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T J Caperna

Publications and source records attributed to T J Caperna.

At least 19 recordsLinked to original sources
PubMed2006

Modeling growth factor activity during proinflammatory stress: methodological considerations in assessing cytokine modulation of IGF binding proteins released by cultured bovine kidney epithelial cells.

The present research was conducted to model potential mechanisms through which IGFBPs might be affected by a key proinflammatory response initiating cytokine tumor necrosis factor (TNF-)-alpha. Madin-Darby bovine kidney epithelial (MDBK) cells, known to release IGFBPs in response to several stimuli, were grown under several conditions and challenged with forskolin (F) or recombinant TNF-alpha for 24h. Forskolin increased IGFBP-3 gene expression and media content of BP-3 protein. TNF-alpha increased basal and augmented F-mediated IGFBP-3 gene expression. However, TNF-alpha effects on the measurable media content of IGFBPs were influenced by culture conditions; in the absence of added protease inhibitors (PIs) or sufficient media albumin concentration (high BSA, 1mg/ml), the effect of TNF-alpha was to decrease (P<0.02) measurable IGFBPs. In the presence of PI and high BSA, media IGFBP-3 levels were shown to be increased by TNF-alpha consistent with the gene expression data. Changes in media IGFBP-3 protease activity were examined further to explain the observed effects of TNF-alpha on production and destruction of IGFBPs in media. When recombinant human IGFBP-3 (500 ng/ml) was added to PI-free, low BSA 100 microg/ml) media from TNF-treated MDBK cells, less than 10% of the BP-3 was recognizable by Western blot in 30 min; conversely, inclusion of High BSA and PI in media resulted in attenuation of the protease effect on the IGFBPs. The data suggest that the MDBK model of cellular response to proinflammatory stimulus is affected by culture conditions and that TNF-alpha affects media content of IGFBPs through effects on IGFBP gene expression coupled with degradation of IGFBPs via enhanced proteolytic enzyme release.

Animals↗
PubMed2006

Proteomic analyses of male contributions to honey bee sperm storage and mating.

Honey bee (Apis mellifera L.) queens mate early in life and store sperm for years. Male bees likely contribute significantly to sperm survival. Proteins were extracted from seminal vesicles and semen of mature drones, separated by electrophoresis, and analysed by peptide mass fingerprinting. Computer searches against three databases, general species, honey bees and fruit flies, were performed. Spectra were used to query the recently generated honey bee genome protein list as well as general species and fruit fly databases. Of the 69 unique honey bee proteins found, 66 are also in Drosophila melanogaster. Two proteins only matched honey bee genes and one is a widespread protein lost from the fly genome. There is over-representation of genes implicated in the glycolysis pathway. Metabolism-associated proteins were found primarily in the seminal vesicle. Male accessory gland proteins as identified in Drosophila rarely had orthologs among proteins found in the honey bee. A complete listing of gel spots chosen including honey bee genome matches and Mascot searches of MALDI-TOF results with statistics is in the Supplementary table. MALDI-TOF spectra and more complete Mascot peptide mass fingerprinting data are available on request. Supplementary figs 1-3 show the stained protein gels.

Animals↗
PubMed2005

Hormonal regulation of leptin receptor expression in primary cultures of porcine hepatocytes.

A study was conducted to elucidate hormonal control of leptin receptor gene expression in primary cultures of porcine hepatocytes. Hepatocytes were isolated from pigs (52 kg) and seeded into collagen-coated T-25 flasks. Monolayer cultures were established in medium containing fetal bovine serum for 1 day and switched to a serum-free medium for the remainder of the 3-day culture period. To establish basal conditions hepatocytes were maintained in serum-free William's E medium containing 10 nM dexamethasone and 1 ng/ml insulin. For the final 24 h, insulin (1 or 100 ng/ml) or glucagon (100 ng/ml), were added in the presence or absence of 100 nM triiodothyronine (T3). RNA was extracted and quantitative RT-PCR was performed with primers specific for the long form and total porcine leptin receptors. Leptin receptor expression was calculated relative to co-amplified 18S rRNA. Expression of the long form of the leptin receptor was confirmed under basal conditions. Insulin, glucagon and synthetic human proteins (ghrelin and GLP-1) at 100 ng/ml had no influence on leptin receptor expression; the addition of T3 was associated with a marked increase (P < 0.001) in expression of total and long forms of the leptin receptor by 1.6 and 2.4-fold, respectively. Addition of leptin to cells which were pre-treated with T3 for 24 h (to up-regulate leptin receptor expression), confirmed the lack of a direct effect of leptin on glucagon-induced glycogen turnover and cAMP production. These data suggest that porcine hepatocytes may be insensitive to leptin stimulation even when leptin receptor expression is enhanced by T3.

