Exchange of Amino Acids by Muscle and Liver in Sepsis

Distribution of a non-metabolizable amino acid in different tissues of tumor-bearing rats in cachexia.

“…Therefore, it is understandable that AIB uptake by the soleus muscle was significantly less in TB rats with cancer cachexia and in PF rats with severely reduced food intake than in control FF rats, although the AIB uptakes of the muscle in PF and TB rats were not significantly different. The reduced AIB uptake by lean skeletal muscle of these rats was similar to the metabolic disturbance seen in sepsis and following injury [17,18,22,23], that is, inhibition of AIB uptake by skeletal muscle. on the other hand, AIB uptake by the liver was significantly greater in PF and TB rats than in FF rats, and was significantly more in PF rats than in TB rats.…”

“…In sepsis or after injury, protein synthesis in muscle is reported to increase [17,29,30], to remain unchanged [23,31], or to decrease [19,32,33], although the characteristic metabolic changes in sepsis and after injury are accelerated muscle proteolysis and increased peripheral release of amino acids, concomitant with stimulated amino acid uptake by the liver [17,18]. Amino acid uptake does not necessarily reflect the rate of protein synthesis, but low amino acid transport into tissues may at least be associated with a low rate of protein synthesis.…”

“…Brennan [16] .suggested that cancer cachexia had some similarity to the metabolic disturbances of host metabolism that are seen in sepsis and after major injury, although it is difficult to determine whether the starvation that accompanies cancer is an entity in itself, or simply a manifestation of malnutrition that accompanies any severe illness. Sepsis and injury are characterized by accelerated muscle proteolysis and increased peripheral release of amino acids, concomitant with stimulated amino acid uptake by the liver [17,18]. A large portion of the amino acids taken up by the liver is used for increased protein synthesis and gluconeogenesis [19][20][21].…”

Curcumin prevents lipopolysaccharide‐induced atrogin‐1/MAFbx upregulation and muscle mass loss

“…Considering that p38 and NF-κB are activated by cytokines TNF-α and IL-1 [Zarubin and Han, 2005]-two recognized mediators of muscle catabolism [Jackman and Kandarian, 2004]-it is likely that these molecules mediate the excessive muscle protein breakdown often associated with inflammatory diseases. Hence, we hypothesized that inflammation-stimulated muscle wasting can be prevented by inhibiting p38 and NF-κB activation.Sepsis is an inflammatory condition that causes a severe and rapid loss of body protein, much of which originates from skeletal muscle [Rosenblatt et al, 1983]. Many studies have provided evidence that muscle atrophy in sepsis is primarily the result of increased protein breakdown [Hasselgren et al, 1986[Hasselgren et al, , 1989Ash and Griffin, 1989] via the ubiquitinproteasome pathway [Tiao et al, 1994[Tiao et al, , 1997.…”

“…Sepsis is an inflammatory condition that causes a severe and rapid loss of body protein, much of which originates from skeletal muscle [Rosenblatt et al, 1983]. Many studies have provided evidence that muscle atrophy in sepsis is primarily the result of increased protein breakdown [Hasselgren et al, 1986[Hasselgren et al, , 1989Ash and Griffin, 1989] via the ubiquitinproteasome pathway [Tiao et al, 1994[Tiao et al, , 1997.…”