The impact of chronic imipramine treatment on amino acid concentrations in the hippocampus of mice

2012 ◽  
Vol 15 (5) ◽  
pp. 26-33 ◽  
Author(s):  
Mao Nagasawa ◽  
Tatsuro Murakami ◽  
Shozo Tomonaga ◽  
Mitsuhiro Furuse
Keyword(s):  
Amino Acid ◽  
The Impact ◽  
Amino Acid Concentrations ◽  
Chronic Imipramine

scholarly journals The glycation level of milk protein strongly modulates post-prandial lysine availability in humans

2019 ◽  
Vol 123 (5) ◽  
pp. 545-552 ◽  
Author(s):  
Jean Nyakayiru ◽  
Glenn A. A. van Lieshout ◽  
Jorn Trommelen ◽  
Janneau van Kranenburg ◽  
Lex B. Verdijk ◽  
...  
Keyword(s):  
Amino Acid ◽  
Milk Protein ◽  
Milk Proteins ◽  
Ultra Performance Liquid Chromatography ◽  
Protein Glycation ◽  
Plasma Amino Acid ◽  
Amino Acid Availability ◽  
Protein Ingestion ◽  
The Impact ◽  
Amino Acid Concentrations

AbstractIndustrial heat treatment of milk results in protein glycation. A high protein glycation level has been suggested to compromise the post-prandial rise in plasma amino acid availability following protein ingestion. In the present study, we assessed the impact of glycation level of milk protein on post-prandial plasma amino acid responses in humans. Fifteen healthy, young men (age 26 (SEM 1) years, BMI 24 (SEM 1) kg/m2) participated in this randomised cross-over study and ingested milk protein powder with protein glycation levels of 3, 20 and 50 % blocked lysine. On each trial day, arterialised blood samples were collected at regular intervals during a 6-h post-prandial period to assess plasma amino acid concentrations using ultra-performance liquid chromatography. Plasma essential amino acid (EAA) concentrations increased following milk protein ingestion, with the 20 and 50 % glycated milk proteins showing lower overall EAA responses compared with the 3 % glycated milk protein (161 (SEM 7) and 142 (SEM 7) v. 178 (SEM 9) mmol/l × 6 h, respectively; P ≤ 0·011). The lower post-prandial plasma amino acid responses were fully attributed to an attenuated post-prandial rise in circulating plasma lysine concentrations. Plasma lysine responses (incremental AUC) following ingestion of the 20 and 50 % glycated milk proteins were 35 (SEM 4) and 92 (SEM 2) % lower compared with the 3 % glycated milk protein (21·3 (SEM 1·4) and 2·8 (SEM 0·7) v. 33·3 (SEM 1·7) mmol/l × 6 h, respectively; P < 0·001). Milk protein glycation lowers post-prandial plasma lysine availability in humans. The lower post-prandial availability of lysine following ingestion of proteins with a high glycation level may compromise the anabolic properties of a protein source.

scholarly journals Casein Protein Processing Strongly Modulates Post-Prandial Plasma Amino Acid Responses In Vivo in Humans

Nutrients ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 2299
Author(s):  
Jorn Trommelen ◽  
Michelle E. G. Weijzen ◽  
Janneau van Kranenburg ◽  
Renate A. Ganzevles ◽  
Milou Beelen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sodium Caseinate ◽  
Ultra Performance Liquid Chromatography ◽  
Protein Processing ◽  
Plasma Amino Acid ◽  
Micellar Casein ◽  
Casein Protein ◽  
The Impact ◽  
Amino Acid Concentrations

