Leucine has earned a reputation as one of the most valuable amino acids in nutrition. It helps stimulate muscle protein synthesis, supports recovery, and plays an important role in how the body senses amino acids and nutrient availability.

But there is another side to the story.

Research investigating too much leucine and insulin resistance has raised an important metabolic-health question: Can chronically excessive leucine exposure activate nutrient-signaling pathways so strongly that a mechanism beneficial in one context becomes problematic in another?

The answer is more nuanced than either extreme.

Leucine is not inherently harmful. Nor does the research establish a simple leucine threshold at which insulin resistance suddenly appears. Instead, experimental research suggests that chronic, excessive amino-acid or protein exposure—particularly in metabolically unhealthy or obesity-related conditions—may produce persistent activation of the mechanistic target of rapamycin complex 1, or mTORC1.

That matters because mTORC1 is the same nutrient-sensing pathway that helps translate leucine availability into an anabolic signal.

In other words, the potential problem is not that leucine has a "good" side and a "bad" side. The issue is that biological signaling depends on dose, duration, nutritional context, energy balance, and metabolic state.

This is the leucine paradox: a signal that can support muscle-building when appropriately regulated may become less favorable when nutrient signaling remains chronically elevated.

Understanding that distinction can help make sense of seemingly contradictory findings about leucine, high-protein diets, insulin sensitivity, branched-chain amino acids, and metabolic health.

What Does Too Much Leucine Have to Do With Insulin Resistance?

The central idea in the research is straightforward:

Leucine activates mTORC1, and chronic overactivation of mTORC1 can interfere with insulin signaling under certain metabolic conditions.

Leucine is a branched-chain amino acid, or BCAA. After protein is consumed and digested, leucine enters circulation and becomes available to tissues. Beyond serving as a building block for proteins, leucine acts as a nutrient signal.

One of its most important signaling effects involves mTORC1.

When amino acids are abundant, leucine can help activate mTORC1 through a nutrient-sensing system involving proteins associated with the lysosome. mTORC1 then promotes processes associated with cellular growth, protein synthesis, and nutrient availability.

That response is useful.

After resistance exercise, for example, amino-acid availability combined with exercise-related signaling helps create an environment favorable to muscle protein synthesis.

The concern arises when the signal is not simply a temporary response to a meal or exercise session but part of a chronically nutrient-rich metabolic environment.

Persistent mTORC1 activity can increase activity of downstream signaling proteins such as S6 kinase. Research has shown that this signaling can negatively affect components of the insulin-signaling pathway, including insulin receptor substrate proteins.

That provides a plausible biological connection between excessive nutrient signaling and reduced insulin responsiveness.

Importantly, this mechanism does not mean that eating a leucine-containing meal automatically causes insulin resistance.

The research is about chronic signaling, metabolic context, and the interaction of multiple pathways, not about treating every leucine exposure as metabolically dangerous.

Leucine Is Beneficial. So Why Would More Ever Be a Problem?

This apparent contradiction is at the heart of leucine dose research.

A nutrient can have beneficial effects without producing proportionally greater benefits at every higher dose.

Leucine illustrates this principle particularly well because it acts as both a substrate and a signal.

As a substrate, leucine contributes to the amino-acid pool used to build proteins.

As a signal, it helps tell the cell that amino acids are available and that conditions may be favorable for growth and protein synthesis.

That signaling role is one reason leucine has received so much attention in sports nutrition.

But biological signaling generally operates within a regulated system. A short-lived increase in mTORC1 after eating or exercising is fundamentally different from a state characterized by prolonged nutrient excess and persistent pathway activation.

This distinction is often lost in simplified fitness messaging.

The statement "leucine activates mTOR" is true.

The statement "therefore more leucine is always better" does not logically follow.

The same pathway can produce different consequences depending on timing, magnitude, duration, and the physiological environment surrounding it.

Understanding the Leucine–mTORC1 Connection

To understand the mTORC1 hyperactivation research, it helps to look at what leucine actually does inside the cell.

What Is mTORC1?

mTORC1 stands for mechanistic target of rapamycin complex 1. It is a major nutrient- and energy-sensing signaling complex.

It responds to several types of information, including:

• Amino-acid availability
• Growth-factor signaling
• Cellular energy status
• Nutrient availability
• Cellular stress

When conditions favor growth, mTORC1 helps coordinate processes such as protein synthesis and cell growth.

