Biomedical subjects

William F Martin

Publications and source records attributed to William F Martin.

7 recordsLinked to original sources

PubMed2025

The early evolution of the glycolytic pathway from autotrophic origins to glycogen and back.

Glycolysis stops where gluconeogenesis starts-at pyruvate, the central metabolite of biosynthesis. The early history of carbon metabolism is preserved in archaeal and bacterial enzymes for glucose synthesis and breakdown. Here, we summarize the distribution and phylogeny of enzymes involved in glycolysis, gluconeogenesis, and glycogen metabolism from genomes of cultured prokaryotes. The presence of glycolytic pathways in H2-dependent chemolithoautotrophs, including methanogens, which cannot grow on exogenous glucose, correlates with their use of glycogen for intracellular carbon storage. Glycogen synthesis and gluconeogenesis are universal among prokaryotes, but glycolysis is not, indicating that the enzymatic conversions of glycolysis arose in the gluconeogenic direction encompassing three phases: (1) an autotrophic origin from H2 and CO2 to pyruvate and triosephosphate (trunk glycolysis) fulfilling basic amino acid and cofactor synthesis in the last universal common ancestor, (2) from triosephosphate to glucose supplying cell wall (murein and pseudomurein) and nucleic acid biosynthetic requirements in the first free-living autotrophs, also giving rise to intracellular carbon reserves (glycogen), followed by (3) diversification and transfer of enzymes for glycogen-mobilizing glycolytic routes. An autotrophic origin of trunk glycolysis followed by glycogen-dependent origin of glucose utilization account for conservation, distribution, and diversity of enzymes observed in microbial sugar phosphate pathways.

Glycolysis↗

PubMed2006

Effects of dietary protein intake on indexes of hydration.

This study aims to characterize the relationship between increased protein intake and hydration indexes. Five men participated in a 12-week, randomized, crossover, controlled diet intervention study. Subjects consumed eucaloric diets containing 3.6 (high protein), 1.8 (moderate protein), and 0.8 (low protein) g/kg/day of protein for 4 weeks each. Energy intakes were based on requirements established relative to resting energy expenditure and activity at baseline. Assessments included blood urea nitrogen, plasma osmolality, urine-specific gravity, and estimates of fluid balance. Repeated-measures analyses of variance and paired t tests were used to determine effects of treatment and time. Fluid intake and fluid balance were unaffected. Blood urea nitrogen was higher for high protein vs low protein and vs moderate protein, and urine-specific gravity was higher for high protein vs moderate protein. Baseline plasma osmolality was greater for high protein vs low protein and vs moderate protein. The effect of increasing dietary protein on fluid status was minimal.

Adult↗

PubMed2006

Level of dietary protein impacts whole body protein turnover in trained males at rest.

The current investigation examined the effect of variations in protein intake on Whole body protein turnover (WBPTO) at rest in endurance-trained males. Whole body protein turnover is influenced by both diet and exercise. Whether endurance athletes require more protein than the non-exerciser remains equivocal. Five male runners (21.3 +/- 0.3 years, 179 +/- 2 cm, 70.6 +/- 0.1 kg, 8.7% +/- 0.4% body fat, 70.6 +/- 0.1 VO(2)max) participated in a randomized, crossover design diet intervention where they consumed either a low-protein (LP; 0.8 g/kg), moderate-protein (MP; 1.8 g/kg), or high-protein (HP; 3.6 g/kg) diet for 3 weeks. Whole body protein turnover (Ra, leucine rate of appearance; NOLD, nonoxidative leucine disposal; and Ox, leucine oxidation), nitrogen balance, and substrate oxidation were assessed at rest following each dietary intervention period. The HP diet increased leucine Ra (indicator of protein breakdown; 136.7 +/- 9.3, 129.1 +/- 7.4, and 107.8 +/- 3.1 micromol/[kg . h] for HP, MP, and LP diets, respectively) and leucine Ox (31.0 +/- 3.6, 26.2 +/- 4.3, and 18.3 +/- 0.6 micromol/[kg . h] for HP, MP, and LP diets, respectively) compared with LP diet (P < .05). No differences were noted in nonoxidative leucine disposal (an indicator of protein synthesis) across diets. Nitrogen balance was greater for HP diet than for MP and LP diets (10.2 +/- 0.7, 1.8 +/- 0.6, and -0.3 +/- 0.5 for HP, MP, and LP diets, respectively). Protein oxidation increased with increasing protein intake (54% +/- 6%, 25% +/- 1%, and 14% +/- 2% for HP, MP, and LP diets, respectively). Findings from this study show that variations in protein intake can modulate WBPTO and that protein intake approximating the current recommended dietary allowance was not sufficient to achieve nitrogen balance in the endurance-trained males in this investigation. Our results suggest that a protein intake of 1.2 g/kg or 10% of total energy intake is needed to achieve a positive nitrogen balance. This is not a concern for most endurance athletes who routinely consume protein at or above this level.

Adult↗

PubMed2006

Aerobic exercise training increases skeletal muscle protein turnover in healthy adults at rest.