Micellar casein is characterized as a slowly digestible protein source, and its structure can be modulated by various food processing techniques to modify its functional properties. However, little is known about the impact of such modifications on casein protein digestion and amino acid absorption kinetics and the subsequent post-prandial plasma amino acid responses. In the present study, we determined post-prandial aminoacidemia following ingestion of isonitrogenous amounts of casein protein (40 g) provided as micellar casein (Mi-CAS), calcium caseinate (Ca-CAS), or cross-linked sodium caseinate (XL-CAS). Fifteen healthy, young men (age: 26 ± 4 years, BMI: 23 ± 1 kg·m−2) participated in this randomized cross-over study and ingested 40 g Mi-Cas, Ca-CAS, and XL-CAS protein, with a ~1 week washout between treatments. On each trial day, arterialized blood samples were collected at regular intervals during a 6 h post-prandial period to assess plasma amino acid concentrations using ultra-performance liquid chromatography. Plasma amino acid concentrations were higher following the ingestion of XL-CAS when compared to Mi-CAS and Ca-CAS from t = 15 to 90 min (all p < 0.05). Plasma amino acid concentrations were higher following ingestion of Mi-CAS compared to Ca-CAS from t = 30 to 45 min (both p < 0.05). Plasma total amino acids iAUC were higher following the ingestion of XL-CAS when compared to Ca-CAS (294 ± 63 vs. 260 ± 75 mmol·L−1, p = 0.006), with intermediate values following Mi-CAS ingestion (270 ± 63 mmol·L−1, p > 0.05). In conclusion, cross-linked sodium caseinate is more rapidly digested when compared to micellar casein and calcium caseinate. Protein processing can strongly modulate the post-prandial rise in plasma amino acid bioavailability in vivo in humans.

scholarly journals Effect of 30 % nutrient restriction in the first half of gestation on maternal and fetal baboon serum amino acid concentrations

2012 ◽  
Vol 109 (8) ◽  
pp. 1382-1388 ◽  
Author(s):  
Thomas J. McDonald ◽  
Guoyao Wu ◽  
Mark J. Nijland ◽  
Susan L. Jenkins ◽  
Peter W. Nathanielsz ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Maternal Blood ◽  
Nutrient Restriction ◽  
Adult Disease ◽  
Amino Acid Availability ◽  
Lower Body Weight ◽  
Uterine Growth ◽  
The Impact ◽  
Amino Acid Concentrations

Mechanisms linking maternal nutrient restriction (MNR) to intra-uterine growth restriction (IUGR) and programming of adult disease remain to be established. The impact of controlled MNR on maternal and fetal amino acid metabolism has not been studied in non-human primates. We hypothesised that MNR in pregnant baboons decreases fetal amino acid availability by mid-gestation. We determined maternal and fetal circulating amino acid concentrations at 90 d gestation (90dG, term 184dG) in control baboons fed ad libitum (C, n 8) or 70 % of C (MNR, n 6). Before pregnancy, C and MNR body weights and circulating amino acids were similar. At 90dG, MNR mothers had lower body weight than C mothers (P< 0·05). Fetal and placental weights were similar between the groups. MNR reduced maternal blood urea N (BUN), fetal BUN and fetal BUN:creatinine. Except for histidine and lysine in the C and MNR groups and glutamine in the MNR group, circulating concentrations of all amino acids were lower at 90dG compared with pre-pregnancy. Maternal circulating amino acids at 90dG were similar in the MNR and C groups. In contrast, MNR fetal β-alanine, glycine and taurine all increased. In conclusion, maternal circulating amino acids were maintained at normal levels and fetal amino acid availability was not impaired in response to 30 % global MNR in pregnant baboons. However, MNR weight gain was reduced, suggesting adaptation in maternal–fetal resource allocation in an attempt to maintain normal fetal growth. We speculate that these adaptive mechanisms may fail later in gestation when fetal nutrient demands increase rapidly, resulting in IUGR.

scholarly journals Impact of an oral amino acid provision on Achilles peritendinous amino acid concentrations in young and older adults

2021 ◽  
Author(s):  
Chad C. Carroll ◽  
Samantha Couture ◽  
Dominick O. Farino ◽  
Shivam H. Patel ◽  
Nathan W.C. Campbell ◽  
...  
Keyword(s):  
Older Adults ◽  
Amino Acids ◽  
Amino Acid ◽  
Tendon Tissue ◽  
Amino Acid Consumption ◽  
Oral Consumption ◽  
Acid Consumption ◽  
The Impact ◽  
Amino Acid Concentrations ◽  
Tendon Collagen

