimates vary from 13,000 to 30,000 different species. The various growth forms are described as crustose, foliose, and fruticose.

A lichen is not a single organism, but the result of a partnership (mutualistic symbiosis) between a fungus and an alga and/or cyanobacteria. A multi-partner (multicellular, multispecies) organism. Some lichens are formed of three or more partners, as mentioned. The body of a lichen consists of fungal filaments (hyphae) surrounding cells of algae(prototheca) and/or cyanobacteria.

Prototheca is a unique genus of algae that falls under the family Chlorellaceae. Unlike other algae, Prototheca species are distinct in their ability to inhabit and interact with the human body, exhibiting an intriguing blend of symbiosis and pathogenicity.

At the most fundamental level, Prototheca are achlorophyllous, meaning they lack chlorophyll and hence are incapable of photosynthesis, a trait atypical for algae. They are eukaryotic organisms characterized by their unicellular nature, distinct cell walls, and the presence of multiple organelles. Furthermore, their life cycle features both sexual and asexual stages, contributing to the robust adaptability and resilience of these organisms.

Among the different species of Prototheca, P. wickerhamii and P. zopfii are the most significant in terms of human interaction. Notably, these organisms demonstrate an unusual ability to inhabit various human body environments, both on the skin and within the internal biological system. They survive within a wide range of pH levels, temperatures, and osmotic pressures, and hence can proliferate in diverse habitats.

While some Prototheca species live harmoniously with their host, others exhibit a pathogenic relationship. Protothecosis, a rare infection caused by Prototheca, primarily affects immunocompromised individuals and may manifest as cutaneous, systemic, or disseminated diseases. Cutaneous protothecosis usually results in lesions and ulcers on the skin surface, while systemic or disseminated protothecosis can affect multiple organs, including the eyes, lymph nodes, and central nervous system.

The fact that Prototheca lacks photosynthetic machinery but retains other typical algal characteristics presents a fascinating evolutionary question. It’s hypothesized that they evolved from photosynthetic ancestors and adapted to a saprophytic lifestyle, utilizing organic material from the surrounding environment for survival. This adaptation may have paved the way for Prototheca’s transition from an external environment to a human host.

Moreover, these algae have developed resistance mechanisms against certain antifungal medications, which complicate their treatment when they cause infections. This suggests a high adaptive capacity and the potential to pose a greater threat to human health in the future if not properly understood and managed.

The genus Prototheca offers a compelling example of how microorganisms can evolve and adapt to novel environments. Despite their rare occurrence, Prototheca species’ ability to thrive in and on the human body underscores their significance in medical microbiology.

Further, prototheca is a genus of algae that, although rare, can cause disease in both humans and animals. Most notably, they cause protothecosis, a rare infection which can range from a localized skin condition to a serious systemic disease depending on the species and the health condition of the individual. Prototheca wickerhamii and Prototheca zopfii are the species most commonly involved in human infections.

1. Prototheca wickerhamii: This species is most often implicated in human disease, causing both localized and systemic forms of protothecosis. In localized infection, the algae typically causes cutaneous lesions, most commonly in the form of nodules, ulcers, or plaques. It is especially prevalent in immunocompromised individuals, such as those with HIV/AIDS, transplant recipients, or those undergoing chemotherapy. If the infection becomes systemic, it can spread to various body organs, including the lymph nodes, eyes, and central nervous system, leading to severe health complications.

2. Prototheca zopfii: While this species is more commonly associated with bovine mastitis (an infection of the udder in dairy cows), it can also cause human disease. Similar to P. wickerhamii, P. zopfii can cause skin lesions in humans, and more rarely, systemic infections. In systemic infections, P. zopfii can affect multiple body systems, leading to symptoms such as weight loss, fever, and fatigue. It can also lead to conditions such as arthritis and olecranon bursitis.

The impact on human health can be quite severe, particularly in immunocompromised individuals, who are more susceptible to systemic infection. It is also important to note that Prototheca species resist most antifungal drugs, making treatment challenging.

Preventing protothecosis involves general infection prevention measures, such as good personal hygiene, using protective clothing and gloves when necessary, and ensuring those with compromised immune systems are especially careful to avoid potential sources of infection.

Their unique features, interaction with the human host, and the diseases they cause warrant comprehensive research and a better understanding of these intriguing organisms.

