What Is Type 2 Collagen? Benefits and How to Use

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What Is Type 2 Collagen? Benefits Plus How to Use

By Jill Levy

March 11,

Collagen is a structural protein that&#;s a key component of cartilage, bone and other tissues in both animals and humans.

Did you know that there&#;s actually more than one type of collagen? A little known fact is that there are at least 16 known collagen types, including type 1 and type 2.

What is type II collagen used for? As explained more below, this type is most abundant in sources including chickens and is associated with benefits including support for healthy joints, healthy skin and gut health.

What Is Type 2 Collagen?

Type 2 collagen is one type of collagen protein found in the human body that helps to build connective tissues, cartilage and bones. It&#;s made up of chains of amino acids like arginine, glutamine, glycine and proline.

Type II is the major collagen found in cartilage, helping to give cartilage its strength and elasticity. Cartilage is connective tissue that functions to protect the ends of bones and supports movement of joints. It also helps to form other body parts, including the ears, nose, the bronchial tubes and the rib cage.

What is type two collagen made from? It is found in high amounts in chicken cartilage (also called chicken collagen). Chicken cartilage can be synthesized and used in powdered collagen supplements and bone broth supplements.

Collagen type 2 can also be naturally obtained from drinking chicken bone broth, which is made with nutrient-filled animal parts such as bones, ligaments and connective tissue.

Type 1 vs. Type 2

A very high percentage of collagen in the human body, between 80 percent and 90 percent, consists of collagen type 1, collagen type 2 and collagen type 3.

Type 1 collagen accounts for most of the body&#;s supply. Type 1 is found in our skin, bones, tendons, corneas, blood vessel walls and other connective tissues. It&#;s made up of amino acids including proline, glycine and hydroxyproline.

Because it helps to build components of the skin that keep it strong and elastic, many people take collagen supplements featuring type 1 collagen to support healthy skin. You&#;ll find type 1 collagen in sources including bovine and marine/fish collagen.

Compared to other animal sources of collagen, chicken collagen is extremely high in type 2 collagen. It also inherently contains chondroitin and glucosamine, two compounds that help support healthy cartilage.

General Benefits of Type II Collagen

1. Supports Healthy Joints

How does collagen benefit joints? Type 2 collagen is the major component of joint cartilage, and because it comes from chicken collagen that is inherently loaded with joint-healthy chondroitin sulfate and glucosamine sulfate, it&#;s typically one of the most helpful collagen supplements for supporting joint comfort and mobility.

Type 2 collagen makes up about 50 percent of all protein in cartilage and 85&#;90 percent of collagen of articular cartilage. Healthy cartilage in our joints makes it easier to move and can, generally speaking, contribute to athletic performance and recovery, plus it allows our bodies to absorb shock and bear stress.

Collagen type 2 also contains amino acids that help form creatine, which promotes healthy muscle growth and supports healthy energy levels to power your workouts. Additionally, type 2 collagen can help to support strong bones, which further contributes to stability and mobility, especially as someone ages.

2. Supports Skin Health

Why is this collagen good for the skin? One reason is because it helps to support healthy cartilage, which is found under the skin of your nose, ears and elsewhere and gives your skin its structure and shape.

It also contains amino acids that stimulate cells in the skin and help with the natural growth and repair process. And not only can collagen type 2 support your skin, but also the health of your hair and nails, too.

3. Supports a Healthy Gut

Collagen for gut health is also backed by research. Amino acids found within collagen type 2 help support maintenance of tissues that form the gastrointestinal tract. This can support an overall healthy gut.

Best Type 2 Collagen Supplements

As mentioned above, you can obtain collagen type 2 by drinking real chicken bone broth, ideally that you make at home using high-quality ingredients, or by taking a collagen supplement that features type II collagen.

Most high-quality collagen supplements contain hydrolyzed collagen, which means the collagen peptides have been partially broken down to help with absorption. Once hydrolyzed, the amino acids in collagen become more bioavailable, which means your body can generally put them to work more easily.