Leucine is particularly important because it serves as one of the amino-acid signals capable of activating this pathway.

This is one reason leucine has become central to research on muscle protein synthesis.

How Does Leucine Activate mTORC1?

Leucine does not simply flip a single molecular switch.

Its effects involve a network of nutrient-sensing proteins and signaling events. Among the best-characterized mechanisms are amino-acid sensors and Rag-family GTPases that help regulate the positioning and activation of mTORC1.

At a simplified level, abundant leucine signals that amino acids are available.

mTORC1 responds.

Protein synthesis and other anabolic processes can then increase.

That is a useful adaptation when the body needs to respond to exercise, feeding, growth, or tissue repair.

The metabolic question is what happens when the same nutrient-sensing system is repeatedly stimulated in a state where energy and nutrients are already abundant.

What Is mTORC1 Hyperactivation?

mTORC1 hyperactivation refers to a state in which mTORC1 signaling is excessively or persistently elevated relative to what is appropriate for the cellular environment.

It is important to distinguish activation from hyperactivation.

Activation is normal.

Cells need mTORC1.

Without appropriate mTORC1 signaling, normal growth, protein synthesis, and nutrient responses would not function properly.

Hyperactivation is different because persistent signaling can interfere with other regulatory systems.

In metabolic research, this distinction is particularly relevant to insulin signaling.

Why Does Chronic mTORC1 Activity Matter for Insulin Signaling?

Insulin normally binds to its receptor and initiates a signaling cascade that helps cells respond to circulating glucose and other nutrients.

One important part of this process involves insulin receptor substrates and downstream signaling proteins.

When mTORC1 and its downstream kinase S6K1 remain strongly activated, feedback mechanisms can impair insulin receptor substrate function.

The result can be reduced efficiency of insulin signaling.

This is one proposed mechanism connecting chronic nutrient excess with insulin resistance.

Again, this does not mean mTORC1 is "bad."

It means that a pathway can be essential under normal conditions yet contribute to dysfunction when its activity becomes chronically dysregulated.

That principle is much more useful than labeling individual nutrients as simply healthy or unhealthy.

What Does the Research on Excessive Leucine Actually Show?

Research on excessive leucine intake does not support a simple headline such as "leucine causes insulin resistance."

The evidence is more complicated.

Experimental studies have investigated leucine and related amino-acid signaling using isolated cells, animal models, controlled feeding conditions, and observations in humans. These approaches provide different kinds of evidence, and they should not be treated as interchangeable.

The strongest mechanistic evidence often comes from cellular and animal research because researchers can tightly manipulate leucine exposure, signaling pathways, energy intake, and metabolic conditions.

Human research is more complicated.

People do not consume isolated amino acids under laboratory conditions indefinitely. Leucine is typically consumed as part of protein-containing foods or supplements. Total protein intake, calorie intake, body composition, physical activity, insulin sensitivity, liver health, and overall dietary pattern all influence the metabolic response.

That makes it difficult to attribute insulin resistance to leucine alone.

The Obesity Connection Is Especially Important

Much of the concern surrounding excessive nutrient signaling becomes more relevant in the context of obesity and metabolic dysfunction.

Obesity is associated with substantial changes in nutrient metabolism, insulin signaling, inflammation, lipid metabolism, and cellular energy regulation.

In that environment, the body's response to amino acids may differ from the response observed in a metabolically healthy, physically active individual.

This is one reason the question should not be framed as:

"Is leucine good or bad?"

A more scientifically useful question is:

"What happens when leucine-dependent nutrient signaling occurs chronically in a particular metabolic environment?"

That framing leaves room for the research's complexity.

A leucine-rich protein meal after exercise is not metabolically equivalent to chronic nutrient excess accompanied by obesity, sedentary behavior, and insulin resistance.

The surrounding physiology matters.

Too Much Leucine Insulin Resistance Research: Why Context Changes the Interpretation

The phrase "too much leucine" sounds precise, but science does not currently provide a universally applicable number that can be labeled as the insulin-resistance threshold for everyone.

That is an important limitation.

Dose Matters

A nutrient's effect can change with dose.

Low, moderate, and high exposures may activate different degrees of signaling. But the response is not necessarily linear.