Algae produce a variety of harmful compounds. These compounds can be toxic to organic life. Here are some examples:

Microcystins: These are potent liver toxins contributing to carcinogenesis.
Anatoxins: These are neurotoxins that can cause paralysis and respiratory failure.
Cylindrospermopsins: These toxins affect the liver and kidney, potentially leading to carcinogenesis.
Cyanotoxins: These are a group of toxins produced by cyanobacteria, a type of algae. They include several subclasses. See below.

Cyanobacteria can produce a range of toxic compounds, collectively referred to as cyanotoxins. They pose significant risks to humans, animals, and the environment. These toxins can be broadly categorized into four groups based on the physiological effects they cause:

1. Hepatotoxins: These primarily target the liver and other internal organs. Microcystins and nodularins are common examples of hepatotoxins produced by cyanobacteria. They inhibit protein phosphatases, leading to liver damage and possibly death in severe cases.

2. Neurotoxins: These toxins primarily affect the nervous system. Anatoxin-a, also known as “Very Fast Death Factor,” and saxitoxin, which is a potent paralytic agent, are examples of neurotoxins produced by cyanobacteria. These toxins can cause symptoms ranging from muscle twitching to respiratory paralysis and death.

3. Cytotoxins: Cylindrospermopsin is an example of a cytotoxin, which primarily targets the liver but can also affect the kidneys, heart, and other organs. It inhibits protein synthesis and can cause cell death.

4. Dermatotoxins: These toxins can cause skin irritation, such as rash, swelling, and blistering. Lipopolysaccharides found in cyanobacteria are suspected to cause these effects.

It’s important to note that not all cyanobacteria produce toxins, and those that do may not produce them under all conditions. The production of toxins can be influenced by environmental factors such as light, temperature, and nutrient availability.

Algae, like all photosynthetic organisms, require several key nutrients for growth and survival. The main nutrients required by algae include:

1. Light: As photosynthetic organisms, algae require light energy to convert carbon dioxide and water into sugars (glucose) and oxygen through the process of photosynthesis.

2. Carbon: Algae utilize carbon dioxide (CO2) from their environment to create organic compounds for growth and reproduction. This is done through the process of photosynthesis.

3. Nitrogen: This is an essential element for protein synthesis and is required for growth and reproduction in algae. Sources of nitrogen for algae can include nitrate (NO3-), ammonia (NH4+), or dissolved organic nitrogen.

4. Phosphorus: Phosphorus is a key component of ATP, nucleic acids (DNA and RNA), and other molecules necessary for energy transfer and genetic information storage. Algae typically absorb phosphorus in the form of phosphate ions (PO4^3-).

5. Potassium: Required for enzyme activity and maintaining the ionic balance within algal cells.

6. Sulfur: Sulfur is a component of some amino acids and vitamins, and is essential for protein synthesis.

7. Trace elements: Algae also require trace amounts of various other elements, such as iron (Fe), manganese (Mn), copper (Cu), zinc (Zn), molybdenum (Mo), cobalt (Co), and several others. These elements are involved in various biochemical processes, such as serving as cofactors for enzymes.

8. Vitamins: Some algae species may require certain vitamins for growth, such as B12, B1, and biotin.

It’s important to note that the specific nutritional needs can vary somewhat depending on the species of algae. Some can fix nitrogen, including prototheca(human algae) from the atmosphere, while others require it from their environment.

Characteristics and Forms of Lichen Presented on and in the Human Body

Lichens are fascinating composite organisms, primarily comprising a symbiotic association of two distinct species: a fungus (mycobiont) and a photosynthetic partner (photobiont), usually an algae or cyanobacteria. Traditionally, lichens have been recognized for their ability to colonize some of the harshest environments on Earth, from desolate Antarctic tundras to bare rocky terrains. Less known, however, is the existence and characteristics of lichens that have adapted to survive in and on the unique ecosystem of the human body.

One should distinguish the lichen-forming fungi from the medically recognized condition called “lichen” in humans, such as lichen planus, lichen planopilaris or lichen sclerosus, which are not associated with the symbiotic organisms found in natural environments but are dermatological conditions characterized by skin lesions. The use of “lichen” in these instances refers to the similarity in appearance to lichen in nature. This essay will focus on the characteristics of true lichen in and on the human body.