Animals↗
PubMed2004

The role of insulin, glucagon, dexamethasone, and leptin in the regulation of ketogenesis and glycogen storage in primary cultures of porcine hepatocytes prepared from 60 kg pigs.

A study was conducted to elucidate hormonal control of ketogenesis and glycogen deposition in primary cultures of porcine hepatocytes. Hepatocytes were isolated from pigs (54-68 kg) by collagenase perfusion and seeded into collagen-coated T-25 flasks. Monolayers were established in medium containing fetal bovine serum for 1 day and switched to a serum-free medium for the remainder of the culture period. Hepatocytes were maintained in DMEM/M199 containing 1% DMSO, dexamethasone (10(-6) or 10(-7) M), linoleic acid (3.4 x 10(-5) M), and carnitine (10(-3) M) for 3 days. On the first day of serum-free culture, insulin was added at 1 or 100 ng/ml and glucagon was added at 0, 1, or 100 ng/ml. Recombinant human leptin (200 ng/ml) was added during the final 24 h; medium and all cells were harvested on the third day. Concentrations of acetoacetate and beta-hydroxybutyrate (ketone bodies) in media and glycogen deposition in the cellular compartment were determined. Ketogenesis was highly stimulated by glucagon (1 and 100 ng/ml) and inhibited by insulin. In contrast, glycogen deposition was stimulated by insulin and attenuated by glucagon; high insulin was also associated with a reduction in the ketone body ratio (acetoacetate:beta-hydroxybutyrate). High levels of dexamethasone stimulated ketogenesis, but inhibited glycogen deposition at low insulin. Culture of cells with leptin for 24 h, over the range of insulin, glucagon, and dexamethasone concentrations had no effect on either glycogen deposition or ketogenesis. These data suggest that while adult porcine hepatocytes are indeed sensitive to hormonal manipulation, leptin has no direct influence on hepatic energy metabolism in swine.

Animals↗
PubMed2002

Effect of dietary betaine on nutrient utilization and partitioning in the young growing feed-restricted pig.

The purpose of this study was to examine the effects of dietary betaine over a range of concentrations (between 0 and 0.5%) on growth and body composition in young feed-restricted pigs. Betaine is associated with decreased lipid deposition and altered protein utilization in finishing pigs, and it has been suggested that the positive effects of betaine on growth and carcass composition may be greater in energy-restricted pigs. Thirty-two barrows (36 kg, n = 8 pigs per group) were restrictively fed one of four corn-soybean meal-skim milk based diets (18.6% crude protein, 3.23 Mcal ME/kg) and supplemented with 0, 0.125, 0.25, or 0.5% betaine. Feed allotment was adjusted weekly according to BW, such that average feed intake was approximately 1.7 kg for all groups. At 64 kg, pigs were slaughtered and visceral tissue was removed and weighed. Carcasses were chilled for 24 h to obtain carcass measurements. Subsequently, one-half of each carcass and whole visceral tissue were ground for chemical analysis. Linear regression analysis indicated that, as betaine content of the diet was elevated from 0 to 0.5%, carcass fat concentration (P = 0.06), P3 fat depth (P = 0.14) and viscera weight (P = 0.129) were decreased, whereas total carcass protein (P = 0.124), protein deposition rate (P = 0.98), and lean gain efficiency (P = 0.115) were increased. The greatest differences over control pigs were observed in pigs consuming 0.5% betaine, where carcass fat concentration and P3 fat depth were decreased by 10 and 26%, respectively. Other fat depth measurements were not different (P > 0.15) from those of control pigs. In addition, pigs consuming the highest betaine level had a 19% increase in the carcass protein:fat ratio, 23% higher carcass protein deposition rate, and a 24% increase in lean gain efficiency compared with controls. Dietary betaine had no effects (P > 0.15) on growth performance, visceral tissue chemical composition, carcass fat deposition rate, visceral fat and protein deposition rates, or serum urea and ammonia concentrations. These data suggest that betaine alters nutrient partitioning such that carcass protein deposition is enhanced at the expense of carcass fat and in part, visceral tissue.

