The relationships among anthropometric variables, dietary nutrients, and plasma steroid, polypeptide, and binding-protein hormone concentrations were investigated in 24 Seventh-day Adventist postmenopausal women, 12 vegetarian (SV) and 12 nonvegetarian (SNV). Fasting blood and 7-d dietary intake information were collected. SVs consumed significantly more crude and dietary fiber and fewer saturated fatty acids than did SNVs. The thigh and sum of three skinfold-thickness measurements were significantly greater for SNVs than for SVs. Plasma concentrations of estradiol-17 beta were significantly lower in SVs than in SNVs. Significant relationships were observed for the combined groups (SV and SNV) between estradiol-17 beta and triceps and suprailiac skinfold thickness and body fat. Plasma concentrations of estradiol-17 beta of the combined groups revealed a significant negative relationship between their crude and dietary fiber intakes. Further study delineating the effects of adiposity and dietary nutrients on basal concentrations of sex hormones is warranted.

An experiment was conducted to determine whether feeding rumen-protected fatty acids (FA) to postpartum heifers would increase plasma concentrations of linoleic acid and PGF2, metabolite (PGFM), shorten the interval from calving to first increase in plasma concentrations of progesterone (P4), and increase pregnancy rate relative to controls. Hereford x Angus heifers (346 kg) were assigned randomly to treatments containing either lipid or barley supplemented diets for the first 30 d postpartum. Lipid was .23 kg.heifer(-1).d(-1) of calcium salts of FA (CSFA; n = 20), and an isocaloric amount of barley served as the control (n = 19). Supplements, with .23 kg of barley as a vehicle, and a basal diet of meadow and alfalfa hays were pen fed to heifers (5/pen). Heifers were bled on alternate days (d1 to 30) and twice weekly (d 30 to 2 wk after first estrus) for RIA of plasma PGFM and P4, respectively. Weight percentage of major FA in plasma on d1 and 7 was determined with gas chromatography. First behavioral estrus was detected by use of intact bulls and confirmed by an increase in plasma P4. On d 7, but not d 1, plasma from heifers fed CSFA had altered proportions of major FA (P< .01), including an increase in linoleic acid compared with those of controls (29.1 vs 25.6% of total FA; SE = .75; P < .01). Analysis of variance of contrast variables revealed an effect of treatment on direction of change in PGFM from d 3 to 5 (P < .01). By d 7 and on d 9, plasma concentrations of PGFM were greater in heifers fed CSFA than in controls (P = .02 and P = .06, respectively). There was no difference in plasma concentration of PGFM between treatments on d 1, 3, 5, 11, 13, and 15 postpartum (P = .80, .17, .52, .82, .46, and .77, respectively). Days to first estrus with ovulation, pregnancy rate, and calving interval were not affected by treatments (P = .58, .52, and .24, respectively). Although supplemental lipid fed to primiparous beef heifers increased plasma levels of linoleic acid and production of PGFM in the early postpartum period, it did not improve the fertility of these heifers in the subsequent breeding season.

Background: In a prior experiment, treatment of goats with the putative PPARγ agonist 2,4-thiazolidinedione (2,4-TZD) did not affect milk fat or expression of milk-fat related genes. The lack of response was possibly due to deficiency of vitamin A and/or a poor body condition of the animals. In the present experiment, we tested the hypothesis that PPARγ activation affects milk fat synthesis in goats with a good body condition and receiving adequate levels of vitamin A. Methods: Lactating goats receiving a diet that met NRC requirements, including vitamin A, were injected with 8 mg/kg BW of 2,4-TZD (n = 6) or saline (n = 6; CTR) daily for 26 days. Blood metabolic profiling and milk yield and components were measured including fatty acid profile. Expression of genes related to glucose and lipid metabolism was measured in adipose tissue and in mammary epithelial cells (MEC). Size of adipocytes was assessed by histological analysis. Results: NEFA, BHBA, and fatty acids available in plasma decreased while glucose increased in 2,4-TZD vs. CTR. Size of cells and expression of insulin signaling and glucose metabolism-related genes were larger in 2,4-TZD vs. CTR in adipose tissue. In MEC, expression of SCD1 and desaturation of stearate was lower in 2,4-TZD vs. CTR. Conclusions: Overall data revealed a lack of PPARγ activation by 2,4-TZD and no effect on milk fat synthesis despite a strong anti-lipolysis effect on adipose tissue.

Alanyl-tRNA synthetase (AlaRS) from Escherichia coli is a multimeric enzyme that catalyzes the esterification of alanine to tRNA(Ala) in the ATP-dependent aminoacylation reaction. The functional binding of all three substrates follows Michaelis-Menten kinetics. The role of cysteines in this enzyme has been evaluated via modification of these residues with p-(hydroxymercuri)phenylsulfonic acid, monobromobimane, and 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB). The former two reagents induce nearly complete inactivation of AlaRS aminoacylation activity and the release of all tightly bound zinc. In the case of mild DTNB treatment, only two of the six cysteines in AlaRS are modified, with release of all zinc and partial loss of aminoacylation activity. These experiments indicate the importance of one or more cysteines, other than those thought to be coordinated with zinc, in the aminoacylation reaction. Substitution of each of the cysteine residues outside the zinc-binding motif with serine does not disrupt zinc binding. However, the cysteine most removed in primary sequence from the active site (Cys665) is identified as important in the aminoacylation step. Mutation of Cys665 to serine induces a 120-fold decrease in the catalytic efficiency of this enzyme, primarily through a kcat effect, and introduces sigmoidal kinetics (nH = 1.8) with respect to the RNA substrate. The results demonstrate that a simple manipulation in the C-terminal region can introduce positive cooperativity in this otherwise noncooperative enzyme.

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