Tendon & Ligament - Joint Support

Tendon & Ligament provides vital support for the 4 physical attributes all elite athletes require for success. While most joint products maintain the state of the joint. Tendon & Ligament helps build, strengthen, and support joint components to sustain an athlete's functional strength. It goes beyond the joints to further support overall healthy skin and connective tissue.*

  • Stronger and more solid foundation*
  • Strong connective tissue*
  • Secure joint structure*
  • Increased elasticity*

Improve flexion and compression at vital pivot points!*

• Performance

What's more, connective tissues and joint structures such as muscle, bone, and cartilage require certain nutrients to assist in building and supporting overall health.* Tendon & Ligament performance provides these nutrients in 3 ways:

1. Build*

  • UCII, an undenatured type II collagen protein, supports joints from the inside out. Type II collagen is the primary collagen found in human cartilage and thus becomes an important component in supporting healthy joints.*

2. Lubricate*

  • Hyaluronic acids' (HA) capability to swell and retain water allows the support of cushioning and lubricating the moving parts within the joints. This supports more effortless joint movement in the athlete.*

3. Strengthen*

  • Specialized collagen protein supports the strengthening of connective tissue and bone. It is an excellent source of amino acids (building blocks of protein), strengthening the tendons and ligaments around the joints, which is crucial for stability and ultimately function of the joints.* 
• Scientific Support

Date: 2012 Active Ingredients (per serving):
Collagen Type I (11g)
Collagen Type II (40 mg)
Hyaluronic acid (20 mg)

Maintaining the structures of bones, ligaments, tendons, and joints is essential in the physical performance of athletes as is the upholding of nutrients required to support these structures.

Collagen is a term for proteins forming a characteristic triple helix of three polypeptide chains. All these structures are formed in the extracellular matrix. However their size, function and tissue distribution varies considerably. So far up to 28 types of collagen types have been identified to date in the body (Gelse 2003; Shoulders 2009). Collagen is the main structural protein found in the human body (Gelse 2003; Kadler 1996) and a total of about 25-35% of the total protein composition in the human body is comprised of collagen (Gelse 2003; Yalovac 2007). Collagen is especially found in bone, muscle, tendons, ligaments, cartilage, skin and other connective tissues (Gelse 2003).

The different collagen types have complex and diverse structure and functionality due to additional structural domains and folding (Gelse 2003; Shoulders 2009). About 90% of total collagen comes from fibril-containing collagens. Collagen Type I and V primarily contribute to the structural make-up of bone. Collagen Type II and XI primarily contribute to the articular cartilage matrix. The tensile strength and torsional stability renders these tissues with stability and integrity (Birk 1988, Gelse 2003, Mayne 1989 von der Mark 1999). Other collagens might be more flexible such as the collagen found in the cartilage of our ears (Gelse 2003), or interwoven with other collagen to create various sorts of networks (Gelse 2003, von der Mark 1984).

Although there are many structural variations among the identified collagens they all have one characteristic among them: they all have a right-handed triple helix composed of three identical chains (such as in Type II collagen) or they have two or more different chains (such as collagen Type I) (Gelse 2003; Kadler 1996; Kühn 1986, Piez 1984). Each of the 3 a-chains is composed of 18 amino acids and rotate in a left-handed manner. The three chains are then super-coiled around each other to form the right-handed triple helix (Fraser 1979, Gelse 2003, Hofmann 1978,).

Fibril-Forming Collagen

The classical fibril-forming collagens include types I, II, III, V, and XI. Fibrillar collagens are characterized by their ability to pack into tightly oriented aggregates with a staggered pattern (Gelse 2003; Shoulders 2009). It has been said that healthy fibrillar collagen is stronger than steel (REF). For the sake of space and interest only Collagen Type I and II will be discussed below.

FACIT Collagens

Various collagen types (IX, XII, XIV, XVI, XIX, and XX) belong to the Fibril-Associated-Collagens with Interrupted Triple helices (FACIT) (Gelse 2003). These structures have collagenous domains which are interrupted by short non-helical domains and they are usually associated with the surfaces of various fibrils. For example, Collagen Type IX is associated with Type II fibrils in an anti-parallel direction (Gelse 2003, von der Mark 1999, Wu 1995) in cartilage and the vitreous body of the eye (Gelse 2003, von der Mark 1999). This allows for the interaction of proteoglycans and other matrix components such as chondroitin sulfate (Gelse 2003, Mayne 1989, van der Rest 1988, Yada 1990).