Adipose Tissue↗
PubMed2001

Methyl-beta-cyclodextrin: an alternative carrier for intravenous infusion of palmitate during tracer studies in swine (Sus scrofa domestica).

Fatty acid-free albumin has been the standard carrier for intravenous infusion of fatty acids to study in vivo lipid metabolism. However, subjects can have adverse reactions to infusion of albumin. We sought an alternative to albumin as a carrier for intravenous infusion of fatty acids, using the pig as a model. Cyclodextrins are naturally occurring water-soluble molecules that can serve as carriers for lipid-soluble compounds. 13C-palmitate was complexed to either 20% methyl-beta-cyclodextrin, 20% 2-hydroxypropyl-beta-cyclodextrin, or 5% porcine albumin (isotopic purity of infusates: 99.22+/-0.06%). 13C-palmitate-albumin was infused under fed conditions and 13C-palmitate-methyl-beta-cyclodextrin was infused under fasted and fed conditions in 50-kg pigs. Palmitate remained in solution at 4 degrees C in methyl-beta-cyclodextrin, but precipitated at 25-30 degrees C in 2-hydroxypropyl-beta-cyclodextrin. Pigs infused with 13C-palmitate-methyl-beta-cyclodextrin maintained normal body temperature and appetite; those infused with 13C-palmitate-albumin became anorexic and exhibited other negative side effects to albumin. Palmitate oxidation rates under fed conditions were similar using either 13C-palmitate-methyl-beta-cyclodextrin or 13C-palmitate-albumin complexes. Fasting increased 13C-palmitate-methyl-beta-cyclodextrin oxidation by approximately eight-fold. These data suggest that methyl-beta-cyclodextrin may be a suitable substitute for albumin in fatty acid metabolism studies in swine.

Albumins↗
PubMed2000

Design and application of a polyclonal peptide antiserum for the universal detection of leptin protein.

An epitope-specific polyclonal antiserum was produced in rabbits immunized against a synthetic 15 amino acid peptide (QRVTGLDFIPGLHPV) derived from the coding sequence reported for the porcine leptin gene (GenBank Accession No. U59894). This peptide contains a core sequence comprised of eight amino acids (GLDFIPGL) that is totally conserved in all leptin proteins studied to date. Purified recombinant human, mouse, rat, pig, and chicken leptin proteins were separated by polyacrylamide gel electrophoresis (SDS-PAGE) and electro-blotted onto PVDF membranes. Western blots were developed employing the leptin-specific peptide antiserum with an alkaline-phosphatase-conjugated anti-rabbit IgG second antibody chromogenic system. The peptide antiserum was found to be highly specific for leptin which exhibited an estimated molecular weight of about 16 kDa for all species analyzed. The sensitivity of the Western blot assay was not sufficient to permit the direct detection of leptin in chicken serum or plasma. However, with this assay we were able to detect native leptin protein in an enriched fraction prepared from chicken plasma using a combination of gel filtration and ion exchange column chromatography. Slot blots indicated a potential application of the immunostaining technique for quantitative analysis of leptin protein. Finally, the peptide antiserum was successfully employed to localize leptin protein by immunohistochemical staining of thin sections prepared from adipose (chicken and pig) and liver (chicken) tissue samples. This study is the first to report a polyclonal peptide antiserum that apparently recognizes intact leptin protein, both native and recombinant, regardless of the species of origin.

Amino Acid Sequence↗
PubMed2000

Bovine blastocyst-derived trophectoderm and endoderm cell cultures: interferon tau and transferrin expression as respective in vitro markers.

