Clinical Biochemistry of Domestic Animals (Sixth Edition) - UMK ...

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84 Chapter | 4 Lipids and Ketones 2 new carbons at the carboxyl end of the existing LCFA. Fatty acid elongase uses the same substrates (malonyl- CoA and NADPH) as fatty acid synthase, but it is located in a different part of the cell and prefers palmityl-CoA as its substrate. However, fatty acid elongase can use longer LCFA-CoA as substrates to a limited degree to produce LCFA-CoA with a length of as great as 24 carbons ( Cook and McMaster, 2002 ). Nonruminant mammals synthesize LCFA in liver, adipose, and mammary tissue. Ruminants synthesize LCFA primarily in adipose and mammary tissue with acetate being the most important precursor. Ruminants generally have a low capacity for LCFA synthesis in liver, but after eating large amounts of high-starch diets, they may synthesize some LCFA in the liver from acetate and propionate ( Hanson and Ballard, 1967 ; Ingle, 1972a, 1972b; Liepa 1978). C. Catabolism of Long Chain Fatty Acids 1. Desaturation Most animals are capable of desaturating LCFA only at the Δ 4 , Δ 5 , Δ 6 , and Δ 9 positions (counting from the carboxyl end). Animals are able to desaturate palmityl-CoA and stearyl-CoA between C 9 and C 10 by means of Δ 9 desaturase system located in the endoplasmic reticulum to produce palmitoleyl-CoA and oleyl-CoA, respectively. However, animals are not able to create additional double bonds beyond C 9 in these products to any significant extent, so linoleic and linolenic acids must be absorbed from the intestinal tract ( Cook and McMaster, 2002 ). By a combination of the actions LCFA elongase and Δ 4 , Δ 5 , and Δ 6 desaturase systems, the livers of most mammals can synthesize arachidonic acid and eicosapentaenoic acid from linoleic and linolenic acids, respectively. However, the cat has very low levels of Δ 6 desaturase in its liver and must have arachidonic acid in its diet ( MacDonald et al ., 1984 ). 2 . β-Oxidation The main catabolic route for LCFA is β-oxidation. Most tissues can perform β-oxidation (erythrocytes are an exception), but those most adept at it are liver, skeletal muscle, and heart. In addition, the liver can partially oxidize LCFA to ketones, an important process that will be discussed extensively later. Before LCFA can be subjected to β-oxidation, they must be esterified to CoA, which is accomplished by the following reaction: LCFA ATP CoA ←⎯⎯ →LCFA-CoA AMP PP The reaction is catalyzed by LCFA-CoA synthetase, an enzyme bound to the endoplasmic reticulum and the outer mitochondrial membrane. The pyrophosphate (PP) is rapidly hydrolyzed, so the reaction effectively consumes two ATP. The activation of LCFA is not rate limiting for β- oxidation ( Pande, 1971 ). For LCFA-CoA to be catabolized, it must pass into the mitochondrion, which is a problem because the inner mitochondrial membrane is impermeable to it. The CoA must be exchanged for a carnitine moiety, a reaction catalyzed outside the mitochondrion by carnitine acyltransferase I ( Fig. 4-2 ): LCFA-CoA carnitine ←⎯⎯ →LCFA-carnitine CoA LCFA-carnitine passes readily through the inner mitochondrial membrane and is acted on by carnitine acyltransferase II, which converts the LCFA-carnitine back to LCFA-CoA ( Kopec and Fritz, 1973 ). Carnitine acyltransferase I appears to be controlled by inhibition by malonyl-CoA ( McGarry et al ., 1977 ), and it is logical that when lipogenesis is stimulated, the LCFA that are produced should be prevented from entering the mitochondrion where they will be catabolized. In the mitochondrion, the process of β-oxidation per se cleaves the LCFA into acetyl-CoA units. The reaction sequence is as follows: R-CH2-CH2-CO-CoA FAD acyl-CoA dehydrogenase ⎯⎯⎯⎯⎯⎯⎯⎯⎯→ R-CHCH-CO-CoA FADH2 R-CHCH-CO-CoA H2O Δ2 -enoyl-CoA hydratase ⎯⎯⎯⎯⎯⎯⎯⎯⎯→R-C( OH)H-CH2CO-CoA R-C(OH)H-CH -CO-CoA NAD 2 L( ) -3-hydroxyacyl-CoA dehydrogenase ⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯→ R-CO-CH2-CO-CoA NADH H R-CO-CH2-CO-CoA CoA thiolase ⎯⎯⎯⎯⎯ → R-CO-CoA CH -CO-CoA The resulting acyl-CoA is two carbons shorter and can recycle through the pathway. Each trip of an acyl-CoA through the pathway generates one FADH 2 and one NADH H 1 , which can generate 5 ATP via oxidative phosphorylation. If the LCFA has an odd number of carbons, which is rare, the final product of β-oxidation will be propionyl- CoA. The double bond produced by the acyl-CoA dehydrogenase reaction is of trans configuration, not the cis configuration occurring in unsaturated LCFA found free or esterified to glycerol. Unsaturated LCFA can proceed through β-oxidation to within three carbons of the double bond. As this point, Δ 2 -enoyl-CoA hydratase cannot act because it requires a trans, rather than a cis, configuration in its substrates, and it requires that the double bond be between C 2 and C 3 rather than between C 3 and C 4 . At this point, Δ 3 , Δ 2 -enoyl-CoA isomerase will convert the Δ 3 -cis double bond to a Δ 2 - trans double bond, which will allow β-oxidation to proceed 3
II. Long Chain Fatty Acids 85 Plasma LCFA by Glucagon by Insulin Acetoacetate 3-Hydroxybutyrate Membrane LCFA ATP CoA Glycerol-3-P Cytosol & Microsomes LCFA-CoA Triglycerides – Malonyl-CoA Carnitine CoA LCFA-Carnitine Inner Mitochondrial Membrane CAT I CAT II 3-Hydroxybutyrate NAD + NADH Acetoacetate Carnitine LCFA-Carnitine CoA Mitochondrial Matrix LCFA-CoA CoA b-Oxidation FAD + NAD + Acetyl-CoA Hydroxymethylglutaryl-CoA CoA FADH 2 + NADH Acetyl-CoA Acetoacetyl-CoA CoA FAD + NAD + Tricarboxylic Acid Cycle FADH 2 + NADH + CO 2 FIGURE 4-2 Long chain fatty acid (LCFA) oxidation and ketogenesis in the liver. Abbreviations: CAT, carnitine acyltransferase. ( Kilponen et al ., 1991 ). Polyunsaturated LCFA require an additional enzyme, 2,4-dienoyl-CoA reductase, because after enoyl-CoA isomerase acts, the new trans double bond will still have the second cis double bond in close proximity, which will prevent Δ 2 -enoyl-CoA hydratase from acting. 2,4-Dienoyl-CoA reductase effectively eliminates the second double bond by reducing it with NADPH ( Roe et al ., 1990 ). β-Oxidation in the mitochondria appears to be controlled mainly by substrate availability. The acetyl-CoA units can be oxidized in the citric acid cycle provided there is sufficient oxaloacetate to condense with them to form citrate. Alternatively, acetyl-CoA units can be recondensed to form ketones, which will occur when there is not sufficient oxaloacetate for citrate formation or when citrate synthase is inhibited by high levels of citrate. Although β-oxidation occurs mostly in mitochondria, the process occurs to a minor extent in peroxisomes as well ( Wanders et al ., 1992 ). Although the main catabolic route for LCFA is β- oxidation, there are two quantitatively minor alternatives.