The human body represents a distinct and specialized habitat for lichen species due to the specific microclimate, availability of nutrients, and constant interaction with the human immune system. Here, lichens have not only adapted to survive but have also diversified into numerous forms, exhibiting various morphologies and reproductive strategies.

Of their morphologies, lichen on the human body can be divided into three main types. The first is the crustose form, which grows flush against the skin. This form is characterized by its encrusting thallus, or body, that adheres tightly to the substrate, making it almost inseparable from the human skin. The second type is the foliose form, which resembles leaf-like structures. They are somewhat flat, and unlike crustose lichens, they can be gently removed from the skin. Lastly, the fruticose form resembles miniature shrubs, displaying a branched or bushy structure. Fruticose lichens are relatively rare in the human ecosystem, likely due to the environment’s constant change and relative instability.

Reproductive strategies of lichens in and on the human body are primarily asexual, involving the production of specialized propagules like soredia and isidia. Soredia are tiny balls of algal cells surrounded by fungal hyphae, which can be dispersed by minor disturbances and form new lichens elsewhere in or on the body. Isidia are cylindrical outgrowths that can break off to initiate new colonies.

Living in and on the human body also poses unique challenges to lichens, including elevated temperatures, varying humidity, constant shedding of skin cells, and the dynamic host microbiome. Think dry sauna. Lichens have adapted to these conditions by developing specialized structures and biochemical compounds. Many lichens produce unique metabolites, collectively termed as lichen substances, which have antibacterial and antifungal properties, helping them to fend off potential competitors and to resist the host’s immune responses.

While the study of human-associated lichens is still in nascent stages, early evidence suggests a complex interaction with the host. They can potentially influence the skin’s microbiota and even participate in nutrient cycles, such as nitrogen fixation.

In conclusion, lichens that reside on the human body showcase a complex array of adaptations to a unique habitat. Understanding their roles, interactions, and implications on human health remains an intriguing area of research, with potential applications in dermatology, microbiology, and pharmaceuticals.

-Michael J. Loomis & ChatGPT

Whether You Lichen It or Not, They Lichen You

Characteristics and Forms of Lichen Presented on and in the Human Body

In conclusion, lichens that reside on the human body showcase a complex array of adaptations to a unique habitat. The understanding of their roles, interactions, and implications on human health remains an intriguing area of research, with potential applications in dermatology, microbiology, and pharmaceuticals.

Proteolysis and Aging. Why I Take Serrapeptase and Lumbrokinase(Sometimes)

What is the relationship between proteolysis and aging?

Note: The use of these enzymes should likely be for a limited time span only. I will use them for a two-week period once every few months to clean out the aging cobwebs…8). The reason why is explained in the last paragraph.

Proteolysis refers to the breakdown of proteins into their constituent amino acids or smaller peptides, typically by enzymatic action. In the context of aging, proteolysis is an essential part of cellular maintenance and repair mechanisms, which are critical for health and longevity. Here are some potential benefits of proteolysis on aging:

1. Clearance of damaged proteins: Over time, proteins can become damaged due to various factors like oxidative stress, exposure to harmful substances, etc. Damaged proteins can become dysfunctional and may contribute to age-related diseases. Proteolysis helps in clearing these damaged proteins, maintaining the health of cells and tissues.

2. Autophagy and longevity: Proteolysis is a key part of autophagy, a cellular process of self-digestion where damaged organelles, misfolded or aggregated proteins are degraded and recycled. Dysfunctional autophagy has been linked with aging and age-related diseases. Enhancing autophagy through proteolysis might promote longevity and slow down the aging process.

3. Regulation of protein homeostasis (proteostasis): Aging is associated with a decline in proteostasis, the balance of protein synthesis, folding, and degradation. Proteolysis is a major factor in maintaining proteostasis, which is crucial for cellular function and health.

4. Activation of beneficial pathways: Certain proteins, when broken down through proteolysis, can activate pathways that are beneficial for health and longevity. For example, proteolysis of certain proteins can activate mTOR (mechanistic target of rapamycin), a key regulator of aging.

5. Immune system function: Proteolysis can support immune system function, which often declines with age. The process helps present antigens to immune cells, aiding in the recognition and clearance of pathogens and potentially cancerous cells.

