2 research outputs found
Bowel health, defecation patterns and nutrient intake following adoption of a vegan diet: a randomized-controlled trial
The beneficial effects of a plant-based diet on gut microbiota diversity are well documented, however, its impact on clinical bowel health and defecation patterns are less well understood. Vegetarian diets have been associated with a higher bowel movement (BM) frequency as well as softer stools in cross-sectional studies. The effects of the de-novo adoption of a vegan diet on bowel health, however, have never been investigated in a randomized-controlled trial. The present study examined bowel health and defecation patterns in relation to diet and nutrient intake in a young and healthy sample of nā=ā65 physically-active German university students who were randomly assigned to either a vegan or a meat-rich diet for eight weeks. Bowel health assessment included the Bristol Stool Form Scale (BSFS), the Gastrointestinal Quality of Life Index (GIQLI) and the Cleveland Clinic Fecal Incontinence Score (CCFIS). Nutrient intake was assessed using weighed food diaries. The study was prospectively registered at the German Clinical Trial Register (DRKS00031541). Weekly BM frequency slightly increased in vegans, whereas it remained unaltered in participants assigned to a meat-rich diet. Fiber intake increased significantly in vegans (34.89 (18.46) g/d) whereas it decreased in those assigned to the meat-rich group (22.79 (12.5) g/d). No significant intergroup differences in BSFS and CCFIS patterns were observed. Adoption of a vegan diet neither resulted in a transient increase in abdominal discomfort nor in a decreased gastrointestinal quality of life, which was comparable across the diet groups. The short-term de-novo adoption of a vegan diet did not negatively affect markers of bowel health in this study.</p
Heme Binding Properties of Glyceraldehyde-3-phosphate Dehydrogenase
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a
glycolytic
enzyme that also functions in transcriptional regulation, oxidative
stress, vesicular trafficking, and apoptosis. Because GAPDH is required
for the insertion of cellular heme into inducible nitric oxide synthase
[Chakravarti, R., et al. (2010) <i>Proc. Natl. Acad. Sci. U.S.A.
107</i>, 18004ā18009], we extensively characterized the
heme binding properties of GAPDH. Substoichiometric amounts of ferric
heme bound to GAPDH (one heme per GAPDH tetramer) to form a low-spin
complex with UVāvisible maxima at 362, 418, and 537 nm and
when reduced to ferrous gave maxima at 424, 527, and 559 nm. Ferric
heme association and dissociation rate constants at 10 Ā°C were
as follows: <i>k</i><sub>on</sub> = 17800 M<sup>ā1</sup> s<sup>ā1</sup>, <i>k</i><sub>off1</sub> = 7.0 Ć
10<sup>ā3</sup> s<sup>ā1</sup>, and <i>k</i><sub>off2</sub> = 3.3 Ć 10<sup>ā4</sup> s<sup>ā1</sup> (giving approximate affinities of 19ā390 nM). Ferrous heme
bound more poorly to GAPDH and dissociated with a <i>k</i><sub>off</sub> of 4.2 Ć 10<sup>ā3</sup> s<sup>ā1</sup>. Magnetic circular dichroism, resonance Raman, and electron paramagnetic
resonance spectroscopic data on the ferric, ferrous, and ferrousāCO
complexes of GAPDH showed that the heme is bis-ligated with His as
the proximal ligand. The distal ligand in the ferric complex was not
displaced by CN<sup>ā</sup> or N<sub>3</sub><sup>ā</sup> but in the ferrous complex could be displaced by CO at a rate of
1.75 s<sup>ā1</sup> (for >0.2 mM CO). Studies with heme
analogues
revealed selectivity toward the coordinating metal and porphyrin ring
structure. The GAPDHāheme complex was isolated from bacteria
induced to express rabbit GAPDH in the presence of Ī“-aminolevulinic
acid. Our finding of heme binding to GAPDH expands the proteinās
potential roles. The strength, selectivity, reversibility, and redox
sensitivity of heme binding to GAPDH are consistent with it performing
heme sensing or heme chaperone-like functions in cells