Continuous cultures of bovine trophectoderm (CT-1 and CT-5) and bovine endoderm (CE-1 and CE-2) were initiated and maintained on STO feeder cells. CT-1 and CT-5 were derived from the culture of intact, 10- to 11-day in vitro-produced blastocysts. CE-1 and CE-2 were derived from the culture of immunodissected inner cell masses of 7- to 8-day in vitro-produced blastocysts. The cultures were routinely passaged by physical dissociation. Although morphologically distinct, the trophectoderm and endoderm both grew as cell sheets of polarized epithelium (dome formations) composed of approximately cuboidal cells. Both cell types, particularly the endoderm, grew on top of the feeder cells for the most part. Trophectoderm cultures grew faster, relative to endoderm, in large, rapidly extending colonies of initially flat cells with little or no visible lipid. The endoderm, in contrast, grew more slowly as tightly knit colonies with numerous lipid vacuoles in the cells at the colony centers. Ultrastructure analysis revealed that both cell types were connected by desmosomes and tight junctional areas, although these were more extensive in the trophectoderm. Endoderm was particularly rich in rough endoplasmic reticulum and Golgi apparatus indicative of cells engaged in high protein production and secretion. Interferon tau expression was specific to trophectoderm cultures, as demonstrated by reverse transcription-polymerase chain reaction, Western blot, and antiviral activity; and this property may act as a marker for this cell type. Serum protein production specific to endoderm cultures was demonstrated by Western blot; this attribute may be a useful marker for this cell type. This simple coculture method for the in vitro propagation of bovine trophectoderm and endoderm provides a system for assessing their biology in vitro.

Animals↗
PubMed1999

Influence of dietary protein on insulin-like growth factor binding proteins in the chicken.

We determined the effect of dietary protein on the distribution of insulin-like growth factor (IGF) binding proteins in chicken plasma. Three groups of male broilers (n = 6 per group) were fed (ad libitum) isocaloric diets containing 12, 21 or 30% dietary protein. Birds were fed respective diets beginning at 7 days of age and killed at 28 days. No differences were observed between adequate (21%) and high (30%) protein intakes for any of the parameters investigated (growth criteria, plasma levels of IGF-I, growth hormone or IGF-binding proteins). Feeding protein deficient diets (12%) resulted in a 34% decrease in body weight, 17% decrease in feed intake and a 39% increase in feed/gain ratio. IGF-binding proteins in plasma samples were separated by SDS-PAGE and transferred to nitrocellulose sheets. Nitrocellulose blots were probed with [125I]chicken IGF-II. Four regions of binding activity corresponding to 70, 43, 30 and 24 kDa were observed in all samples. Birds consuming 12% dietary group protein had less than 50% of the 43-kDa binding activity of birds consuming 21 or 30% dietary protein. The 30-kDa binding activity was 42% lower in the 12% dietary protein group compared to birds consuming adequate protein. In contrast, 70- and 24-kDa binding activities were not influenced by dietary protein. Chickens consuming 12% dietary protein had higher levels of growth hormone and lower levels of IGF-I than those consuming 21 or 30% dietary protein. These data indicate that in chickens, the circulating levels of at least two independent IGF-binding proteins are influenced by dietary protein.

Animals↗
PubMed1998

Porcine somatotropin, dietary protein and energy effects on arginase and transaminase activities in pigs.

Two experiments were conducted with cross-bred barrows to determine the effect of somatotropin administration on liver enzyme activities. In the first experiment, pigs growing from 26 to 55 kg body weight were given two doses of pituitary porcine somatotropin (pST; 0 and 100 micrograms per kg body weight) and three levels of dietary energy (60, 80 and 100% of free choice intake). In the second experiment, pigs growing from 30 to 60 kg body weight were given two doses of recombinant porcine somatotropin (rpST; 0 and 100 micrograms per kg body weight) and five levels of dietary crude protein (110, 150, 190, 230 and 270 g crude protein/kg diet). Liver arginase (ARG, EC 3.5.3.1) and aspartate aminotransferase (AAT, EC 2.6.1.1) activities were then determined in organ samples taken at slaughter time. Dietary energy did not change liver ARG. Activities of both ARG and AAT increased as dietary crude protein increased. Both pST and rpST decreased ARG, AAT and serum utrea nitrogen. There was a lack of interaction between rpST therapy and dietary protein on either ARG or AAT activities, suggesting that set nutritional states are not required for expression of pST effects.

