Unless otherwise requested, this will be my last post on protein for a while. I promise. Maybe.
Came upon another review that went over some of the nuances of different protein sources, amino acid profiles, etc., and lean mass (Gorissen and Witard, 2018).
While I don’t think this really matters that much, most people on Earth get their protein 60% from plants, 40% from animals. Flip those values for the Americas and Europe.
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Wrt protein: I think quantity from diverse sources is more important than shooting for some specific amino acid score. It’s more practical and less guesswork, imo.
- Sarcopenia sucks (P<0.05). It’s one of the leading causes of reduced quality of life.
- Anabolic resistance: dietary protein intake usually stimulates muscle protein synthesis. This is reduced in inflammation and aging. There are a few steps to get around this.
- Protein balance is muscle protein synthesis (MPS) AND muscle protein breakdown (MPB). The authors acknowledged this in the intro (YAY!), but the whole review focused on the former.
- In general, it is thought that dietary protein supports MPS while insulin blunts MPB (over-simplified).
As detailed below, strategies to augment muscle protein synthesis (MPS) to the anabolic effects of dietary protein:
- increase the dose (moar protein) — added protein provides more substrate to support MPS. Protein-induced insulin secretion helps blunt MPB
- exercise can sensitize skeletal muscle to the anabolic effects of protein
- seafood/DHA may have a similar sensitizing effect (2 or 3 studies support this)
- cheat code LEUCINE (supported by many studies) – the gymbroni’s got this one right. It’s why whey, soy, and lean chicken are go-to’s: most leucine per calorie. Steak, nuts, and eggs have it too, but much less per calorie.
#context
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