The route of absorbed nitrogen into milk protein

2005 ◽  
Vol 80 (1) ◽  
pp. 11-22 ◽  
Author(s):  
H. Lapierre ◽  
R. Berthiaume ◽  
G. Raggio ◽  
M. C. Thivierge ◽  
L. Doepel ◽  
...  

AbstractA database reviewing the metabolism of nitrogen (N) compounds from absorption to milk has been compiled from 14 published and unpublished studies (33 treatments) that measured the net flux of N compounds across the splanchnic tissues in dairy cows. Apparent N digestibility averaged 0·65, with this then partitioned between 0·34 excreted in urine and 0·31 secreted as milk.Nitrogen metabolites are absorbed from the lumen of the gut into the portal vein, mainly as free amino acids (AA) and ammonia; these represented 0·58 and 0·57 of digested N, respectively. All of the ammonia absorbed was removed by the liver with, as a result, a net splanchnic flux of zero. Detoxification of ammonia by the liver and catabolism of AA results in production of urea as an end-product. Hepatic ureagenesis is a major cross-road in terms of whole body N exchange, being the equivalent of 0·81 of digested N. Therefore, salvage of a considerable part of this ureagenesis is needed to support milk protein synthesis. This salvage occurs via transfer of urea from the blood circulation into the lumen of the gut. On average, 0·47 of hepatic ureagenesis was returned to the gut via the portal-drained viscera (equivalent to 0·34 of digested N) with 0·56 of this then used for anabolic purposes e.g. as precursor N for microbial protein synthesis. On average, 0·65 of estimated digestible AA was recovered in the portal vein. This loss (0·35) is due to oxidation of certain AA across the gut wall and non-absorption of endogenous secretions. The magnitude of this loss is not uniform among AA and varies between less than 0·05 for histidine to more than 0·90 for some non-essential AA, such as glutamine.A second database (six studies, 14 treatments) was constructed to further examine the subsequent fate of absorbed essential AA. When all AA are aggregated, the liver removed, on average, 0·45 of portal absorption but this value hides the considerable variation between individual AA. Simplistically, the AA behave as two major groups: one group undergoes very little hepatic removal and includes the branched-chain AA and lysine. For the second group, removal varies between 0·35 and 0·50 of portal absorption, and includes histidine, methionine and phenylalanine. For both groups, however, the efficiency of transfer of absorbed AA into milk protein decreases with increasing supply of protein. This loss of efficiency is linked directly with increased hepatic removal of AA from the second group and, probably, increased catabolism by peripheral tissues, including the mammary gland, of AA from the first group. Therefore, we must stop using fixed factors of conversion of digestible AA to milk in our predictive schemes and acknowledge that metabolism of AA between delivery from the duodenum and conversion to milk protein will vary with nutrient supply. New information evolving from re-analysis of the literature and recent studies will allow better models to be devised for the prediction of nutrient-based responses by the lactating cow. Consideration of biological efficiency, rather than maximal milk yield, will lead to systems that are economically more sensible for the farmer and that have better environmental impacts.

2003 ◽  
Vol 90 (5) ◽  
pp. 939-952 ◽  
Author(s):  
Isabelle C. Savary-Auzeloux ◽  
Linda Majdoub ◽  
Nathalie LeFloc'h ◽  
Isabelle Ortigues-Marty

The influence of propionate supplementation on the splanchnic metabolism of amino acids (AA) and other N compounds (urea-N and NH3-N) and the supply of AA and NH3-N to the hindlimb was investigated in growing lambs. Six rumen-cannulated and multicatheterised lambs (32·2kg) were fed frozen rye grass at 690kJ metabolisable energy intake/d per kg average metabolic body weight. They were infused intraruminally with a salt solution (control) or with propionate solutions at 0·23mol/l (P1) or 0·41mol/l (P2) infused at a maximal rate of 1·68 (sd 0·057) ml/min according to a repeated Latin square design. The propionate infusion did not increase the net portal appearance of total AA (TAA)-N but increased that of some branched-chain AA (valine and to a lesser extent isoleucine). Simultaneously, the propionate treatment (especially P2) induced an increased TAA utilisation by the liver. This was due mainly to an increased (+79%;P<0·07) utilisation of the essential AA and particularly the branched-chain AA. A stimulation of protein synthesis in the liver is hypothesised since (1) propionate stimulated insulin secretion and (2) utilisation of non-essential AA were less influenced by the propionate treatment in the liver (except for alanine), suggesting that the AA utilised by the liver were directed towards protein synthesis rather than towards oxidation or urea synthesis. At the splanchnic level, the propionate treatment did not have any effect on the TAA, non-essential AA and essential AA, except for a net splanchnic release that was decreased for leucine (P<0·02) and methionine (P<0·01) and increased for threonine (P<0·05). The propionate treatment did not have any effect on the hindlimb uptake of AA (essential and non-essential). As a consequence, even though the propionate treatment induced some major alterations in the splanchnic metabolism of AA, there were no changes in the net AA balance in the hindlimb (and hence probably on muscle growth). The role of the splanchnic tissues in the regulation of the AA supply to the peripheral tissues (such as muscle) therefore appears to be prominent in the regulation of muscle growth. Whether the peripheral tissues regulate their own supply by interacting with the splanchnic tissues (and especially the liver) or the liver is the only regulator of the AA supply to the muscle remains in doubt.