Animal Nutritional Physiological Phenomena↗
PubMed1996

Ultrastructure, enzymatic, and transport properties of the PICM-19 bipotent liver cell line.

The pig epiblast-derived PICM-19 cell line was previously shown to spontaneously differentiate into liver-like cells and structures and to secrete serum proteins. A study was undertaken to further define the liver-like characteristics of the PICM-19 cell line. PICM-19 cells displayed in vitro ultrastructure, enzymatic, and transport characteristics similar to those of parenchymal hepatocytes and bile duct epithelium. The PICM-19 cells contained large oval nuclei, numerous oval to elongate mitochondria with flat cristae, extensive rough and smooth endoplasmic reticulum, Golgi complexes, lipid vacuoles, and glycogen granules. Biliary canaliculi with intraluminal projecting microvilli were delimited by the junctional apparatuses between adjacent PICM-19 cells. The PICM-19 cells rapidly transported fluorescein into their biliary canaliculi from the extracellular environment. PICM-19 cells that had differentiated into multicellular ductal structures had high gamma-glutamyltranspeptidase (GGT) activity at their apical surfaces as shown by histochemical staining. PICM-19 total GGT activity was at least 19 times higher than that found in porcine hepatocytes. Metyrapone induced cytochrome P-450 content of PICM-19 cells was at least one-fourth of that found in porcine hepatocytes. PICM-19 P-450 activity induced by 7-ethoxycoumarin was nearly equivalent to that of primary cultures of pig hepatocytes. The data support the proposal that differentiated PICM-19 cells resembled hepatocytes, or bile duct epithelium cells, and, therefore, the PICM-19 cell line behaved like early embryonic liver progenitor cells.

Animals↗
PubMed1996

Influences of somatotropin on Na(+)-K(+)-ATPase, Mg(2+)-ATPase and Ca(2+)-ATPases of Porcine visceral tissues.

Two experiments were conducted to determine the overall influence of porcine somatotropin (pST) administration on the specific activity of visceral tissue ATPases. Pigs were fed a corn-soybean meal-skim milk-based diet approximately 85% of ad libitum, such that for each experiment, control and pST-treated pigs consumed similar amounts of feed. As observed for pigs chronically treated with pST, enhanced growth of visceral tissues was evident in pigs treated for 6 and 14 days (d) with pST. The specific activity of detergent-activated Na(+)-K(+)-ATPase (ouabain-sensitive adenosine triphosphatase activity) was determined in fresh tissue homogenates prepared from liver, heart, kidney and duodenum. Treatment with pST was associated with a 19% increase in Na(+)-K(+)-ATPase-specific activity in the liver; specific activity of Mg(2+)-ATPase was not influenced by pST. Whole liver Na(+)-K(+)-ATPase and Mg(2+)-ATPase activities were 35% and 25% greater, respectively, in somatotropin-treated pigs. The specific activities of Na(+)-K(+)-ATPase in heart, kidney and duodenum were similar for controls and pigs treated for 14 d with pST. The specific activities of high- and low-affinity Ca(2+)-ATPase in kidney medulla were 20 and 26% lower, respectively, in pigs treated for 14 d with pST compared with controls. In contrast, Ca(2+)-ATPases in other tissues, including kidney cortex, were not influenced by pST treatment. These data indicate that some of the observed increase in energy expenditure associated with pST treatment may be attributable to increased organ size as well as to enhanced hepatic Na+ and K+ flux. While Na(+)-K(+)-ATPase activity is specifically enhanced in the liver, pST does not appear to be a general Na(+)-K(+)-ATPase activator in all tissues and may be associated with depressed activity of Ca(2+)-ATPases in the kidney.

Animals↗
PubMed1996

Plasma clearance and tissue distribution of labelled chicken and human IGF-I and IGF-II in the chicken.

