The objective was to examine the effects of postruminal partially hydrolyzed starch (SH) and/or casein on the expression of pancreatic alpha-amylase mRNA, protein and activity in calves. Holstein calves [(n = 24) 88 plus minus 3 kg body weight (BW)], fitted with abomasal infusion cannulas, were randomly assigned within block (week of infusion) to one of four abomasal infusion treatments. Calves were fed an alfalfa-based diet, and SH [4 g/(kg BW.d)] and/or casein [0.6 g/(kg BW.d)] was infused abomasally for 10 d before tissue collection. There was a SH x casein interaction (P < 0.10) for pancreatic weight (g and g/kg BW) because casein increased pancreatic weight in the absence of SH but did not influence pancreatic weight in the presence of SH. Pancreatic alpha-amylase mRNA tended to be lower (P = 0.06) and protein and activity (U/g pancreas and U/g protein) were lower (P = 0.02) in calves receiving abomasal SH. The concentration of pancreatic trypsin activity (U/g pancreas and U/g protein) was lower (P < 0.03) in calves receiving abomasal SH. There was a SH x casein interaction for total alpha-amylase and trypsin activity [U/pancreas and U/(pancreas.kg BW)] because casein increased total activity in the absence of SH but not in the presence of SH. These data suggest that increases in small intestinal protein flow enhance pancreatic weight and thus total pancreatic alpha-amylase and trypsin activity, yet small intestinal SH inhibits the increase in pancreatic weight resulting from increased small intestinal protein flow. Additionally, postruminal SH decreases alpha-amylase expression largely by translational events.

/pdf/postruminal-administration-of-partially-hydrolyzed-starch-jhihfcmfac.pdf

Postruminal Administration of Partially Hydrolyzed Starch and Casein Influences Pancreatic α-Amylase Expression in Calves

In ruminants, pancreatic alpha-amylase is the primary enzyme responsible for the initial hydrolysis of alpha-linked glucose in the small intestinal lumen. The objective of this experiment was to examine the effects of altered dietary starch and energy supply on the expression of pancreatic alpha-amylase mRNA, protein and activity in lambs. Wether lambs (n = 24; 28 +/- 0.5 kg body weight) were fed low or high starch diets at 1.2 or 1.8 x net energy of maintenance for at least 28 d before tissue collection. Lambs fed the high energy/high starch diet tended to have more pancreatic alpha-amylase protein (54.5 kDa; P: = 0.08) and had greater activity (P: = 0.03), but alpha-amylase mRNA (1.6 kb) tended to be lower (P: = 0.17). Additionally, rumen fluid total short-chain fatty acid concentration was greater (P: = 0.04) and plasma glucose concentration tended to be greater (P: = 0.07) in lambs fed the high energy/high starch diet. However, pancreatic trypsinogen protein (25. 5 kDa) and jejunal maltase activity were not influenced by dietary treatment, suggesting that different regulatory systems are involved in regulating the tissue protein or activity levels of these two enzymes compared with alpha-amylase. These data suggest that dietary regulation of pancreatic alpha-amylase expression in ruminants is complex and probably regulated by transcriptional and post-transcriptional events.

/pdf/dietary-carbohydrate-source-and-energy-intake-influence-the-51skhuivw0.pdf

Dietary Carbohydrate Source and Energy Intake Influence the Expression of Pancreatic α-Amylase in Lambs

Twenty-four yearling beef steers (initial BW = 510 +/- 4.9 kg) predominantly of Angus breeding were used in a randomized complete block design to determine the effect of dietary CP concentration on pancreatic cellularity, mass, and alpha-amylase and trypsin activities. Treatment diets were formulated to contain 8.8, 11.0, 13.2, and 15.4% CP. Soybean meal and Top Soy (ruminal bypass soybean meal) were used as supplemental protein sources to ensure that MP intake was increased with increasing dietary CP concentrations. Steers were penned in groups of 4 (1 steer per treatment) and individually fed at 2.5x the NE(m) requirement by using Calan gates for 28 d before tissue collection. Four steers (1 pen) were slaughtered per week. Pancreases were weighed, subsampled, frozen in liquid N(2), and stored at -80 degrees C until analyses for DNA, RNA, and protein concentrations, and alpha-amylase and trypsin activities. Pancreatic weight (g and g/kg of BW) did not differ among treatment groups. Pancreatic DNA concentration (mg/g) decreased linearly (P = 0.06) with increasing CP concentration. Pancreatic protein (g/pancreas) increased linearly (P = 0.08) with increasing dietary CP concentration. Pancreatic alpha-amylase activity (U/g, U/mg of DNA, U/g of protein, U/pancreas, and U/kg of BW) increased linearly (P < or = 0.04) with increasing dietary CP concentration. Pancreatic trypsin activity (U/g, U/g of DNA, U/g of protein, U/pancreas, and U/kg of BW) increased linearly (P < or = 0.09) with increasing dietary CP concentration. Pancreatic alpha-amylase and trypsin activities (U/mg of RNA) responded quadratically (P < or = 0.09), with the greatest alpha-amylase activity observed in the 13.2% CP treatment. These data indicate that increasing dietary CP concentration decreases pancreatic cell numbers and also increases the concentration and content of pancreatic alpha-amylase and trypsin activities. Changes in cell number and size may be important factors regulating digestive enzyme production in the pancreas of cattle.