The effect of a 4-wk aerobic exercise training program (30-45 min, 3-5 d/wk, >or=65% maximal heart rate) on mixed skeletal muscle protein fractional synthetic rate (FSR), fractional breakdown rate (FBR), and net protein balance (FSR - FBR) (NET) was examined in 8 healthy, previously unfit men and women [21.0+/- 0.4 y, 163.7+/- 4.4 cm, 75.6+/- 5.7 kg, 33.5+/- 4.1% body fat, VO(2 peak) 38.6+/- 2.3 mL/(kg.min)] fed eucaloric diets providing 0.85 g protein/(kg.d) for the 6-wk study. Measurements were made at baseline after 2 wk of diet intervention only, and after 4 wk of aerobic exercise training and diet intervention. Primed continuous infusions of ring-[(2)H(5)]-phenylalanine (2 micromol/kg; 0.05 micromol/(kg.min) and [(15)N]-phenylalanine (2 micromol/kg; 0.05 micromol/(kg.min) were used to assess skeletal muscle protein turnover at rest via the precursor-product method. Endurance training improved cardiovascular fitness, with a significant increase in VO(2 peak) (P<0.01) and a significant decrease in running time on a standard course (P<0.01). There were o significant changes in body mass or composition. There was a significant increase in FSR (0.077+/- 0.007 vs. 0.089+/- 0.006%/h, P<0.05) and decrease in NET (FSR - FBR) (-0.023 +/-0.004 vs. -0.072 +/- 0.012%/h, P < 0.05); FBR tended to increase (0.105+/- 0.014 vs. 0.143+/- 0.018%/h; P=0.06) after training. Findings show that aerobic training for 4 wk increases skeletal muscle protein turnover in previously unfit subjects.

Adolescent↗

PubMed2005

Dietary protein intake and renal function.

Recent trends in weight loss diets have led to a substantial increase in protein intake by individuals. As a result, the safety of habitually consuming dietary protein in excess of recommended intakes has been questioned. In particular, there is concern that high protein intake may promote renal damage by chronically increasing glomerular pressure and hyperfiltration. There is, however, a serious question as to whether there is significant evidence to support this relationship in healthy individuals. In fact, some studies suggest that hyperfiltration, the purported mechanism for renal damage, is a normal adaptative mechanism that occurs in response to several physiological conditions. This paper reviews the available evidence that increased dietary protein intake is a health concern in terms of the potential to initiate or promote renal disease. While protein restriction may be appropriate for treatment of existing kidney disease, we find no significant evidence for a detrimental effect of high protein intakes on kidney function in healthy persons after centuries of a high protein Western diet.

Journal Article↗

PubMed2005

Aerobic exercise training decreases leucine oxidation at rest in healthy adults.

Both exercise and dietary protein intake affect whole-body protein turnover (WBPTO). Few studies have investigated the effect of aerobic exercise training on WBPTO [leucine rate of appearance (Ra), oxidation (Ox), and nonoxidative leucine disposal (NOLD)] in untrained individuals consuming a specified level of protein. This study examined the effect of aerobic exercise training on WBPTO in untrained men and women during a controlled diet intervention providing 0.88 g protein/(kg . d). After a 2-wk adaptation to the study diet, 7 subjects [3 men, 4 women; 76.1 +/- 5.8 kg, 164.7 +/- 4.4 cm, 30.7 +/- 4.5% body fat, 39.1 +/- 2.8 VO(2max) (maximal oxygen uptake) mL/(kg . min)] participated in 4 wk of aerobic exercise training (running and walking 4-5 times/wk at 65-85% maximal heart rate). WBPTO (determined via constant infusion of 1-[(13)C] leucine), nitrogen balance, and body composition were determined at baseline and after 4 wk of training. Nitrogen balance (-1.0 +/- 0.7 vs. 0.9 +/- 1.1 g N/24 h, P = 0.03) improved with exercise training, whereas body mass and composition did not change. Leucine Ra did not change, Ox decreased [18 +/- 2 to 15 +/- 2 micromol/(kg . h), P </= 0.001], and NOLD tended to increase [128 +/- 18 to 151 +/- 19 micromol/(kg . h), P = 0.09] in response to training. These data indicate improved protein utilization in response to exercise training in weight-stable subjects. This study emphasizes the importance of dietary control, with specific regard to energy and protein intakes, in the characterization of protein utilization in response to an exercise intervention.

Adult↗

PubMed2003

Structure and properties of an engineered transketolase from maize.

The gene specifying plastid transketolase (TK) of maize (Zea mays) was cloned from a cDNA library by southern blotting using a heterologous probe from sorghum (Sorghum bicolor). A recombinant fusion protein comprising thioredoxin of Escherichia coli and mature TK of maize was expressed at a high level in E. coli and cleaved with thrombin, affording plastid TK. The protein in complex with thiamine pyrophoshate was crystallized, and its structure was solved by molecular replacement. The enzyme is a C2 symmetric homodimer closely similar to the enzyme from yeast (Saccharomyces cerevisiae). Each subunit is folded into three domains. The two topologically equivalent active sites are located in the subunit interface region and resemble those of the yeast enzyme.

Amino Acid Sequence↗