The metabolic clearance of chicken IGF-I (cIGF-I), cIGF-II, human IGF-I (hIGF-I), and hIGF-II was examined in the chicken using 125I-labelled growth factors. Superose-12 chromatography of plasma collected at 7.5 min post-infusion revealed peaks of radioactivity corresponding to 150 and 43 kDa and unbound tracer. Statistical analysis of trichloroacetic acid (TCA)-precipitable radioactivity in sequential plasma samples as well as following chromatography of the same samples revealed that clearance of the radiolabelled peptides followed an apparent triphasic pattern. The close similarity of the individual chromatographically defined pools in their clearance rate compared with the three components described by TCA precipitation strongly suggested their identity. Both free 125I-labelled cIGF-II (3.11 min) and hIGF-II (3.01 min) were cleared at a greater rate than their IGF-I counterparts. Unbound hIGF-I was cleared at a greater rate than cIGF-I (4.45 vs 5.66 min respectively). A similar pattern for clearance was evident in the radio-labelled growth factors associated with the 43 kDa component, although at a longer half-life. There was no difference in the apparent clearance of the radiolabelled growth factors associated with the 150 kDa component between IGF-I or -II or between species. Analysis of the chromatographic profiles of radioactive IGF-I peptides complexed to serum proteins versus those bound to labelled IGF-II peptides revealed the presence of a large molecular mass binding protein in vivo. Ligand blotting of chicken serum determined that a binding protein with a mass of 70 kDa was detectable with 125I-IGF-II probes only, and was not present in pig serum. In addition, tissue uptake of 125I-cIGF-I and -II was evaluated. Similar patterns of tissue distribution and uptake were observed for 125I-cIGF-I and -II, except that cIGF-II uptake by the liver exceeded that of 125I-cIGF-I at 15 min post-infusion. The rank order of tissue distribution was as follows: kidney > testis > heart > liver > pancreas > small intestine > cartilage > bursa > gizzard > leg muscle > breast muscle > brain. We conclude from these studies that the clearance of IGFs from the compartments identified in blood and the potential target tissues is dependent on their interactions with IGF-binding proteins and receptors.

Animals↗
PubMed1995

Endotoxin infusion in anesthetized sheep is associated with intrapulmonary sequestration of leukocytes that immunohistochemically express tumor necrosis factor-alpha.

Plasma levels of tumor necrosis factor-alpha (TNF-alpha) peak between 2 and 4 h during a 12-h continuous infusion of endotoxin in awake sheep. We hypothesized that a source of this TNF-alpha is the pool of leukocytes that accumulate in the pulmonary circulation. To test this hypothesis, we physiologically monitored six anesthetized sheep during baseline and 4-h endotoxin infusion periods (10 ng/kg x min). We obtained open-lung biopsies at baseline and at 20 min and 2 and 4 h during the endotoxin infusion period for immunohistochemical localization of TNF-alpha. The plasma concentration of TNF-alpha increased from an average baseline concentration of 0.06 +/- 0.03 ng/ml (mean +/- SD) to a peak of 1.40 +/- 0.28 ng/ml at 2 h of the endotoxin infusion. We observed increased cytoplasmic TNF-alpha immunoreactivity in situ among neutrophils and intravascular mononuclear phagocytes during the endotoxin infusion compared with baseline. Also, the number of immunopositive leukocytes increased in the pulmonary circulation during the continuous infusion of endotoxin. We conclude that TNF-alpha-producing leukocytes accumulate in the pulmonary circulation during endotoxemia. These cells probably contribute to both the rise in the circulating levels of TNF-alpha and the development of acute lung injury.

Anesthesia↗
PubMed1995

Effect of dietary energy intake and exogenous porcine growth hormone administration on circulating porcine growth hormone concentration and response to human growth hormone-releasing factor administration in growing swine.