Want a protein powder made of exclusively type 2 collagen? Look no further than Bone Broth Protein, which includes exclusively type II collagen along with glucosamine, chondroitin, hyaluronic acid and 19 amino acids. It also comes in multiple flavors, including chocolate and vanilla.

We consider this the top bone broth supplement on the market and don't consider it very close. In fact, it's three times more potent than homemade broth, twice as potent compared to the leading bone broth brands (based on protein content), and five times more than leading brands on micronutrients and macronutrients. 

Ancient Nutrition also makes a Multi Collagen Protein powder that provides you with 10 types of collagen (including type I, II, III, V and X) from four real food sources. Taking a supplement containing multiple types of collagen means you get an array of benefits.

Many folks, including Dr. Axe himself, take both Multi Collagen Protein and Bone Broth Protein daily to maximize the benefits for the joints, skin and gut.

How to Use

Making a type 2 collagen supplement a regular part of your routine is very simple. Of course, you should always consult your healthcare professional prior to starting any new dietary or supplement routine.

Bone broth and collagen powders &#; which are typically unflavored but also come in a variety of flavors &#; can easily be mixed into smoothies, soups and even baked goods. If you opt for an unflavored supplement, you&#;ll be able to get collagen&#;s health benefits without adding any taste to recipes like broth or stews.

A general recommendation is for most adults to take between 1&#;3 scoops/servings per day. However, you should always read label directions for suggested use.

Are you interested in learning more about hydrolyzed collagen type ii wholesalers? Contact us today to secure an expert consultation!

Multi collagen capsules are also available, which are extremely convenient to take daily either with or without a meal.

To get the most benefits from collagen supplements, pair collagen with certain nutrients and focus on eating a nutrient-dense diet that contains &#;collagen boosters&#; &#; including foods high in vitamin C, manganese, copper and antioxidants that help your body make and use collagen.

Final Thoughts

• Type II collagen is one type of collagen protein found in the human body that helps to build connective tissues, cartilage and bones.

• Supplements featuring chicken collagen, such as Bone Broth Protein powder, are brimming with type 2 collagen. Chicken collagen/type 2 collagen also inherently features chondroitin sulfate and glucosamine sulfate, which are both popular for supporting healthy joints.

• Type 2 collagen vs type 1, which is better? Both have their benefits, including supporting skin, gut and joint health. Type 1 is usually sought out for its skin-related benefits. Ideally, you&#;ll obtain a mix of both from a hydrolyzed multi-collagen protein supplement, such as Ancient Nutrition&#;s Multi Collagen Protein.

Jill Levy has been with the Dr. Axe and Ancient Nutrition team for six years. She completed her undergraduate degree in Psychology from Fairfield University, followed by a certification as a Holistic Health Coach from the Institute for Integrative Nutrition. Jill takes a &#;non-diet&#; approach to health and really enjoys teaching others about mindful eating, intuitive eating and the benefits of eating real foods.

Type II collagen is the most abundant protein found in articular cartilage and intervertebral discs. Because type II collagen is the main protein in cartilage, there have been suggestions that oral collagen supplementation may help to support cartilage repair. However, definitive proof for this is still lacking. Different formulations of collagen have been developed based on the degree of hydrolysis, the most prevalent being undenatured collagen and hydrolyzed collagen.

Nutraceutical supplements derived from collagen can be made from beef, pork, or fish bones and skins, which undergo processing to increase the bioavailability of their amino acids and/or peptides; the enzymatic hydrolysis of collagens enhances the postprandial absorption of its processed components [ 22 ]. Processed and pre-digested collagen products are called collagen hydrolyzates CHs and are sold in the form of collagen capsules at pharmacies and health food suppliers. Different processing and manufacturing methods to make collagen hydrolyzates can yield different products, with differences in amino acid content and peptide sequences that vary in molecular weight (MW). Lower MW peptides may be more easily absorbed in the small intestine, increasing the likelihood of delivery to other areas in the body such as joints (Fig. ).