More leucine does not automatically mean proportionally more muscle protein synthesis, nor does more mTORC1 signaling automatically mean proportionally greater metabolic harm.

Duration Matters

A temporary increase in mTORC1 after eating is different from chronic activation.

This is perhaps the most important concept for understanding the research.

The body is designed to experience fluctuations.

Nutrients rise after meals.

They decline between meals.

Exercise changes energy demand.

Fasting changes cellular signaling.

These cycles allow metabolic pathways to turn on and off.

Chronic nutrient excess can disrupt that dynamic pattern.

Energy Balance Matters

Leucine does not exist in isolation from calorie intake.

A high-protein diet may have very different metabolic effects depending on whether total energy intake is appropriate, excessive, or insufficient.

Similarly, a person's physical activity level can alter how nutrients are handled.

Muscle contractions increase glucose uptake and change nutrient metabolism. A sedentary state produces a different metabolic environment.

Metabolic Health Matters

The same dietary exposure may not have identical consequences in someone with excellent insulin sensitivity compared with someone who already has metabolic dysfunction.

This is why findings from obesity models deserve attention without being automatically generalized to every person who eats protein.

What About High-Protein Diets and Insulin Resistance?

The high protein diet insulin resistance research is similarly nuanced.

High-protein diets have been studied for weight management, body composition, appetite regulation, muscle preservation, and metabolic health. Results vary substantially depending on the type of protein, total calorie intake, carbohydrate and fat composition, fiber intake, body weight, activity level, and study population.

Some studies have found neutral or favorable effects of higher protein intake on body composition and metabolic markers.

Other research has raised concerns about particular high-protein dietary patterns, especially when considered alongside obesity or preexisting metabolic dysfunction.

That apparent contradiction is not necessarily evidence that one side is wrong.

A "high-protein diet" is not a single intervention.

Consider two hypothetical diets:

Diet A: A physically active person consumes protein-rich legumes, tofu, vegetables, whole grains, nuts, and seeds while maintaining appropriate energy intake.

Diet B: A sedentary person with obesity consumes very large amounts of concentrated protein while also consuming excess calories and an overall low-fiber, highly processed diet.

Calling both simply "high-protein diets" hides important differences.

Protein quantity is only one variable.

Leucine Alone vs. Leucine in Whole Foods

Another critical point is that isolated leucine research should not automatically be interpreted as evidence about every leucine-containing food.

Protein foods contain many amino acids and other nutrients.

Plant foods may also provide:

• Fiber
• Polyphenols
• Minerals
• Unsaturated fats
• Complex carbohydrates
• Other phytochemicals

The food matrix can affect digestion, absorption, satiety, glucose metabolism, and the overall metabolic response.

A laboratory experiment involving isolated leucine is therefore answering a different question from a long-term dietary study involving mixed meals.

This distinction is frequently overlooked when mechanistic findings are turned into nutrition headlines.

Does Eating Protein Automatically Cause mTORC1 Hyperactivation?

No.

Eating protein naturally stimulates nutrient-sensing pathways, including mTORC1. That is a normal part of post-meal physiology.

The research concern is excessive or persistent signaling under particular conditions, not normal protein consumption.

A temporary increase in mTORC1 following a meal is not equivalent to pathological hyperactivation.

This is why statements such as "protein turns on mTOR, therefore protein causes insulin resistance" are scientifically incomplete.

They skip the most important variables: amount, duration, total energy intake, metabolic health, exercise, and dietary context.

The Role of Branched-Chain Amino Acids

Leucine belongs to the branched-chain amino acid family along with isoleucine and valine.

BCAAs have received extensive attention in metabolic research because elevated circulating BCAA levels have been associated with obesity and insulin resistance in observational research.

But association is not the same as causation.

Elevated BCAA levels may reflect changes in how the body processes amino acids rather than being a simple cause of metabolic dysfunction.

This distinction matters because metabolic disease can change amino-acid metabolism.

In other words, high BCAA levels and insulin resistance may be connected without high BCAA intake being the sole initiating factor.

Leucine is therefore best understood as one component of a much larger metabolic network.

Why the Leucine Paradox Is Relevant to Muscle Building

For people interested in muscle growth, this topic can sound alarming.

It shouldn't.

The research does not erase leucine's established physiological role in stimulating muscle protein synthesis.

Leucine remains an important amino acid for skeletal muscle.