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Preface It has been more than a dec
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viii Contributors Björn P. Meij (5
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2 Chapter | 1 Concepts of Normality
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10 Chapter | 1 Concepts of Normalit
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Chapter 2 Comparative Medical Genet
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I. Introduction 29 Green Red Green
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I. Introduction 31 A1 genetic map d
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VI. Normal Plasma and Serum Protein
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VII. Interpretation of Serum Protei
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References 149 Andersson , M. , Ste
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References 151 response of haptoglo
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References 153 dogs with metastasiz
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References 155 Watson , T. D. G. (
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158 Chapter | 6 Clinical Veterinary
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V. Methods for Evaluation of the Im
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VI. Laboratory Diagnosis of Disease
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Chapter 7 The Erythrocyte: Physiolo
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II. Hematopoiesis 175 progenitor ce
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III. Developing Erythroid Cells 177
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IV. Mature RBC 185 immune-mediated
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IV. Mature RBC 187 TABLE 7-3 Erythr
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IV. Mature RBC 189 TABLE 7.5 Erythr
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IV. Mature RBC 191 Echinocyte forma
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IV. Mature RBC 193 Pig RBC isoantig
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IV. Mature RBC 195 occurs in chicke
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IV. Mature RBC 197 inorganic phosph
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IV. Mature RBC 199 (a) FIGURE 7-6 T
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IV. Mature RBC 201 RBC 2,3DPG incre
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IV. Mature RBC 203 mechanisms would
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IV. Mature RBC 205 released during
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IV. Mature RBC 207 reduced by ascor
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V. Determinants of RBC Survival 209
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V. Determinants of RBC Survival 211
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VI. Inherited Disorders of RBCs 213
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described in people. They include a
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References 221 Boas , F. E. , Forma
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References 223 Della Rovere , F. ,
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References 227 phosphofructokinase-
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Chapter 8 Porphyrins and the Porphy
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II. Porphyrins 243 two vinyl groups
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II. Porphyrins 245 TABLE 8-2 Nomenc
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IV. Porphyrias 247 6. Uroporphyrins
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IV. Porphyrias 249 i . Urine It is
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IV. Porphyrias 251 to localize the
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IV. Porphyrias 253 FIGURE 8-6 Metab
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IV. Porphyrias 255 estrogens. The d
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References 257 and hexachlorobenzen
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Chapter 9 Iron Metabolism and Its D
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II. Iron Distribution 261 plasma of
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IV. Plasma Iron Transport 263 pathw
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VI. Iron Metabolism in Cells 265 of
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VI. Iron Metabolism in Cells 267 in
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VII. Tests for Evaluating Iron Meta
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VII. Tests for Evaluating Iron Meta
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VIII. Disorders of Iron Metabolism
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References 279 ( Norrdin et al ., 2
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References 281 Fresco , R. ( 1981 )
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References 283 Moore , C. V. , Duba
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References 285 Weiden , P. L. , Hac
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288 Chapter | 10 Hemostasis TABLE 1
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292 Chapter | 10 Hemostasis The pro
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294 Chapter | 10 Hemostasis exhibit
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298 Chapter | 10 Hemostasis that is
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302 Chapter | 10 Hemostasis However
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304 Chapter | 10 Hemostasis 2. Comp
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306 Chapter | 10 Hemostasis is a re
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308 Chapter | 10 Hemostasis 2. Asse
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310 Chapter | 10 Hemostasis necessi
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312 Chapter | 10 Hemostasis disease
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314 Chapter | 10 Hemostasis concent
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316 Chapter | 10 Hemostasis the rol
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318 Chapter | 10 Hemostasis proport
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320 Chapter | 10 Hemostasis a consi
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322 Chapter | 10 Hemostasis Bakhtia
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324 Chapter | 10 Hemostasis Dowd ,
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326 Chapter | 10 Hemostasis Kier ,
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328 Chapter | 10 Hemostasis Nielsen
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330 Chapter | 10 Hemostasis Tablin
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332 Chapter | 11 Neutrophil Functio
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352 Chapter | 12 Diagnostic Enzymol
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380 Chapter | 13 Hepatic Function L
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382 Chapter | 13 Hepatic Function e
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384 Chapter | 13 Hepatic Function p
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388 Chapter | 13 Hepatic Function s
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390 Chapter | 13 Hepatic Function f
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392 Chapter | 13 Hepatic Function T
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394 Chapter | 13 Hepatic Function 2
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396 Chapter | 13 Hepatic Function u
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398 Chapter | 13 Hepatic Function 2
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400 Chapter | 13 Hepatic Function c
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402 Chapter | 13 Hepatic Function F
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404 Chapter | 13 Hepatic Function A
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406 Chapter | 13 Hepatic Function E
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408 Chapter | 13 Hepatic Function K
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410 Chapter | 13 Hepatic Function R
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412 Chapter | 13 Hepatic Function W
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414 Chapter | 14 Gastrointestinal F
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Chapter 15 Skeletal Muscle Function