These nutritional supplements are often a by-product from the food industry. Collagen supplements are rich in amino acids such as glycine, proline, and hydroxyproline; all of which play important roles in the building of joint cartilage and may also have anti-inflammatory and antioxidant effects, and have been speculated to act as signaling molecules [ 5 ]. While a seminal study published in Science in revealed efficacy of oral type II collagen supplementation in reducing joint swelling in RA [ 6 ], trials into the role of collagen supplementation in treating OA have demonstrated inconsistent results [ 19 &#;&#;]. There have been several reported analgesic and anti-inflammatory effects of collagen in unpublished clinical trials, but according to recently published systematic and narrative reviews, these have not been reproduced across studies [ 19 &#;&#;, 20 ]. Further trials with improved study designs are therefore needed to evaluate their proposed nutraceutical potential (Fig. ).

Whether UC-II, glycosylated or biochemically modified by some other means, has functional benefits beyond the provision of relevant amino acids as precursors for de novo collagen protein synthesis, will be an important area of research and innovation and exemplifies an opportunity for further evidence-based product development by consumer health companies. Work in this space will need to systematically correlate efficacy at reducing symptoms with mechanism of action, with adaptive trial designs and with many open questions remaining on the ability of UC-II to exert direct effects on cartilage metabolism in joints.

Undenatured type II collagen (UC-II) is a patented agent that is often derived from chicken cartilage and has been used in various clinical trials in humans and companion animals, including dogs and horses [ 23 &#; 25 , 26 &#;, 27 &#;]. Undenatured collagen is biochemically modified (glycosylated), has a good safety profile [ 28 ], and has been speculated, but not proven, to possess immunomodulatory properties. To what extent undenatured collagen is digested and absorbed following ingestion in vivo in humans remains to be assessed, but it has been speculated that potential bioactive peptides may be preserved and absorbed as free amino acids, especially glycine and proline. These amino acids represent quantitatively important precursors for the synthesis of cartilage extracellular matrix (ECM) macromolecules.

Hydrolyzed Collagen

Hydrolyzed collagen is a form of collagen that is also referred to as collagen hydrolyzate. Collagen hydrolyzate and gelatin may be the same in terms of amino acid composition, but they possess different chemical properties. Collagen is a native protein molecule with a molecular weight of ~300 kDa [29]; and collagen hydrolyzates are processed intensively to break up the large collagen molecules into smaller fragments to increase absorption (Fig. ).

To produce hydrolyzed collagen, native collagen undergoes denaturation followed by a hydrolysis process, resulting in very low molecular mass (3&#;6 kDa) collagen peptides, compared to native collagen size (285&#;300 kDa) [29]. Different processing and post-processing methods to make collagen hydrolyzates can yield vastly different products, creating different collagen peptide sequences and molecular weights. These differences can potentially impact biological function in terms of regulating joint inflammation and effect on subchondral bone. Furthermore, lower molecular weight collagen peptides may be more easily absorbed in the small intestine, theoretically increasing the likelihood of being delivered to other areas in the body including joints. The resistance of collagen peptides to hydrolysis and digestion is primarily based on amino acid composition. In that regard, peptides with the amino acid proline or hydroxyproline are not readily hydrolyzed, or digested by the gastrointestinal system which may allow them to be absorbed in the small intestine. In support, peptides such as Pro-Hyp and Pro-Hyp-Gly, derived from the repeating motif Pro-Hyp-Gly, have been reported to circulate in the blood up to 4 h after oral collagen and gelatin ingestion [30, 31]. Thus far, there are no published studies that have conducted a quantitative assessment of the actual quantity of collagen derived peptides that are absorbed in the gastrointestinal tract and/or released in the circulation.