The more useful lesson is that maximizing one biological signal indefinitely is not necessarily the same as optimizing health.

Muscle protein synthesis is only one component of whole-body metabolism.

A nutrition strategy can influence:

• Muscle protein turnover
• Glucose metabolism
• Insulin signaling
• Appetite
• Energy balance
• Lipid metabolism
• Gut health
• Body composition
• Cardiometabolic health

Optimizing one pathway in isolation can miss interactions elsewhere.

That is precisely why leucine dose research requires nuance.

Is There a Safe Leucine Intake?

There is no single universally established leucine intake that can be described as the point above which everyone develops insulin resistance.

This is an important answer for anyone searching for a "too much leucine" number.

Research investigating excessive leucine exposure does not establish a universal cutoff applicable to all adults.

Responses can depend on:

• Overall protein intake
• Total calorie intake
• Body composition
• Exercise habits
• Insulin sensitivity
• Age
• Health status
• Dietary pattern
• Duration of exposure
• Whether leucine comes from whole foods or concentrated products

That means the research should not be used to invent a precise danger threshold.

It is better interpreted as evidence that more is not automatically better when a nutrient is also acting as a signaling molecule.

Symptoms of Insulin Resistance: What Should You Know?

Insulin resistance can develop without obvious symptoms.

That makes symptom-based searches such as "signs of insulin resistance from diet" difficult to interpret.

Some people may experience metabolic changes for years without knowing they are occurring.

Possible signs associated with impaired glucose regulation can include fatigue, increased hunger, difficulty managing body weight, or changes in blood glucose, but these symptoms are nonspecific and can have many causes.

They should not be interpreted as evidence that leucine is responsible.

If someone is concerned about insulin resistance, the appropriate approach is evaluation by a qualified healthcare professional rather than attempting to diagnose the condition based on dietary symptoms.

This is particularly important because insulin resistance can be influenced by many factors beyond protein or leucine intake.

Could Excessive Leucine Affect Blood Sugar?

Potentially, but the relationship is not straightforward.

Leucine interacts with nutrient-sensing pathways that intersect with insulin signaling. Chronic dysregulation of those pathways has been investigated as one possible contributor to impaired insulin action.

However, consuming leucine does not necessarily produce an immediate increase in blood glucose.

In fact, amino acids can influence insulin secretion and post-meal metabolism in complex ways.

The important distinction is between acute metabolic responses and long-term metabolic adaptation.

A single meal tells you very little about whether a person's overall diet is promoting or worsening insulin resistance.

Long-term metabolic health depends on the combined effects of diet, body composition, activity, sleep, genetics, energy balance, and other factors.

Does More Leucine Mean More Muscle?

Not indefinitely.

Leucine is a potent trigger for muscle protein synthesis, but muscle-building responses are not infinitely proportional to leucine intake.

Once the relevant signaling and amino-acid availability are sufficient to stimulate the muscle-building response, adding substantially more leucine does not necessarily produce an equivalent increase in muscle protein synthesis.

This is sometimes described as a threshold or ceiling concept.

The precise response depends on factors such as age, exercise, total protein quality and quantity, meal composition, and individual physiology.

That is another reason to be skeptical of simplistic "more leucine is better" messaging.

The body has regulatory limits.

Why Chronic Nutrient Signaling Is Different From Pulsed Signaling

One of the most useful ways to understand the leucine paradox is to think in terms of pulses versus persistence.

After a meal, nutrients rise.

Signaling pathways respond.

The body uses those signals to coordinate digestion, storage, repair, and growth.

Later, nutrient availability changes.

Other cellular pathways become more active.

This flexibility is a defining characteristic of healthy metabolism.

The concern with chronic nutrient excess is that the body may spend too much time in a nutrient-signaling state.

mTORC1 is particularly relevant because it responds to amino-acid abundance and energy availability.

The goal is not to eliminate mTORC1 activation. That would be neither realistic nor desirable.

The goal of healthy physiology is regulation.

A pathway should be able to activate when appropriate and decrease when conditions change.

How Obesity Can Change the Nutritional Picture

Obesity is not simply a condition of having more stored body fat.

It is associated with changes in endocrine signaling, inflammation, lipid metabolism, mitochondrial function, glucose handling, and nutrient sensing.

Those changes can affect how the body responds to protein and amino acids.