1992 ◽  
Vol 263 (4) ◽  
pp. E794-E799 ◽  
Author(s):  
P. De Feo ◽  
F. F. Horber ◽  
M. W. Haymond

The present studies were performed to test the hypothesis that the liver, by increasing the synthesis of specific plasma proteins during the absorption of an amino acid meal, may play an important role in the temporary "storage" of ingested essential amino acids and to explore the effects of glucocorticosteroids and recombinant human growth hormone (rhGH) on these processes. The fractional synthetic rates of albumin and fibrinogen were determined using simultaneous infusions of intravenous [1-14C]leucine and intraduodenal [4,5-3H]leucine after 22 h fasting and during absorption of glucose and amino acids in four groups of normal subjects treated for 1 wk with placebo, prednisone (0.8 mg.kg-1.day-1), rhGH (0.1 mg.kg-1.day-1), or combined treatment. When compared with the fasted state and independent of the route of tracer delivery and hormonal treatment, albumin, but not fibrinogen, synthesis increased (P < 0.0001) during absorption of a mixed glucose amino acid meal in all groups. This increase in albumin synthesis accounted for 28% of the increase in whole body protein synthesis associated with feeding and for 24, 22, and 14% in the prednisone, rhGH, and combined treatment groups, respectively. These data suggest that the stimulation of albumin synthesis observed during feeding prevents irreversible oxidative losses of a significant fraction of ingested essential amino acids and may serve as a vehicle to capture excess dietary amino acids and transport them to peripheral tissues to sustain local protein synthesis.


1986 ◽  
Vol 250 (6) ◽  
pp. E695-E701 ◽  
Author(s):  
S. Nissen ◽  
M. W. Haymond

Whole-body leucine and alpha-ketoisocaproate (KIC) metabolism were estimated in mature dogs fed a complete meal, a meal devoid of branched-chain amino acids, and a meal devoid of all amino acids. Using a constant infusion of [4,5-3H]leucine and alpha-[1-14C]ketoisocaproate (KIC), combined with dietary [5,5,5-2H3]leucine, the rate of whole-body proteolysis, protein synthesis, leucine oxidation, and interconversion of leucine and KIC were estimated along with the rate of leucine absorption. Ingestion of the complete meal resulted in a decrease in the rate of endogenous proteolysis, a small increase in the estimated rate of leucine entering protein, and a twofold increase in the rate of leucine oxidation. Ingestion of either the meal devoid of branched-chain amino acids or devoid of all amino acids resulted in a decrease in estimates of whole-body rates of proteolysis and protein synthesis, decreased leucine oxidation, and a decrease in the interconversion of leucine and KIC. The decrease in whole-body proteolysis was closely associated with the rise in plasma insulin concentrations following meal ingestion. Together these data suggest that the transition from tissue catabolism to anabolism is the result, at least in part, of decreased whole-body proteolysis. This meal-related decrease in proteolysis is independent of the dietary amino acid composition or content. In contrast, the rate of protein synthesis was sustained only when the meal complete in all amino acids was provided, indicating an overriding control of protein synthesis by amino acid availability.