A number of clinical trials have been conducted concerning oral supplementation of collagen and its derivatives, undenatured and hydrolyzed collagen. All have shown to be safe and tolerable for the patient, causing no or only mild adverse effects to some patients [32, 33]. One of the concerns regarding oral collagen supplementation is associated with oral tolerance. Oral tolerance is the ability of orally administered antigen to suppress or minimize the immune response, and has been used to manage the occurrence of immunogenicity in other disease areas [34&#;39].

As for oral tolerance associated with collagen, the response relies on structural properties of the collagen derivative because only specific epitopes found in an intact helix structure of the undenatured collagen are recognized by the immune system. The epitopes interact with gut-associated lymphoid tissue (GALT) and result in reduction of systemic T cell attack on the cartilage as well as reduced joint inflammation and cartilage damage [40&#;42]. This suggests that, if taken orally, hydrolyzed collagen is digested and broken down into small peptides and amino acids, thus potentially eliminating its immunomodulatory properties.

Due to its lower molecular weight, hydrolyzed collagen has been proposed to have higher bioavailability and solubility, and thus better absorption from the small intestine compared to undenatured collagen [22, 29]. Absorption of orally administered hydrolyzed collagen has been evaluated by studying vascular-perfused rat intestine in situ. The results implied that the breakdown products of hydrolyzed collagen digestion can be absorbed as small peptides [43]. Defining and understanding the difference between collagen products, collagen hydrolyzates, and ultrahydrolyzed collagen can be difficult, confusing, and remains unclear in the literature.

Studies evaluating collagen digestion and amino acid and/or peptide absorption in vivo in humans are required to address the proposed differences in the postprandial bioavailability of collagen-derived amino acids and peptides.

In vitro studies have been used to suggest that collagen derived peptides may: (a) potentially accumulate in cartilage (if given in sufficiently high doses); (b) stimulate chondrocytes to synthesize ECM macromolecules in vitro; and (c) increase osteoblast activity as well as decrease osteoclastic activity [44&#;, 45, 46&#;48]. However, whether such peptides are actually absorbed and released in an in vivo setting remains highly speculative. Further studies are required to identify such absorbable bioactive peptides derived from (hydrolyzed) collagen digestion, as the impact of digestion and first pass metabolism on the generation of bioactive peptides from collagen hydrolyzates remains to be investigated. Such research may help to identify peptides and amino acids contributing to the proposed antioxidant and anti-inflammatory properties of collagen hydrolyzate supplementation. In this regard, preclinical research using innovative simulated digestion models in combination with relevant cell/tissue cultures can become an innovative higher throughput platform for investigating new collagen hydrolyzate formulations.

The early papers that appeared on collagen hydrolyzates reported efficacy in the preclinical context (beneficial effects on cartilage metabolism) and improvements in joint pain in the clinical context. Bello and Oesser reviewed the available literature on collagen supplements without date limits and published their results in [44&#;]. In addition to published papers, they included abstracts presented at scientific congresses and articles published in German medical journals [44&#;]. They reported that orally administered collagen hydrolyzate end products can be taken up by the intestine and accumulate in cartilage [44&#;]. They also proposed that collagen hydrolyzate ingestion can stimulate the synthesis of ECM macromolecules. Bello and Oesser identified four open-label and three double-blind studies. Although some of these clinical trials were of very low quality, they reported that collagen hydrolyzates are safe and may improve pain and function in men and women with OA and other arthritic conditions. It is important to note, however, that the authors included other joint diseases in their review and their focus was not exclusively on OA.

In a trial investigating hydrolyzed collagen and green tea extract supplementation in dogs, the combined treatment decreased indicators of pain in dogs that received the combination product for 3 months. However, the biomarkers selected for evaluation of the effects of supplementation (Coll2&#;1 and Coll2&#;1 NO2) were unaffected [49].