This helps explain why findings from animal models of obesity may show metabolic effects that are not necessarily observed in lean, active individuals.

It also explains why the same amount of protein cannot be interpreted without knowing the broader metabolic context.

When researchers investigate excessive leucine intake in obesity-related models, the question is often less about leucine as an isolated toxin and more about what happens when nutrient abundance intersects with an already altered metabolic system.

That is a much more accurate interpretation of the research.

Practical Takeaways From the Research

Although this research should not be turned into a rigid dietary prescription, it does offer several useful principles.

1. Don't confuse "necessary" with "more is better"

Leucine is necessary for normal protein metabolism and plays an important role in muscle protein synthesis.

That does not mean unlimited increases provide unlimited benefits.

2. Look at the whole dietary pattern

Leucine-containing foods are rarely consumed in isolation.

Consider the broader pattern, including fiber, micronutrients, food quality, total energy intake, and the balance of plant and animal protein sources.

3. Don't interpret mechanistic studies as direct human dietary instructions

Cell and animal studies are valuable for understanding mechanisms.

They are not automatically equivalent to long-term human outcomes.

An experiment designed to produce sustained pathway activation under controlled conditions may not represent an ordinary diet.

4. Consider metabolic health, not just muscle signaling

If the goal is overall health, muscle protein synthesis is only one outcome.

Glucose regulation, insulin sensitivity, cardiovascular health, body composition, and metabolic flexibility also matter.

5. Be skeptical of single-nutrient narratives

"Leucine is good" and "leucine is bad" are both inadequate conclusions.

The more useful question is what role leucine plays within a particular physiological and dietary context.

What Does This Mean for Plant-Based Diets?

The leucine paradox is also relevant to people following plant-based diets, although it should not be used to suggest that plant protein is inherently metabolically superior or inferior.

Plant foods vary considerably in protein content and amino-acid composition.

Legumes, soy foods, grains, nuts, seeds, and other plant foods contribute different amino-acid profiles. A plant-based eating pattern also commonly includes substantial amounts of fiber and other bioactive compounds, depending on food choices.

For someone interested in plant-based living, the bigger picture is therefore more useful than obsessing over individual amino acids.

A varied diet can provide protein and essential amino acids while also supplying the other nutrients found in minimally processed plant foods.

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What the Research Does Not Prove

This is one of the most important sections for interpreting the topic responsibly.

Research on mTORC1 hyperactivation does not prove that:

• Normal protein intake causes insulin resistance.
• Eating leucine-rich foods inevitably produces metabolic disease.
• Every high-protein diet worsens insulin sensitivity.
• Leucine supplements automatically cause insulin resistance.
• Everyone should minimize leucine.
• There is one universally harmful leucine dose.
• mTORC1 activation itself is unhealthy.
• Plant protein and animal protein have identical metabolic effects.
• Elevated BCAA levels always cause insulin resistance.

These conclusions go beyond what the evidence can support.

Instead, the research provides a biological rationale for investigating how persistent amino-acid signaling interacts with insulin signaling and metabolic dysfunction.

That is a more cautious—and more scientifically useful—conclusion.

How to Read an Excessive Leucine Intake Study

If you encounter an excessive leucine intake study online, ask several questions before drawing a conclusion.

Was the research conducted in humans?

Human clinical research is generally more directly relevant to human dietary decisions than cell culture or animal studies.

Animal studies are still extremely valuable, particularly for investigating mechanisms that would be difficult to isolate in humans.

Was leucine isolated?

If researchers administered purified leucine, the study may tell you something about leucine signaling specifically.

It may not tell you what happens when leucine is consumed as part of a mixed meal.

How long was the exposure?

A short-term experiment cannot necessarily predict what happens after months or years.

Likewise, a chronic animal experiment may involve exposure levels that are difficult to compare with ordinary human eating patterns.

What was the metabolic state?

Was the model lean?

Obese?

Insulin resistant?

Physically active?

Sedentary?

These details can substantially change interpretation.

What happened to total energy intake?

Protein and leucine cannot be separated completely from overall energy balance when studying metabolic health.

What outcome was measured?

Researchers may measure mTORC1 activity, insulin signaling proteins, glucose tolerance, fasting glucose, insulin levels, or other markers.

These are not interchangeable endpoints.

