Collagen & strength training: How much do you really need for optimal tendon and joint health?

More is better – at least when it comes to supplementing collagen.

Lee and colleagues investigated the influence of different collagen doses on collagen synthesis after intensive strength training. It is already known that strength training stimulates collagen synthesis - but can additional collagen intake enhance this effect?

The study protocol: Four sets of squats!

The test subjects, all young men with training experience, took either a placebo or 15 g or 30 g of hydrolyzed collagen and then started lifting weights one hour later. After completing four sets of barbell squats with 10 repetitions each (10 repetition maximum), the guinea pigs... er... study participants were allowed to rest for 6 hours while the scientists took several blood samples from them during this period.

The markers examined: Attention, technical jargon!

The concentrations of two markers for collagen synthesis and collagen degradation were determined in the blood: PINP and ß-CTX. The abbreviations stand for procollagen type I N-terminal propeptide and β-isomerized C-terminal telopeptide of type I collagen, for those who want to know exactly.

PINP is a peptide that is split off from procollagen (the precursor) during the formation of collagen. If more PINP is found in the serum, this means that more collagen has been formed. ß-CTX is a marker for collagen degradation. As in our muscles, the processes of building up and breaking down are in constant competition. If the build-up exceeds the breakdown, the thickness and density of the tendons increases.

Conclusion: More is better!

The study result was clear: The highest collagen dose of 30 g resulted in a significantly higher PINP concentration in the blood serum than the other two interventions, while all three interventions (strength training + 0 g, 15 g, 30 g collagen) were equally able to reduce collagen degradation.

As expected, the intake of 30 g of collagen led to the highest blood concentrations of the amino acids relevant for collagen synthesis, such as glycine and proline. The authors conclude that the amount of amino acids supplied seems to play an important role in optimizing collagen synthesis.

This observation is consistent with that of de Paz-Lugo and colleagues from 2018. The authors treated cartilage cells with glycine and found that this significantly increased collagen synthesis (compared to treatment with other amino acids). Since glycine is by far the most common amino acid in collagen, this connection is somehow not entirely illogical. We already thought so when formulating our premium collagen powder. In addition to the highest quality Solugel® collagen peptides, it also contains free glycine, as well as the important cofactors vitamin C, copper and manganese.

Do you regularly take collagen powder to do something good for your tendons? If not, you should at least think about it. We'll also give you a good price: With the code "procollagen type I N-terminal propeptide" you get 25% off our premium collagen. Just kidding, of course... Not the discount, but the code. Try " Collagen25 ".