An equine study from Utrecht University examined the effect of supplementation with collagen hydrolyzates and a multi-ingredient supplement for 60 days on experimentally induced acute synovitis in horses [50]. Synovitis was induced in the right intercarpal joint by intra-articular injection of 0.5 ng lipopolysaccharide (LPS) of Escherichia coli. Although supplementation with collagen hydrolyzates and the combination product showed anti-inflammatory effects in this validated synovitis model and prostaglandin E2 (PGE2) levels were reduced compared with placebo, no statistical differences were seen with respect to interleukin 6 (IL-6), glycosaminoglycans (GAGs), the biomarker CPII, or matrix metalloproteinases (MMPs) among treatment groups.

A supplement called PETAGILE, which provides collagen peptides, was orally administered to horses with mild or moderate OA for 3 months with daily doses of 25 g and 50 g. A weekly questionnaire to horse owners was provided in order to follow the progress of horse behavior and willingness to run. All 28 horses, (16 received 25 g/day and 12 received 50 g/day of PENTAGILE), improved their mobility and showed increased willingness to run when compared to the placebo group. The higher dosage (50 g) supplementation was concluded to be more effective and promising enough to further test in longer term studies [51].

Clark and colleagues performed a 24-week clinical study on the use of collagen hydrolyzates as a dietary supplement in 147 healthy athletes with activity-related joint pain who were physically fit, active, and had no evidence of joint disease [52]. The study design involved 72 males and 75 females randomly assigned to two groups. The experimental group (n = 73) received 25 mL of a liquid formulation of 10 g of collagen hydrolyzates. The placebo group (n = 74) received 25 mL of liquid xanthan. The primary measured outcome was a change in the visual analog scales (assessed by a physician) from baseline during the study phase in relation to pain, mobility, and inflammation. The team investigated joint pain at rest and when walking, standing, carrying objects, and lifting. This was the first clinical trial that used a healthy population as a study group and showed improvement in joint discomfort and pain in the group given an oral supplement containing collagen hydrolyzates. Despite the small sample size and limitations of the study, the results suggested that athletes perceived a benefit from consuming collagen hydrolyzates [52].

A clinical study in 15 healthy male subjects was carried out to determine and compare the plasma concentrations of four representative amino acids from collagen (glycine, proline, hydroxyproline, and hydroxylysine) following a single administration of a fresh fermented milk product containing hydrolyzed collagen [53]. This was a single-center, randomized open crossover study. In a fasting state, the 15 healthy subjects randomly received a single dose of product 1 (10 g of collagen hydrolyzate in 100 mL of milk) or product 2 (10 g of collagen hydrolyzate dissolved in 100 mL of water). The study showed that consumption of milk containing collagen hydrolyzate increased the concentration of collagen-specific amino acids in plasma. This suggests that orally ingested collagen hydrolyzates might increase the plasma concentrations of collagen-derived amino acids that could potentially reach tissues in the synovial joint.

Another clinical trial used a randomized double-blind, controlled study design and recruited 250 subjects with primary knee OA to assess the efficacy of a collagen hydrolyzate supplementation on OA pain and function [54]. The patients were given 10 g collagen hydrolyzate daily for 6 months. The authors reported a significant improvement in knee joint function and pain as assessed by visual analog scales as well as the the Western Ontario and McMaster Universities Osteoarthritis Index (WOMAC) pain subscales. Subjects with the greatest joint deterioration, and with the lowest intake of meat protein in their diets, appeared to benefit the most. The study concluded that collagen hydrolyzates are safe and effective and warrant further consideration as a functional food ingredient [54].