In a 2 x 2 treatment array (n = 4 pigs/treatment), the effects of feed intake (ad libitum vs. restricted to 60% ad libitum) and the daily administration of excipient buffer or porcine pituitary-derived growth hormone (GH) at a dose of 100 micrograms/kg body weight per day on serum GH profile and human growth hormone-releasing factor (hGRF) response were examined in barrows weighing 55 kg. Feed intake treatment was implemented from 25 to 55 kg live weight. Buffer or GH treatment was implemented for 10 d before sampling. After GH treatment, the integrated serum GH concentration area was 25% greater in barrows fed restrictively. Data are consistent with the suggestion that GH dose to improve the efficiency of lean tissue deposition be adjusted according to feeding regimen. The serum GH response to hGRF was also altered by level of feed intake. The ad libitum feeding of buffer-treated animals resulted in a monophasic serum GH response to hGRF, whereas barrows fed restrictively had a biphasic response to hGRF. Together, these data suggest that feed intake pattern alters GH secretion and as such could influence the practical implementation of somatotropin as a metabolism modifier in swine.

Animals↗
PubMed1995

Somatotropin enhances the rate of amino acid deposition but has minimal impact on amino acid balance in growing pigs.

This experiment was conducted to establish the influence of porcine somatotropin on tissue distribution and deposition rates of amino acids in growing pigs. Barrows were treated daily with buffer or porcine somatotropin (100 micrograms/kg body wt) when they weighed between 30 and 64 kg (eight pigs/group). Pigs were restrictively fed so that the average food intake was 1.86 kg/d. The corn-soybean meal-skim milk-based diet contained 18% crude protein and 1.2% lysine, and was designed to meet muscle amino acid ratio profile with respect to lysine as the first limiting amino acid for growth. Tissue levels of eighteen amino acids were determined on lyophilized samples that were appropriately hydrolyzed and analyzed by HPLC. The concentrations (mg/g dry wt) of all amino acids were greater in carcass, skin, head and empty body of porcine somatotropin-treated pigs; amino acid concentration in viscera was not influenced by porcine somatotropin. However, when the concentration of each amino acid was expressed on a per unit protein basis, the amino acid profiles of control and porcine somatotropin-treated pigs were quite similar. The average deposition rate of each amino acid was increased approximately 67% by porcine somatotropin. When the deposition of each amino acid was calculated in relation to lysine, however, the pattern of amino acid utilization for growth was similar for control and porcine somatotropin-treated pigs; exceptions were arginine, glycine and tryptophan. The ratio of indispensable to dispensable amino acids that were deposited was also similar for control and porcine somatotropin-treated pigs. These data indicate that the synthesis rate of individual proteins can be influenced by porcine somatotropin, but the balance of amino acids remains largely unaffected, suggesting that the changes in protein and amino acid metabolism elicited by porcine somatotropin are consistent with normal growth processes.

Amino Acids↗
PubMed1995

Endotoxin administration decreases plasma insulin-like growth factor (IGF)-I and IGF-binding protein-2 in Angus x Hereford steers independent of changes in nutritional intake.

Endotoxemia and sepsis cause severe shifts in metabolism towards catabolic events. The objective of the research was to determine whether endotoxin administration changes plasma concentrations of IGF-I and IGF-binding protein-2 (IGFBP-2) in Angus x Hereford steers. In Experiment 1, mean feed intake in endotoxin-treated steers (n = 6) decreased 60% within the first 24 h after endotoxin and averaged, for the duration of the 96 h test period, an intake 35.5% lower than the mean ad libitum intake recorded prior to endotoxin. Plasma concentrations of IGF-I averaged 182 ng/ml in steers before endotoxin (E. coli, 055:B5, 0.2 micrograms/kg, i.v. bolus) and decreased an average of 24.2% at 24 to 96 h after endotoxin. In Experiment 2, a paired feeding strategy was used to determine whether the reduced feed intake was a significant factor in changing plasma concentrations of IGF-I and IGFBP-2 after endotoxin challenge. Steers were divided into endotoxin (0.2 micrograms/kg, i.v., n = 6) or control (saline, i.v., n = 3) treatments. Each of three endotoxin-treated steers was paired to a specific control. In this fashion, the adjusted feed intake of each endotoxin-treated steer was fed to it's paired control every 24 h through 96 h after endotoxin.(ABSTRACT TRUNCATED AT 250 WORDS)

Animal Nutritional Physiological Phenomena↗