6. Cell signaling: Proteolysis also plays a role in various cell signaling pathways, many of which can impact aging. For example, Notch signaling, which is regulated in part by proteolysis, is involved in cell differentiation and tissue homeostasis.

While proteolysis appears to have beneficial effects on aging, it’s also important to note that uncontrolled proteolysis can lead to muscle wasting and other detrimental effects. Balance is key, and maintaining optimal levels of proteolysis is important for health and longevity. Further research is needed to better understand how to regulate proteolysis for anti-aging benefits.

-Michael J. Loomis & ChatGPT

Protein…Too Much of a Good Thing.

Are there any health-related problems created by consuming too much protein?

Author: Find my solution at the end…8)

Yes, consuming too much protein can potentially lead to several health issues. Here are some of them:

1. Kidney Damage: High protein diets, particularly animal protein, may strain the kidneys and lead to kidney disease, especially in people with pre-existing renal conditions. The kidneys have to work harder to remove the waste products of protein metabolism.

2. Dehydration: Increased protein intake can lead to dehydration. This is because the kidneys need more water to eliminate the byproducts of protein metabolism.

3. Digestive Problems: Consuming too much protein can lead to digestive issues like constipation, bloating, and other discomforts, especially if your diet is low in fiber.

4. Nutrient Deficiencies: A diet high in protein can sometimes result in neglecting other food groups, potentially leading to deficiencies in important nutrients.

5. Heart Disease: High protein diets, especially those rich in red meat and full-fat dairy, can increase the risk of heart disease due to a higher intake of saturated fat and cholesterol.

6. Bone Health: Some studies suggest that overconsumption of protein, especially animal protein, could lead to calcium loss from bones, increasing the risk of osteoporosis. However, this topic is debated, with other research suggesting adequate protein is beneficial for bone health.

7. Liver Damage: People with liver disease are advised to limit their protein intake because overconsumption could worsen liver function.

While protein is an essential part of a balanced diet, it’s important to ensure it’s consumed in moderation and as part of a varied diet to ensure the intake of other essential nutrients.

As always, it’s advisable to consult a healthcare professional or a dietitian for personalized advice before making major changes to your diet.

What are the waste products of protein metabolism?

Protein metabolism involves a number of steps that lead to the production of several waste products. Here are a few of them:

1. Ammonia (NH3): This is a toxic substance produced when proteins are broken down. The body converts it into a less harmful substance called urea.

2. Urea: This is the primary waste product of protein metabolism and is excreted in the urine. The liver converts ammonia into urea as part of the urea cycle, which is then transported to the kidneys for excretion.

3. Creatinine: This is a waste product formed from the metabolism of creatine, a compound that provides energy to muscles.

4. Uric Acid: This is a waste product formed from the breakdown of nucleic acids (the building blocks of DNA). While not directly a product of protein metabolism, diets high in certain proteins can contribute to increased levels of uric acid.

5. Carbon Dioxide (CO2): This is produced during the process of energy production in cells, including during the metabolism of the carbon skeletons of amino acids.

These waste products, especially urea, and creatinine, are often measured in blood and urine tests to assess kidney function, as the kidney plays a key role in filtering and excreting these substances.

What are the carbon skeletons of amino acids?

Amino acids, the building blocks of proteins, are composed of a central carbon atom (the alpha carbon) attached to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom, and a side chain (R group) that varies for each specific amino acid.

When the amino group is removed from an amino acid in a process called deamination, the remaining structure — which includes the central carbon atom, the carboxyl group, and the unique side chain — is often referred to as the carbon skeleton, or sometimes the keto acid.

These carbon skeletons can be further metabolized in the body. Depending on their structure, they can enter into various metabolic pathways. Some can be converted into glucose through a process called gluconeogenesis. Others can be converted into ketone bodies or directly enter the citric acid cycle (also known as the Krebs cycle or the TCA cycle) for energy production.

In summary, the carbon skeletons of amino acids refer to the remaining molecular structure after the amino group is removed, and they can be metabolized in various ways depending on the body’s needs.

What foods contribute to the citric acid cycle?

The citric acid cycle, also known as the Krebs cycle or the tricarboxylic acid (TCA) cycle, is a series of chemical reactions used by all aerobic organisms to generate energy. This cycle doesn’t directly involve food but rather certain molecules that can be derived from the macronutrients in our diet: carbohydrates, fats, and proteins.