DICP ◽  
1989 ◽  
Vol 23 (5) ◽  
pp. 411-416 ◽  
Author(s):  
Kathleen M. Teasley ◽  
Renee L. Buss

The critically ill, stressed patient has been characterized as having altered cellular metabolism. Altered protein metabolism is manifested as negative nitrogen balance, reduced whole-body protein synthesis, and increased proteolysis. An increased oxidation of the branched-chain amino acids (BCAA) leucine, isoleucine, and valine has also been observed. Exogenous administration of BCAA as part of a total parenteral nutrition (TPN) regimen has been proposed to compensate for the altered protein metabolism in the stressed patient by sparing endogenous sources of BCAA, thereby reducing skeletal muscle catabolism and increasing protein synthesis. Numerous clinical studies have been performed investigating this theory. The results are controversial. Differences in study outcomes appear to be related to study design, especially patient selection. Our review of those studies which were randomized, prospective, and controlled indicates that an improvement in nitrogen retention and visceral protein status can be achieved in stress-stratified patients who receive a TPN regimen containing a BCAA-enriched formula. The significance of these outcomes on morbidity, length of hospital stay, and mortality has not been evaluated.


2003 ◽  
Vol 90 (2) ◽  
pp. 271-281 ◽  
Author(s):  
D. Pacheco ◽  
M.H. Tavendale ◽  
G. W. Reynolds ◽  
T. N. Barry ◽  
J. Lee ◽  
...  

The utilisation of essential amino acids (EAA) by the mammary gland of lactating dairy cows fed fresh forages was studied to provide basic information useful in designing strategies to increase the production of milk protein from pasture-fed dairy cows. The relationship between the flux of EAA in the whole body and their uptake by the mammary gland was determined in four cows in early lactation (length of time in milk 44 (SD 14·5) d) producing 21 (SD 4·0) kg milk/d. The cows were maintained in metabolism stalls and fed fresh perennial ryegrass (Lolium perenne) and white clover (Trifolium repens) pasturead libitumor restricted to 75 %ad libitumintake. The whole-body fluxes of amino acids (AA) were measured using an arterio-venous infusion of universally13C-labelled AA. Whole-body fluxes of fourteen AA were estimated. Isotope dilution indicated that mammary utilisation accounted for one-third of the whole-body flux of EAA, with individual AA ranging between 17 and 35 %. Isoleucine, leucine, valine and lysine were the EAA with the greatest partitioning towards the mammary gland (up to 36 % of the whole-body flux), which could reflect a potentially limiting effect on milk protein synthesis. In the case of AA with low partitioning to the mammary gland (for example, histidine), it is suggested that non-mammary tissues may have priority over the mammary gland and therefore the supply of this AA may also limit milk protein synthesis.


2011 ◽  
Vol 94 (4) ◽  
pp. 1952-1960 ◽  
Author(s):  
J.A.D.R.N. Appuhamy ◽  
J.R. Knapp ◽  
O. Becvar ◽  
J. Escobar ◽  
M.D. Hanigan

1996 ◽  
Vol 63 (2) ◽  
pp. 209-222 ◽  
Author(s):  
Brian J. Bequette ◽  
John A. Metcalf ◽  
Diane Wray-Cahen ◽  
F. R. Colette Backwell ◽  
John D. Sutton ◽  
...  

SummaryMammary gland protein metabolism, determined by an arteriovenous difference technique, was monitored in four Holstein-Friesian dairy cows in response to supplemental dietary protein (provided as rumen-protected soyabean meal) during late lactation (weeks 24–30). Each cow was offered two isoenergetic diets composed of grass silage (170 g crude protein/kg dry matter) plus either a low (108 g/kg) or medium (151 g/kg) crude protein concentrate in a single crossover design involving two 21 d periods. On day 21, arteriovenous measurements across the mammary gland were made during a 13 h continuous i.v. infusion of [1-13C]leucine and with frequent (2 hourly) milk sampling during the final 6 h. Although total milk yield was slightly increased (+1 kg/d) by protein supplementation, milk protein yield was not significantly affected. Whole body protein flux (protein synthesis plus oxidation) was not significantly affected by supplementation. Total mammary gland protein synthesis (milk plus non-milk protein) was also not affected by supplementation but on both diets gland synthesis was always greater (by 20–59%) than milk protein output. The fractional oxidation rate of leucine by the mammary gland was significantly increased by protein supplementation (0·047 v. 0·136). Although the enrichment of leucine in secreted milk protein continued to increase, the final value (at 13 h) was 0·94 of the arterial plasma free leucine plateau value (not significantly different), suggesting almost exclusive use of plasma free leucine for milk protein synthesis. Based on current feeding schemes for dairy cattle, a fixed proportion (0·65–0·75) of the additional protein intake (+490 g/d) should have been partitioned into milk protein. Instead, leucine oxidation by the mammary gland was increased. Whether oxidation of other amino acids was also enhanced is unknown but if amino acid oxidation and the ‘additional’ non-milk protein synthesis occurring in the gland are not crucial to milk synthesis, then by reducing such activities improvements in the efficiency of converting absorbed amino acid into milk protein can be achieved.