McAlindon and colleagues performed biochemical and imaging studies to examine the effect of collagen supplementation in human patients with OA. They attempted to determine whether either of two MRI approaches, delayed gadolinium enhanced magnetic resonance imaging of cartilage (dGEMRIC), or T2 mapping, might detect short-term changes in knee cartilage among individuals taking a formulation of collagen hydrolyzates. Their early results suggest that the dGEMRIC MRI technique may be able to detect changes in proteoglycan content in knee cartilage in individuals taking collagen hydrolyzate after 24 weeks compared to placebo [55]. Only weak correlations were observed between changes in dGEMRIC and biochemical markers, suggesting that the study duration was insufficient to detect measurable changes in biomarkers or that the biomarkers they selected were insufficiently sensitive and discriminatory. They found a positive effect of collagen hydrolyzates on cartilage morphology in patients with knee OA in their interventional OA study (ClinicalTrials.gov: {"type":"clinical-trial","attrs":{"text":"NCT","term_id":"NCT"}}NCT) [56]. However, they could not identify any consistent correlations in changes in collagen and proteoglycan biomarkers PIIANP and CS846 with changes of the dGEMRIC scores in patients who had received oral collagen hydrolyzates. An important weakness of this study was that the authors were looking for short-term changes which are difficult to detect, even after 48 weeks of oral treatment with collagen hydrolyzates. Although the study was time limited, the dGEMRIC score increased in the medial and lateral tibial regions of the knee joint in participants who were given collagen hydrolyzate compared to placebo.

A systematic review published in examined the evidence on the symptomatic and chondroprotective effects of collagen derivatives in OA. They reported that there is insufficient evidence to recommend the generalized use of collagen hydrolyzates in daily practice for the treatment of patients with OA [57]. They proposed that the overall quality of evidence was moderate to very poor and recommended more independent and high-quality studies to assess the proposed therapeutic effects of collagen derivatives on OA. It is important to note that they did not include studies on only collagen hydrolyzates; they reviewed the evidence from eight different studies: six on collagen hydrolyzates, two on gelatin, and one on undenatured type II collagen (UC-II). As previously mentioned, processing of collagen and their hydrolyzates may result in formulations with differing peptide and amino acid profiles, which may affect patient outcome.

A study published in examined the metabolic responses of human OA cartilage to biochemically characterized and fractionated collagen hydrolyzates [58]. It compared three different collagen hydrolyzates, two from fish (Peptan® F , Peptan® F ) and one from pigs (Mobiforte®) and used biochemical (fluorescence) and biophysical techniques to characterize the products and their effects on human OA cartilage. It also determined the total number of peptides within each product and the peptides that were common between them. The investigators found that none of the three collagen hydrolyzates had the ability to positively modulate collagen biosynthesis in human knee cartilage explants. The authors noted that Peptan® F enhanced the activities of aggrecanases ADMATS4 and ADMATS5 in vitro. Furthermore, IL-6, MMP-1, -3, and -13 levels were elevated in explants that were treated with Mobiforte® and Peptan® F . This study concluded that due to the heterogeneous peptide composition and disparate pharmacological effects among different collagen hydrolyzates, the effect of a particular preparation or processing cannot be extrapolated to other formulations.

Although there are promising collagen hydrolyzates, the literature has been riddled with poorly designed and executed studies decreasing the credibility of published material, even though positive effects have been demonstrated. For example, another poor study on fish collagen hydrolyzates was published by a group based in Thailand. This group claimed that collagen hydrolyzates can modulate cartilage metabolism [59]. Despite being published, the study was fundamentally flawed because the authors only looked at the effects of collagen hydrolyzates on cartilage explants. Knowing that the explant model is not always suitable for mechanistic studies of hydrolysate action, the results from this study should be interpreted with caution.

The most recent systematic review and meta-analysis of dietary and botanical supplements for OA looked at the evidence supporting the use of collagen hydrolyzates define and UC-II. Although their analysis showed significant improvements on pain, the quality of the published evidence was low and thus the clinical studies were deemed to have limited clinical impact [19&#;&#;]. The poor quality of published literature highlights the many knowledge gaps regarding collagen-based nutraceuticals, which require further high-powered and well-designed studies to propose evidence-based recommendations.

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