Lemmy Shitpost
Welcome to Lemmy Shitpost. Here you can shitpost to your hearts content.
Anything and everything goes. Memes, Jokes, Vents and Banter. Though we still have to comply with lemmy.world instance rules. So behave!
Rules:
1. Be Respectful
Refrain from using harmful language pertaining to a protected characteristic: e.g. race, gender, sexuality, disability or religion.
Refrain from being argumentative when responding or commenting to posts/replies. Personal attacks are not welcome here.
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That means:
-No promoting violence/threats against any individuals
-No CSA content or Revenge Porn
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Posting the same post, no matter the intent is against the rules.
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4. No Porn/Explicit
Content
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Brigading, Doxxing or Witch Hunts
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-Content that might be distressing should be kept behind NSFW tags.
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If you see content that is a breach of the rules, please flag and report the comment and a moderator will take action where they can.
Also check out:
Partnered Communities:
1.Memes
10.LinuxMemes (Linux themed memes)
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All communities included on the sidebar are to be made in compliance with the instance rules. Striker
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The efficiency of phenylalanine (Phe) utilization for milk protein synthesis in dairy cows is limited, and its uptake and metabolic mechanisms in the mammary tissue remaining unclear. This study investigated the effects of Phe availability (0.07, 0.14, 0.28, and 0.56 mM) on amino acid metabolism and casein synthesis in bovine mammary epithelial cells (BMECs) cultured for 24 h. Results showed that αS1-casein, β-casein, and κ-casein expression peaked at 0.14 mM Phe (p < 0.05). At this optimal concentration, amino acid transporters (SLC7A5, SLC7A8, and SLC38A2) were upregulated, corresponding with enhanced uptake of Met, Ile, His, and Arg (p < 0.05). The mammalian target of rapamycin (mTOR) signaling pathway was activated as evidenced by increased phosphorylation of P70 S6 kinase (P70S6K) and mTOR (p < 0.05), while the general control nonderepressible 2 (GCN2) pathway was suppressed through reduced eukaryotic initiation factor 2α (eIF2α) phosphorylation (p < 0.05). As Phe concentration increased, its net uptake increased linearly (Plinear < 0.05) while uptake efficiency decreased linearly (Plinear < 0.05). High Phe concentration (0.56 mM) inhibited amino acid transporter expression and reduced uptake of Leu, Pro, and Tyr (p < 0.05). Additionally, Phe-to-Tyr conversion was dynamically regulated, with phenylalanine hydroxylase (PAH) activity inhibited at 0.07 mM Phe (p < 0.05) but enhanced at higher concentrations, concurrent with reduced exogenous Tyr uptake (p < 0.05). These findings show that casein synthesis in BMECs is optimal at 0.14 mM Phe, coinciding with enhanced expression of amino acid transporters and activation of protein synthesis pathways. In contrast, higher Phe concentrations (0.56 mM) are associated with reduced amino acid utilization efficiency. These observations suggest potential mechanisms by which Phe concentration may regulate milk protein synthesis in dairy cows.
Xing Y, Luo Y, Sun M, Yang J, Lin S, Mu X, Niu X, Li D and Liu Y (2025) Phenylalanine modulates casein synthesis in bovine mammary epithelial cells by influencing amino acid transport and protein synthesis pathways. Front. Nutr. 12:1598191. doi: 10.3389/fnut.2025.1598191