2003 ◽  
Vol 89 (2) ◽  
pp. 167-179 ◽  
Author(s):  
S. O. Hoskin ◽  
I. C. Savary-Auzeloux ◽  
A. G. Calder ◽  
G. Zuur ◽  
G. E. Lobley

Responses in variables of amino acid (AA) metabolism across peripheral tissues to feed intake were studied in six sheep (mean live weight 32 kg) prepared with arterio–venous catheters across the hindquarters. Four intakes (0·5, 1·0, 1·5 and 2·5 × maintenance energy) were offered over 2-week periods to each sheep in a Latin square design with two animals replicated. Animals were infused intravenously with a mixture of U-13C-labelled AA for 10 h and integrated blood samples withdrawn from the aorta and vena cava hourly between 5 and 9 h of infusion. Biopsy samples were also taken from skin andm. vastus lateralis. Data from both essential (histidine, isoleucine, leucine, lysine, phenylalanine, threonine) and nonessential (glycine, proline, serine, tyrosine) AA were modelled to give rates of inward and outward transport, protein synthesis and degradation, plus the fraction of total vascular inflow that exchanged with the hindquarter tissues. Rates of inward transport varied more than 10-fold between AA. For all essential AA (plus serine), inward transport increased with food intake (P<0·04). There were corresponding increases in AA efflux (P<0·05) from the tissues for threonine and the branched-chain AA. Protein synthesis rates estimated from the kinetics of these AA also increased with intake (P<0·02). Rates of inward transport greatly exceeded the amount of AA necessary to support protein retention, but were more similar to rates of protein synthesis. Nutritional or other strategies to enhance AA transport into peripheral tissues are unlikely to increase anabolic responses.


2001 ◽  
Author(s):  
Mark A. McGuire ◽  
Amichai Arieli ◽  
Israel Bruckental ◽  
Dale E. Bauman

Objectives To determine endocrine factors that regulate the partitioning of amino acids by the mammary gland. To evaluate dietary flow and supply of energy and amino acids and their effects on milk protein synthesis and endocrine status. To use primary cultures of cow mammary epithelial cells to examine the role of specific factors on the rates and pattern of milk protein synthesis. Milk protein is an increasingly valuable component of milk but little is known regarding the specific hormonal and nutritional factors controlling milk protein synthesis. The research conducted for this project has determined that milk protein synthesis has the potential to be enhanced much greater than previously believed. Increases of over 25% in milk protein percent and yield were detected in studies utilizing abomasal infusion of casein and a hyperinsulinemic-euglycemic clamp. Thus, it appears that insulin, either directly or indirectly, can elicit a substantial increase in milk protein synthesis if additional amino acids are supplied. For additional amino acids, casein provided the best response even though substantial decreases in branched chain amino acids occur when the insulin clamp is utilized. Branched chain amino acids alone are incapable of supporting the enhanced milk protein output. The mammary gland can vary both blood flow and extraction efficiency of amino acids to support protein synthesis. A mammary culture system was used to demonstrate specific endocrine effects on milk protein synthesis. Insulin-like growth factor-I when substituted for insulin was able to enhance casein and a-lactalbumin mRNA. This suggests that insulin is a indirect regulator of milk protein synthesis working through the IGF system to control mammary production of casein and a-lactalbumin. Principal component analysis determined that carbohydrate had the greatest effect on milk protein yield with protein supply only having minor effects. Work in cattle determined that the site of digestion of starch did not affect milk composition alone but the degradability of starch and protein in the rumen can interact to alter milk yield. Cows fed diets with a high degree of rumen undegradability failed to specifically enhance milk protein but produced greater milk yield with similar composition. The mammary gland has an amazing ability to produce protein of great value. Research conducted here has demonstrated the unprecedented potential of the metabolic machinery in the mammary gland. Insulin, probably signaling the mammary gland through the IGF system is a key regulator that must be combined with adequate nutrition in order for maximum response.


Sign in / Sign up

Export Citation Format

Share Document