Other Collagens

There are many more collagen types found in the body. These include network-forming collagens, anchoring fibrils, transmembrane collagens, basement membrane collagens, etc. (Gelse 2003). They all maintain the structural integrity of tissue and organs in the human body.

Collagens also are also involved in cellular microenvironment. Due to their binding and network-forming/anchoring capacity, they are involved in cell signaling of adhesion, differentiation, growth, cellular re-activities as well as contribute to the formation and promotion of tissue repair and regeneration (Frenkel 1997, Gelse 2003; Schuppan 1998, Wakitani 1989). They also bind to growth factors and cytokines and thus might play a role in organ development (Gelse 2003, Hay 1981, Yamaguchi 1990).


Type I Collagen

Collagen Type I is one of the most important stress-carrying protein structures in the humans (Fratzl 1997). This collagen type is the most common and abundant form and forms >90% of the organic mass of bone. It is the major type of collagen in tendons, ligaments, skin, cornea of the eye, interstitial connective tissues, and arterial walls. It also makes up scar tissue and can be found in teeth (Di Lullo 2002; Gelse 2003).

The triple helix usually comprises of two identical a1-chains and one slightly different a2-chain and is usually incorporated together with either collagen Type III (as in the skin) or collagen type V (as in bone, tendon, and cornea) (Fleischmajer1990; Gelse 2003; Kadler 1996; Niyibizi 1989; Shoulders 2009). This protein has an atypical amino acid composition because it is relatively high in the amino acid hydroxyproline. The collagen molecule (also known as tropocollagen) is a subunit of the larger aggregates such as fibrils. Each tropocollagen has a left-handed rotation helix and three of these are twisted together to form the right-handed triple helix we all know with a length of about 300nm and about 1.5 nm in diameter (Kadler 1996; Makaareva 2007). This triple helix is stabilized by numerous hydrogen bonds and then further twist together with other triple-helices to form a microfibril (Perumal 2008).

A distinct feature of each tropocollagen is the regular amino acid arrangement of Glycine-Proline-XXX or Glycine-XXX-Hydroxyproline, where XXX is any other amino acid. The high Gly content allows the three helices to tightly wind around each other and facilitate hydrogen bonds as well as molecular cross-links between the molecules. Due to the high concentration of proline and hydroxyproline the geometrical constraint shows a tendency of the tropocollagen to have a left-handed rotation and the subunits to self-assemble. In the triple helix, glycine is in the interior towards the middle and the Pro and Hydroxy-Pro side chains are facing the outside (Yalovac 2007).

Collagen Type I provides tensile stiffness especially in tendons and fascia. In bone it defines the biochemical properties regarding load bearing, tensil strength, and stiffness especially after mineralization. Here the collagen triple-helices are arranged in a parallel and staggered pattern. The small gap at each end of the tropocollagen subunits most likely serves as a nucleation site for depositing calcium minerals (Ross 2011).

 Collagen acts to transmit forces and dissipate energy and one of the important mechanical characteristics of collagenous tissue such as tendons and ligaments is its ability to store and transmit energy elastically during mechanical deformation (Pins 1997). Tendons are the energy transfer bridge between contracting muscles to bone, with the result of movement of the extremity. During normal gait, the body decelerates as the foot lands on the ground, causing kinetic energy to be stored in the stretched muscles and tendons. Elastic recoil in the tendons converts most of the energy into kinetic energy as the foot leaves the ground and the circle is complete (Freeman 2005, Silver 2001).

Ligaments absorb energy during the movement in order to protect joints from damage. For example the anterior cruciate ligament (ACL) absorbs energy during movement that could lead to anterior translation of the tibia, and thus prevents knee damage.

As the collagenous tissues are cross-linked and mineralized the energy storage ability of the tissue can be altered (Freeman 2005, Silver 2000).

Type II Collagen

Hyaline cartilage (as seen in joints) contains around 50-80% predominately Collagen Type II fibrils (Gelse 2003; Shoulders 2009). Type II Collagen can also be found in the vitreous body, corneal epithelium, nucleus pulposus of intervertebral discs, and embryonic epithelial-mesenchymal transitions (Gelse 2003, von der Mark 1999). The triple helix comprised of three identical chains to form a helix that is similar in size and biomechanical properties as Collagen Type I (Bruckner 1994, Gelse 2003). Cartilage also contains collagen types IX and XI to limit the size potential of collagen type II fibrils diameters (Gelse 2003, Mendler 1989, van der Rest 1991). Type II collagen contains a higher concentration of hydroxylysine as well as glycosyl and galactosyl residues. These mediate the interaction to proteoglycans, another important component of highly hydrated hyaline cartilage (Gelse 2003; Mayne 1989).