A molecular change does not automatically equal a clinically meaningful disease outcome.

The Bigger Lesson From Leucine Dose Research

The leucine paradox illustrates a broader principle in nutritional science: the biological effect of a nutrient depends on more than whether the nutrient is "good" or "bad."

Dose matters.

Timing matters.

Duration matters.

Metabolic state matters.

The food matrix matters.

The rest of the diet matters.

Physical activity matters.

And the difference between an acute response and chronic adaptation matters enormously.

Leucine is a particularly useful example because it has such a clearly defined signaling role.

Its ability to activate mTORC1 is part of why it can stimulate muscle protein synthesis.

But that same pathway participates in feedback mechanisms that can influence insulin signaling when activation becomes chronically dysregulated.

That is not a contradiction.

It is physiology.

Frequently Asked Questions About Leucine and Insulin Resistance

Does too much leucine cause insulin resistance?

Research suggests that chronically excessive leucine or amino-acid exposure may contribute to impaired insulin signaling under certain conditions, particularly in experimental models involving metabolic dysfunction. However, there is not enough evidence to say that ordinary leucine consumption directly causes insulin resistance in everyone.

What is the connection between leucine and mTORC1?

Leucine acts as an amino-acid signal that helps activate mTORC1, a nutrient-sensing pathway involved in protein synthesis, cell growth, and nutrient metabolism. Temporary activation is normal and important. The research concern involves excessive or persistent activation in certain metabolic contexts.

Can high protein intake cause insulin resistance?

The evidence is mixed and depends heavily on the overall dietary pattern, protein source, energy intake, activity level, and metabolic health of the individual. High-protein diets should not automatically be equated with insulin resistance, and mechanistic findings involving leucine should not be interpreted as proof that all high-protein diets are harmful.

Is leucine good for muscle but bad for metabolic health?

That is an oversimplification. Leucine supports muscle protein synthesis and normal amino-acid signaling. Research raises questions about chronic nutrient-signaling excess, particularly in metabolically unhealthy conditions. The relevant issue is regulation and context, not whether leucine is inherently beneficial or harmful.

Are BCAAs linked to insulin resistance?

Elevated circulating BCAAs, including leucine, have been associated with obesity and insulin resistance in research. However, association does not establish that BCAA intake alone causes insulin resistance. Changes in amino-acid metabolism may also occur as part of metabolic dysfunction.

Should people avoid leucine-rich foods?

The research does not justify a blanket recommendation to avoid leucine-rich foods. Leucine is an essential amino acid and an important component of dietary protein. Questions about unusually high protein or amino-acid intake are best considered in the context of the person's overall diet, health status, activity, and nutritional needs.

The Leucine Paradox in Perspective

Leucine's reputation as a muscle-building amino acid is based on real biology.

So is the research examining what happens when nutrient signaling becomes chronically elevated.

Those ideas can coexist.

The most important distinction is between normal physiological activation and persistent metabolic dysregulation.

Leucine activates mTORC1. That is part of its usefulness.

mTORC1 supports protein synthesis and cellular growth.

But chronic nutrient excess can alter signaling networks, and sustained mTORC1 activity has been investigated as one mechanism that may interfere with insulin signaling.

The evidence becomes particularly interesting in the context of obesity and existing metabolic dysfunction, where nutrient sensing and insulin signaling may already be impaired.

At the same time, the research does not establish a universal leucine danger threshold, nor does it demonstrate that ordinary protein consumption inevitably causes insulin resistance.

That nuance matters.

Rather than asking whether leucine is good or bad, a better question is whether more of a nutrient signal is actually better when the body is already receiving abundant energy and nutrients.

For metabolic health, that broader question is far more informative.

The emerging lesson from too much leucine insulin resistance research is therefore not to fear leucine. It is to recognize that nutrition is a system of interacting signals.

Leucine can stimulate muscle-building pathways.

Those same pathways can participate in feedback mechanisms affecting insulin sensitivity.

Both statements can be true at the same time.

The real scientific challenge is understanding when beneficial signaling becomes excessive, how metabolic health changes that response, and how findings from mechanistic research translate into long-term human nutrition.

That is the leucine paradox—and why "more" should never be treated as synonymous with "better."

The information in this article is for educational purposes only and should not be considered medical advice. Always consult a qualified healthcare professional regarding dietary or health concerns.