ABSTRACTRecent studies have indicated that consumption of amino acid-rich compounds can increase tendon collagen content and enhance biomechanical function. Still, it is not clear as to what extent oral consumption of amino acids alters peritendinous amino acid concentrations. Whether aging alters the delivery of amino acids to tendon tissue after oral consumption is also not known. Using microdialysis, we determined the impact of a single oral essential amino acid bolus on Achilles peritendinous amino acid concentrations in younger (n=7; 27±1 yr.) and older adults (n=6; 68±2 yrs.) over four hours. The peritendinous concentration of all amino acids in the beverage except methionine (p=0.136) and glycine (p=0.087) increased with time (p<0.05). Additionally, the concentrations of glycine and arginine were greater in older adults (p≤0.05). We also accessed the impact of amino acid consumption on peritendinous concentrations of pro-collagen Iα1, a marker of collagen synthesis. Pro-collagen Iα1 tended to change with time (p=0.071) but was not altered age (p=0.226). We demonstrate that an oral amino acid bolus leads to modest increases in Achilles peritendinous amino acid concentrations in young and older adults. The concentration of some amino acids was also greater in older adults. However, the amino acid bolus did not significantly impact peritendinous pro-collagen concentrations.

scholarly journals HLA-DRB1 Alleles Associated with Lower Leishmaniasis Susceptibility Share Common Amino Acid Polymorphisms and Epitope Binding Repertoires

Vaccines ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 270
Author(s):  
Nicky de Vrij ◽  
Pieter Meysman ◽  
Sofie Gielis ◽  
Wim Adriaensen ◽  
Kris Laukens ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Epitope ◽  
Human Leukocyte ◽  
Leishmania Species ◽  
Hla Polymorphism ◽  
Common Amino Acid ◽  
Binding Core ◽  
Epitope Discovery ◽  
Epitope Binding ◽  
The Impact

Susceptibility for leishmaniasis is largely dependent on host genetic and immune factors. Despite the previously described association of human leukocyte antigen (HLA) gene cluster variants as genetic susceptibility factors for leishmaniasis, little is known regarding the mechanisms that underpin these associations. To better understand this underlying functionality, we first collected all known leishmaniasis-associated HLA variants in a thorough literature review. Next, we aligned and compared the protection- and risk-associated HLA-DRB1 allele sequences. This identified several amino acid polymorphisms that distinguish protection- from risk-associated HLA-DRB1 alleles. Subsequently, T cell epitope binding predictions were carried out across these alleles to map the impact of these polymorphisms on the epitope binding repertoires. For these predictions, we used epitopes derived from entire proteomes of multiple Leishmania species. Epitopes binding to protection-associated HLA-DRB1 alleles shared common binding core motifs, mapping to the identified HLA-DRB1 amino acid polymorphisms. These results strongly suggest that HLA polymorphism, resulting in differential antigen presentation, affects the association between HLA and leishmaniasis disease development. Finally, we established a valuable open-access resource of putative epitopes. A set of 14 HLA-unrestricted strong-binding epitopes, conserved across species, was prioritized for further epitope discovery in the search for novel subunit-based vaccines.

Assessing the Impact of Secondary Structure and Solvent Accessibility on Protein Evolution

Genetics ◽  
1998 ◽  
Vol 149 (1) ◽  
pp. 445-458 ◽  
Author(s):  
Nick Goldman ◽  
Jeffrey L Thorne ◽  
David T Jones
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Protein Evolution ◽  
Solvent Accessibility ◽  
Strong Association ◽  
Length Distribution ◽  
Parametric Bootstrap ◽  
Amino Acid Replacement ◽  
Physical Constraints ◽  
The Impact

Abstract Empirically derived models of amino acid replacement are employed to study the association between various physical features of proteins and evolution. The strengths of these associations are statistically evaluated by applying the models of protein evolution to 11 diverse sets of protein sequences. Parametric bootstrap tests indicate that the solvent accessibility status of a site has a particularly strong association with the process of amino acid replacement that it experiences. Significant association between secondary structure environment and the amino acid replacement process is also observed. Careful description of the length distribution of secondary structure elements and of the organization of secondary structure and solvent accessibility along a protein did not always significantly improve the fit of the evolutionary models to the data sets that were analyzed. As indicated by the strength of the association of both solvent accessibility and secondary structure with amino acid replacement, the process of protein evolution—both above and below the species level—will not be well understood until the physical constraints that affect protein evolution are identified and characterized.

Sign in / Sign up

Export Citation Format

Share Document