Pancreatic mass, cellularity, and α-amylase and trypsin activity in feedlot steers fed diets differing in crude protein concentration

Quantitative data on digestive anatomy of the world's largest ruminant, the giraffe, are scarce. Data were collected from a total of 25 wild-caught and 13 zoo-housed giraffes. Anatomical measures were quantified by dimension, area or weight and analysed by allometric regression. The majority of measures scaled positively and isometrically to body mass. Giraffes had lower tissue weight of all stomach compartments and longer large intestinal length than cattle. When compared to other ruminants, the giraffe digestive tract showed many of the convergent morphological adaptations attributed to browsing ruminants, for example lower reticular crests, thinner ruminal pillars and smaller surface area of the omasal laminae. Salivary gland weight of the giraffe, however, resembled that of grazing ruminants. This matches a previous finding of similarly small salivary glands in the other extant giraffid, the okapi (Okapia johnstoni), suggesting that not all convergent characteristics need be expressed in all species and that morphological variation between species is a combination of phylogenetic and adaptational signals.

/pdf/quantitative-macroscopic-anatomy-of-the-giraffe-giraffa-1vcvlgiggi.pdf

Quantitative Macroscopic Anatomy of the Giraffe (Giraffa camelopardalis) Digestive Tract

BACKGROUND Small intestinal starch digestion in ruminants is potentially limited by inadequate production of carbohydrases. Previous research has demonstrated that small intestinal starch digestion can be improved by postruminal supply of casein or glutamic acid. However, the mechanisms by which casein and glutamic acid increase starch digestion are not well understood. OBJECTIVES The objective of this experiment was to evaluate the effects of duodenal infusions of starch with casein or glutamic acid on postruminal carbohydrase activities in cattle. METHODS Twenty-two steers [mean body weight (BW) = 179 ± 4.23 kg] were surgically fitted with duodenal and ileal cannulas and limit-fed a soybean hull-based diet containing small amounts of starch. Raw cornstarch (1.61 ± 0.0869 kg/d) was infused into the duodenum alone (control), or with 118 ± 7.21 g glutamic acid/d, or 428 ± 19.4 g casein/d. Treatments were infused continuously for 58 d and then steers were killed for tissue collection. Activities of pancreatic (α-amylase) and intestinal (maltase, isomaltase, glucoamylase, sucrase) carbohydrases were determined. Data were analyzed as a randomized complete block (replicate group) design using the GLM procedure of SAS to determine effects of infusion treatment. RESULTS Duodenal casein infusion increased (P < 0.05) pancreatic α-amylase activity by 290%. Duodenal glutamic acid infusion increased (P < 0.03) duodenal maltase activity by 233%. Duodenal casein infusion increased jejunal maltase (P = 0.02) and glucoamylase (P = 0.03) activity per gram protein by 62.9% and 97.4%, respectively. Duodenal casein infusion tended to increase (P = 0.10) isomaltase activity per gram jejunum by 38.5% in the jejunum. Sucrase activity was not detected in any segment of the small intestine. CONCLUSIONS These results suggest that small intestinal starch digestion can be improved in cattle with increased small intestinal flow of casein through increases in postruminal carbohydrase activities.

Duodenal Infusions of Starch with Casein or Glutamic Acid Influence Pancreatic and Small Intestinal Carbohydrase Activities in Cattle.

Effects of nutritional level on digestive enzyme activities in the pancreas and small intestine of calves slaughtered at same body weight

【目的】イオン選択性電極（ISE）法での血清イオン化Ca（iCa）の測定は3から4時間以内にすべきとされる．全血ガス分析検査で3時間超の遅延がiCa測定に及ぼす影響を検討した．【方法】血液透析（HD）患者43名に，透析前バランスヘパリンコートシリンジを用い内シャントより全血2 mL採血し，速やかにガス分析検査を行った．検体を常温で3.5時間放置後再びガス分析検査を行った．【結果】3.5時間放置によりpHは7.375から7.304，HCO3は20.20から19.91，Base Excess（BE）は－4.38から－6.1に有意（いずれもp＜0.001）に下降し，pCO2は35.39から40.81，Lactateは1.32から3.02と有意（いずれもp＜0.001）に上昇，lactic acidosisを呈した．AcidosisにもかかわらずiCaは1.13から1.12（p＜0.03），pH補正iCaは1.12から1.08（p＜0.001）に低下した．【結論】全血検査の測定時間遅延は，乳酸の増加，pHの低下，pH補正iCa濃度の低下を惹起する． 

Influence of measurement time delay on the ionized calcium concentration according to blood gas analysis ―Lactate values increase and ionized calcium values fall when the gas analysis syringe is left at room temperature for 3.5 hours―

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Effects of nutritional level on digestive enzyme activities in the pancreas and small intestine of calves slaughtered at same body weight

Influence of measurement time delay on the ionized calcium concentration according to blood gas analysis ―Lactate values increase and ionized calcium values fall when the gas analysis syringe is left at room temperature for 3.5 hours―