Cartilage-Bone Interface

The purpose of the cartilage-bone interface in the joint such as the knee, is to maintain structural integrity during physical movements such as walking, kneeling, running, pivoting, jumping, etc. (Hoemann 2012). At those moments tensile, compressive and shear forces are transmitted from the articular cartilage, which is more viscoelastic, to the much stiffer mineralized end of the bone. Articular cartilage is attached to the subchondral bone through a 20-250 mm thick layer of calcified cartilage and the type II collagen fibers become structurally cemented to type I collagen osteoid deposited by osteoblasts (cells responsible for bone formation).

Hyaluronic Acid

Hyaluronic acid (HA) is the largest non-sulfated glycosaminoglycan (GAG; a polymer of D-glucuronic acid + N-acetylglucosamine) which is primarily found in connective, epithelial, neural tissue, and synovial fluid (Armstrong 1997; Hong 2004). It is one of the main components of extracellular matrix as well as synovial fluid where it increases viscosity and is together with lubricin one of the fluids lubricating component. It is an important component of joint cartilage, where it interacts with chondrocytes. It is a negatively charged protein and forms aggregates that bind water and are responsible for the resiliance of cartilage (Toole 2000).

Cell receptors for hyaluronic acid have also been identified and so far fall into three categories: CD44, Receptor for HA-mediated motility (RHAMM) and intracellular adhesion molecule-1 (ICAM-1). CD44 and ICAM-1 are already known as cell adhesion molecules with other recognized ligands before their HA binding was discovered. CD44 is widely distributed throughout the body, and the formal demonstration of HA-CD44 binding was proposed by Aruffo et al. in 1990. To date, it is recognized as the main cell surface receptor for HA. CD44 mediates cell interaction with HA and the binding of the two functions as an important part in various physiologic events, such as cell aggregation, migration, proliferation and activation; cell-cell and cell-substrate adhesion; endocytosis of HA.

ICAM-1 is known mainly as a metabolic cell surface receptor for HA, and this protein may be responsible mainly for the clearance of HA from lymph and blood plasma, which accounts for perhaps most of its whole-body of this receptor, thus, triggers a highly coordinated cascade of events that includes the formation of an endocytotic its fusion with primary enzymatic digestion to active transmembrane transport of these sugars to cell sap, Like its name, ICAM-1 may also serve as a cell adhesion molecule, and the binding of HA to ICAM-1 may contribute to the control of ICAM-1-mediated inflammatory activation.

The major difference in biological activities is attributed to its variable molecular weight. There are clear molecular weight cut-offs for HA's lubricating properties, cell-signaling, and efficacy for joint support. Molecular weight of less than 500 kD seems to be the magic cut-off target number (Camenisch 2000). Very low MW HA fragments either do not bind to specific cell membrane receptors that recognize native HA or they transduce different signals to cells (Bucci 2004). The molecular weight between 700,000 and 1,000,000 is used in Tendon & Ligament. The majority of in vitro and animal research showed stimulated synthesis of HA from human osteoarthritic synovial fibroblasts and anabolic reactions in extracellular matrix components (proteoglycan synthesis, enhanced chondroitin proliferation and synthesis, improve bone mineralization, decrease cartilage degradation, antioxidant activity, regulatory function, etc.) (Bucci 2004).



Clinical studies investigating the effects of hydrolyzed collagen have been done for a few decades (Bello 2006). Hydrolyzed collagen is a source of bioavailable peptide fragments and a rich source of the important amino acids for tendons, ligaments and bones, i.e. glycine, proline, hydroxyproline, lysine, and hydroxylysine. Absorption studies in both animals and humans (at amounts found in Tendon & Ligament) have shown that hydrolyzed collagen is readily absorbed throughout the body and supplies collagen-containing tissues with these building blocks (Oesser 1999).

Absorption studies of hyaluronic acid (HA) have also been done in animals and shows that HA is preferably taken up in joints and skin (Balogh 2008; Schauss 2004) as well as liver, spleen, bone marrow and lymph nodes (Fraser 1983; Fraser 1989; Westerberg 1995. The human body metabolizes large quantities of HA daily as well as have a large capacities to remove HA from the bloodstream (Fraser 1984; Fraser 1986; Fraser 1989; Laurent 1992; Lebel 1994; Lindqvist 2000).

