Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.15.1 (ACE)
 18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The adult protein turn-over daily affects 250 grammes, which is equivalent to four times the average daily protein intake. Regulation of synthesis and catabolism appears to occur by independent ways. These systems are altered during the nephrotic syndrome and ultimately lead to a loss of total body nitrogen and a risk for malnutrition. Indeed, during the nephrotic syndrome, muscle protein synthesis is further impaired as the urinary protein losses increase. This may suggest that anabolic compounds are lost in the urine of such patients. A moderate protein restriction (0.8 g/kg BW/day) allows a reduction in proteinuria, as well as pharmacological agents (ACE inhibitors) and should therefore slow the progressive renal insult.
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PMID:[Nephrotic syndrome and protein metabolism]. 892 6

Naturally occurring ACE (angiotensin converting enzyme) inhibitory peptides have a potential as antihypertensive components in functional foods or nutraceuticals. These peptides have been discovered in various food sources from plant and animal protein origin. In this paper an overview is presented of the ACE inhibitory peptides obtained by enzymatic hydrolysis of muscle protein of meat, fish, and invertebrates. Some of these peptides do not only show in vitro ACE inhibitory activity but also in vivo antihypertensive activity in spontaneously hypertensive rats. To focus on new sources of ACE inhibitory peptides, more specifically insects and other invertebrates, we compared the vertebrate and invertebrate musculature and analyzed phylogenetic relationships.
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PMID:ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: a review. 1621 51

Angiotensin II (Ang II) has been implicated in muscle protein loss in cachexia. To determine whether the Ang I/II system directly inhibits protein synthesis in muscle their effect has been monitored in vitro using murine myotubes as a surrogate model system. Ang I inhibited protein synthesis by 40-50% over the concentration range of 0.05-2.5 microM within 30 min of addition, and the inhibition remained relatively constant over 24 h. The effect was attenuated by co-incubation with the angiotensin converting enzyme inhibitor imidaprilat (50 microM) suggesting that inhibition of protein synthesis was due to the formation of Ang II. Ang II also inhibited protein synthesis by 40-50% over the concentration range of 0.1-5 microM, and the inhibition also remained relatively constant between 30 min and 24 h after addition. The effect was attenuated by insulin-like growth factor-1 (IGF-1) (25-100 ng/ml). Thus, Ang I/II have the ability to induce muscle atrophy through inhibition of protein synthesis.
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PMID:Angiotensin II directly inhibits protein synthesis in murine myotubes. 1639 30