Campus Training *Is* Connective Tissue Training

Campus Training *Is* Connective Tissue Training

March 05, 2019

Since its invention in the late 1980s, by the late, great Wolfgang Güllich, campus training has become recognized as an essential training modality for advanced climbers. The unique value of the campus training, over hangboard training or just climbing, is the remarkable power gains that result from both short-term acute training interventions and over the long term (i.e. many years of incrementally harder campus training).

A distinctive characteristic of campus training is that you get stronger and more powerful without putting on any muscle massexactly what an elite climber seeks! Assuming you have excellent technique and mental game, then pursuing your genetic potential in largely a matter of increasing strength- and power-to-weight ratio season over season.

Unique Stimulus Unique Adaptations

So what is the unique stimulus and adaptation that makes campus training so valuable? All along, us coaches and climbing scientists assumed the power gains were mostly the result of neurological adaptions (motor unit synchronization, increased rate coding, etc.), since muscle hypertrophy was clearly not an adaptation that resulted from campus training. Now three decades after the invention, we have come to realize that remodeling and stiffening of tendons and muscle extracellular matrix is likely the more important and longer-tail adaptation to an appropriate campus training program. 

Recent studies have discovered that while the tendon core changes little between the ages of 17 and 70, the outer part of the tendon (paratenon) is dynamic and metabolically active. Chronic appropriate training can lead to very gradual tendon hypertrophy (over many months, years, and decades), while rapid, forceful mechanical loading—as in campus training—leads to an increase in enzymatic cross-linking of collagen molecules (over weeks, months, years) which increases tendon and ECM rigidity. In aggregate, increased tendon cross-sectional area and cross-linking results in a stronger, stiffer tendon that will elevate performance and reduce injury risk.

It's also important to recognize that tendon structure is tightly coupled to the architecture of the muscle. Optimal function (and injury resistance) of the muscle-tendon system requires an exquisitely tuned viscoelastic structure in which tendon stiffness and muscle strength upscale together. At the myotendinous junction, the tendon fibers fan out like a river delta and extend throughout the length of the muscle in a scaffold-like fashion. Within the muscle, extracellular matrix forms a honeycomb-like structure that groups contractile fibers together and facilitates lateral force transfer to “scaffold” and then to tendon and bone, while protecting individual fibers from exercise-induced damage.

Whereas the classic textbook model for muscle force transfer is one of longitudinal transfer, from sarcomere to sarcomere through the full length of the muscle, recent research has shown that up to 80 percent of muscle force arrives at the tendon via lateral force transfer through the extracellular matrix. Efficient lateral force transfer reduces micro tears in contractile fibers (less delayed onset muscle soreness) and increases the rate of force development and power. These findings underpin the multiple and profound long-term benefits of regular, appropriately scaled campus training.

Feed Extracellular Matrix Just As You Feed Tendons and Ligaments

It's important to note that just as with your tendons and ligaments, collagen is the principle constituent of extracellular muscle matrix. At the heart of these collagen-based structures is a triple helix with a repeating sequence of glycine, proline, and any other amino acid. Consequently, inadequate daily intake of glycine and proline may compromise collagen synthesis in connective tissues and extracellular matrix. Obviously, this is not a trivial matter for a serious athlete; especially when you consider that the requirements of proline for whole-body protein synthesis are the greatest among all amino acids. Furthermore, glycine is a conditionally essential amino acid because humans are unable to synthesize enough glycine to satisfy metabolic requirements. The average adult requires nearly 12 grams of glycine per day to synthesize collagen, yet the body can only make about 2.5 grams per daythis suggests that humans require nearly 10 grams of dietary glycine per day.

So what are the best sources of glycine and proline?

  • Foods that are high in glycine - gelatin, pork, fish, soy isolate, turkey, chicken, egg white, beef, seeds, peanut butter, and seaweed.
  • Foods that are high in proline - gelatin, cottage cheese, milk, beef, egg white, soy protein, cheese, and cabbage.

If these foods aren't on your pre-workout diet (I doubt they are!), you can thankfully consume a scoop of Supercharged Collagen to spike your blood levels of glycine and proline just as you engage the campus board, hangboard, or climbing wall!



Supercharged Collagen has no peer when it comes to promoting collagen synthesis in connective tissues and strengthening muscle extracellular matrix. Consume 1 to 1.5 scoops, mixed into your favorite beverage, 30 to 60 minutes before training to optimally feed your connective tissues and promote post-workout collagen synthesis.

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