With the combination of Collagen Type I, HA and Collagen Type II a solid foundation is laid that provides the necessary building blocks to sustain bone, tendons, ligaments, and cartilage. Thus all the building blocks are there to maintain and build a stronger and more solid foundation for athletic performances.


Fernandez and Perez (1998) investigated the effects of 10g of hydrolyzed collagen on shoulder and knee joints in healthy male competitive mountain bikers during a six-month trial. Biometric ultrasounds of the cartilages showed statistically significant increases in cartilage thickness, whereas the controls showed no or decreases cartilage thickness. In another study 84 German athletes with painful knee, hip, and shoulder joints were examined for 12 weeks after ingesting 10g/d hydrolyzed collagen. The results showed decrease in knee, hip, and shoulder pain at rest and during test exercise (Flechsenhar 2005). Another research group investigated the effects of 10g of hydrolyzed collagen in healthy and physically active at club levels complaining of joint pain or discomfort (Clark 2008). After 24 weeks of treatment this randomized, placebo-controlled, double-blind study showed significant improvement in joint pain using a Visual Analogue Scale. In vitro tissue culture studies have shown that in the presence of hydrolyzed collagen joint chondrocytes were able to stimulate type II collagen biosynthesis over the 11 day testing period. This suggests that hydrolyzed collagen might have a stimulatory effect on type II collagen biosynthesis of chondrocytes (Oesser 2003).

Undenatured Type II Collagen, called UC-II from Inter Health N.I., is a patented ingredient derived from chicken sternum cartilage. During manufacturing native epitopes of collagen type II are preserved and remain immune-reactive as it passes through the gut to the small intestine where the Peyer's Patches absorb them (Bagchi 2002). Once in the lymphoid tissue UC-II works together with the immune system to modulate the breakdown of joint cartilage and prevent degradation of type II collagen in the joints as well as support rebuilding of cartilage. Collagen specific, regulatory T-cells migrate to the joint areas and modulate the ongoing local inflammatory responses. Collagenase secretion by macrophages is slowed down and the production of inflammatory cytokines as well. As inflammation reactions subside, the imbalance of cartilage turnover appears to shift in favor of normal cartilage rebuilding (Bagchi 2002; Hu 2003; Nagler-Anderson 1986; Park 2009; Prakken 2004).

Many studies have been performed in animals (Thompson 1985, Zhang 1990), especially horses and dogs with arthritis (D'Altilio 2007, Deparle 2005; Gupta 2009). All studies show vast improvements in clinical symptoms of arthritis. In a randomized, double-blind, clinical study using the same amount of UC-II as found in Tendon & Ligament 52 subjects with knee osteoarthritis where supplemented for 90 days and compared to a group supplemented with 1500 mg glucosamine + 1200 mg chondroitin (GC group: the standard supplementation). Total WOMAC scores declined by 33% as compared to 14% in the GC group and was 2x more effective in promoting joint comfort, flexibility and mobility compared to baseline. UC-II was 70% more effective at 30 days than GC (Crowley 2009).

Other studies have also investigated the effects of UC-II in human subjects with arthritis and found that undenatured type II collagen improved arthritis symptoms significantly (Barnett 1998; Trentham 1993; Wei 2009, Zhang 2008)


With improvement in the articular components using collagen type I (Bello 2006; Clark 2008; Fernandez-Perez 1998; Flechsenhar 2005; Oesser 1999), undenatured Collagen Type II (Bagchi 2002, Barnett 1998; Crowley 2009; Hu 2003; Nagler-Anderson 1986; Park 2009; Prakken 2004; Trentham 1993; Wei 2009; Zhang 2008), and hyaluronic acid (Balogh 2008; Fraser 1984; Fraser 1986; Fraser 1989; Laurent 1992; Lebel 1994; Lindqvist 2000; Schauss 2004), the joints become a healthier place. Healthier joints mean healthier overall function. With Tendon & Ligament, the structural components of the joints such as the tendons, ligaments and bone receive the proper nourishment and building blocks to regenerate and maybe even repair and thus secure the joint structure better and more efficient.


Tendon & Ligament provides all the building blocks for a stronger and more solid foundation, stronger connective tissue, increased elasticity and thus secure joint structure for athletes. It creates a healthier environment within and around joints by targeting bones, ligaments, tendons, cartilage and the synovial fluid.

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* These statements have not been evaluated by the Food and Drug Administration. This product is not intended to diagnose, treat, cure, or prevent disease.

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