Here’s how different nutrients from food contribute to the cycle:

1. Carbohydrates: These are broken down into glucose during digestion. Glucose then undergoes a process known as glycolysis, resulting in a compound called pyruvate. Pyruvate enters the mitochondria (the energy-producing structures within cells), where it is further converted into Acetyl-CoA, a crucial molecule that enters the citric acid cycle.

2. Fats: Dietary fats are primarily composed of triglycerides, which are broken down into glycerol and fatty acids. Fatty acids are converted into molecules called acyl-CoA, which are then converted to Acetyl-CoA via a process called beta-oxidation. This Acetyl-CoA can then enter the citric acid cycle.

3. Proteins: Proteins are broken down into their individual amino acids. Some of these amino acids can be deaminated (removing the amino group) to form molecules that can be converted into Acetyl-CoA or other intermediates of the citric acid cycle.

In summary, a wide range of foods can contribute to the citric acid cycle indirectly, as the cycle uses Acetyl-CoA and other intermediates that are derived from the breakdown of carbohydrates, fats, and proteins in the foods we eat. Foods rich in these nutrients include whole grains, fruits, vegetables, meat, poultry, fish, legumes, nuts, seeds, and oils.

Does the citric acid cycle have any effect on urine or blood ph?

The citric acid cycle itself does not directly affect blood or urine pH. This cycle primarily serves to generate energy for the cell by oxidizing Acetyl-CoA to produce ATP, carbon dioxide, and water. However, there are indirect ways that elements of metabolism linked to the citric acid cycle can impact blood and urine pH.

1. Respiration and Blood pH: One of the products of the citric acid cycle is carbon dioxide (CO2), which is expelled from cells, transported in the blood to the lungs, and exhaled. CO2 in the blood can combine with water to form carbonic acid, which can dissociate into bicarbonate and hydrogen ions. An increase in CO2 in the blood, therefore, can increase the acidity (lower the pH) of the blood. This is usually corrected by an increased breathing rate to expel more CO2, but in certain situations like respiratory disorders, it could lead to a state of acidosis.

2. Diet and Urine pH: While the citric acid cycle itself doesn’t directly influence urine pH, the types of foods you eat (which contribute different metabolites to pathways like the citric acid cycle) can influence urine pH. For example, a diet high in animal protein can lead to more acidic urine due to the generation of sulfurous waste products from protein metabolism. On the other hand, a diet rich in fruits and vegetables can lead to more alkaline urine due to the metabolites they contribute.

3. Metabolic Acidosis or Alkalosis: In certain pathologic conditions, metabolic acidosis (low blood pH due to increased production of acids or inadequate removal of acids by the kidneys) or metabolic alkalosis (high blood pH due to loss of acid from the body or increased bicarbonate levels) can occur. These conditions can involve metabolites that are part of or related to the citric acid cycle, but these are usually complex situations involving multiple physiological processes.

The body has multiple systems in place to tightly regulate blood pH, including the respiratory system, the renal system, and various buffer systems in the blood. Disturbances in pH can have significant effects on bodily function and require medical attention.

Hey Mike, are rice and beans combined a good source of protein?

Why yes they are. Combining rice and beans can provide a complete protein source. Proteins are made up of amino acids, some of which the body cannot make on its own. These are called essential amino acids, and they must be obtained from the diet.

Individual plant-based foods often lack one or more of these essential amino acids, but you can combine foods to get all of them. This is known as protein combining or complementary proteins. For example, grains like rice are low in the amino acid lysine but have enough of another amino acid, methionine. On the other hand, legumes like beans are low in methionine but have enough lysine.

When you eat rice and beans together, they can provide all of the essential amino acids in sufficient amounts, making the combination a complete protein source. This is particularly beneficial for those following a vegetarian or vegan diet.

However, it’s worth noting that you don’t need to eat complementary proteins at every single meal. As long as you’re consuming a variety of protein sources throughout the day, your body can assemble the amino acids into complete proteins.

Collagen and Glucose

Protein(Collagen) and Glucose. These are what we need to be arguing about and what are the best sources of them. Vegan, Carnivore, Vegetarian, Keto, Pescatarian, Paleo, or Whatevero misses the point. It’s not what our stomach needs but what do our cells and their mitochondria need.

The protein that is most abundant in the human body is collagen. Collagen is the main component of connective tissue and is crucial for maintaining the structure and integrity of skin, tendons, bones, and ligaments. In fact, about one-third of the protein content in your body is made up of collagen. It also plays a vital role in maintaining healthy hair and nails.

Your body makes collagen by combining amino acids, which you can get from eating protein-rich foods. Additionally, the process requires vitamin C, zinc, and copper. Here are some foods that can help your body produce collagen:

Protein-Rich Foods: The key amino acids needed for collagen production include glycine, proline, and hydroxyproline. You can get these from protein-rich foods like lean meats, fish, eggs, dairy products, and plant-based proteins like beans and legumes.

Vitamin C: This vitamin is necessary for collagen synthesis. Citrus fruits like oranges, lemons, and grapefruits are rich in vitamin C. Other good sources include strawberries, bell peppers, and broccoli.

Zinc: This mineral is a co-factor in collagen synthesis. Zinc is present in high amounts in foods like oysters, red meat, poultry, beans, nuts, whole grains, and dairy products.

Copper: This trace mineral can help promote collagen production. You can find copper in organ meats, sesame seeds, cocoa, cashews, and lentils.

Bone Broth: This is a particularly good source of collagen, as it is made by boiling down the bones of animals, which are rich in this protein.

Antioxidant-Rich Foods: Antioxidants help protect against damage to collagen. Foods high in antioxidants include berries, green tea, dark chocolate, and colorful fruits and vegetables.

Remember, the best way to ensure adequate collagen production is to maintain a balanced, varied diet with plenty of whole foods. It’s also important to note that factors such as aging, smoking, and excessive sun exposure can impair collagen production and damage existing collagen in your body.

1. Protein-Rich Foods: The key amino acids needed for collagen production include glycine, proline, and hydroxyproline. You can get these from protein-rich foods like lean meats, fish, eggs, dairy products, and plant-based proteins like beans and legumes.

2. Vitamin C: This vitamin is necessary for collagen synthesis. Citrus fruits like oranges, lemons, and grapefruits are rich in vitamin C. Other good sources include strawberries, bell peppers, and broccoli.

3. Zinc: This mineral is a co-factor in collagen synthesis. Zinc is present in high amounts in foods like oysters, red meat, poultry, beans, nuts, whole grains, and dairy products.

4. Copper: This trace mineral can help promote collagen production. You can find copper in organ meats, sesame seeds, cocoa, cashews, and lentils.

5. Bone Broth: This is a particularly good source of collagen, as it is made by boiling down the bones of animals, which are rich in this protein.

6. Antioxidant-Rich Foods: Antioxidants help protect against damage to collagen. Foods high in antioxidants include berries, green tea, dark chocolate, and colorful fruits and vegetables.

And then there is Glucose. Glucose is a simple sugar that your body uses as its main source of energy. All carbohydrates you consume are broken down into glucose during digestion, although the speed and efficiency of this process vary depending on the type of carbohydrate. Here are some food sources that can be easily turned into glucose:

1. Simple Carbohydrates: These are the quickest source of glucose since they require less processing in the body. These include fruits like bananas, grapes, apples, and oranges; honey; milk; and sugar.

2. Complex Carbohydrates: These take a bit longer to be converted into glucose, providing a more steady release of energy. They include whole grains (like brown rice, oats, quinoa), legumes (like beans, lentils), starchy vegetables (like potatoes, corn), and whole grain breads and pastas.

3. High Glycemic Index Foods: Foods with a high glycemic index (GI) are digested more quickly and hence raise blood glucose levels rapidly. This includes foods like white bread, most breakfast cereals, potatoes, and sugary drinks.

It’s important to note that while all these foods can be turned into glucose easily, it doesn’t mean you should rely on them for your energy needs. A balanced diet that includes a mix of macronutrients (carbohydrates, proteins, and fats) along with fiber, vitamins, and minerals is the best approach for overall health. Also, consuming too many high-GI or simple carbohydrate foods can lead to health issues such as obesity and type 2 diabetes.

The best way to ensure adequate collagen production is to maintain a balanced, varied diet with plenty of whole foods. It’s also important to note that factors such as aging, smoking, and excessive sun exposure can impair collagen production and damage existing collagen in your body.