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II. Specialization of the Sarcolemm
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II. Specialization of the Sarcolemm
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III. Heterogeneity of Skeletal Musc
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III. Heterogeneity of Skeletal Musc
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V. Exercise and Adaptations to Trai
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VI. Diagnostic Laboratory Methods f
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VI. Diagnostic Laboratory Methods f
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IX. Selected Neuromuscular Disorder
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IX. Selected Neuromuscular Disorder
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References 479 and, recently, there
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References 481 Engel , A. G. ( 2004
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References 483 Paciello , O. , Maio
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Chapter 16 Kidney Function and Dama
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II. Kidney Morphology and Function
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II. Kidney Morphology and Function
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III. Tests of Kidney Function 491 (
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III. Tests of Kidney Function 493 T
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III. Tests of Kidney Function 495 B
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6 5 4 3 2 1 0 Dog Cat Equine Cattle
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III. Tests of Kidney Function 499 d
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IV. Tests of Kidney Damage 501 1000
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IV. Tests of Kidney Damage 503 and
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IV. Tests of Kidney Damage 505 Enzy
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V. Biochemical Changes in Kidney Di
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V. Biochemical Changes in Kidney Di
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References 511 were reported to occ
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References 523 creatinine measureme
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Chapter 17 Fluid, Electrolyte, and
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532 Chapter | 17 Fluid, Electrolyte
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VIII. Clinicopathological Indicator
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References 555 plasma water, electr
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References 557 Krzywanek , H. ( 197
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References 559 Strombeck , D. R. (1
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562 Chapter | 18 Pituitary Function
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606 Chapter | 19 Adrenocortical Fun
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624 Chapter | 20 Thyroid Function a
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626 Chapter | 20 Thyroid Function t
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628 Chapter | 20 Thyroid Function A
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630 Chapter | 20 Thyroid Function S
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632 Chapter | 20 Thyroid Function a
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634 Chapter | 20 Thyroid Function O
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636 Chapter | 21 Clinical Reproduct
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664 Chapter | 22 Trace Minerals the
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666 Chapter | 22 Trace Minerals the
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668 Chapter | 22 Trace Minerals P i
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670 Chapter | 22 Trace Minerals be
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Copper Cuproreductase Cytochromes C
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674 Chapter | 22 Trace Minerals 2 .
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676 Chapter | 22 Trace Minerals Cor
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678 Chapter | 22 Trace Minerals inf
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680 Chapter | 22 Trace Minerals tis
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682 Chapter | 22 Trace Minerals VI
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684 Chapter | 22 Trace Minerals red
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686 Chapter | 22 Trace Minerals of
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688 Chapter | 22 Trace Minerals Per
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692 Chapter | 22 Trace Minerals Liu
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Chapter 23 Vitamins Robert B. Rucke
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III. Fat-Soluble Vitamins 697 TABLE
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III. Fat-Soluble Vitamins 699 Carot
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III. Fat-Soluble Vitamins 701 Major
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III. Fat-Soluble Vitamins 703 doses
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III. Fat-Soluble Vitamins 705 Diet
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III. Fat-Soluble Vitamins 707 conta
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III. Fat-Soluble Vitamins 709 immun
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IV. Water-Soluble Vitamins 711 are
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IV. Water-Soluble Vitamins 713 abil
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IV. Water-Soluble Vitamins 715 5’
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IV. Water-Soluble Vitamins 717 H 2
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IV. Water-Soluble Vitamins 719 Enzy
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722 Chapter | 23 Vitamins When biot
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724 Chapter | 23 Vitamins Cyanocoba
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726 Chapter | 23 Vitamins V . VITAM
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728 Chapter | 23 Vitamins nature, r
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730 Chapter | 23 Vitamins Stites ,
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732 Chapter | 24 Lysosomal Storage
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Chapter 25 Tumor Markers Michael D.
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II. Serum Tumor Markers 753 also be
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III. Flow Cytometry 755 cancer of t
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V. Immunohistochemistry/Immunocytoc
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V. Immunohistochemistry/Immunocytoc
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References 761 analysis will facili
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References 763 Fernandez , N. J. ,
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References 765 Meinecke , B. , and
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References 767 Walter , J. ( 2000 )
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770 Chapter | 26 Cerebrospinal Flui
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TABLE 26-7 Continued Constituent Ro
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Chapter 27 Clinical Biochemistry in
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II. Hepatotoxicity 823 Therefore, A
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III. Nephrotoxicity 825 suggested a
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IV. Toxins Affecting Skeletal and C
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VII. Toxins Affecting Erythrocytes
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VIII. Toxins Affecting Hemoglobin a
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IX. Toxins Affecting the Nervous Sy
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References 835 Plants classified as
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References 837 Solaiman , S. G. , M
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840 Chapter | 28 Avian Clinical Bio
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Budgerigar ALAT (IU/g tissue) Budge
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874 Appendix | I SI Units TABLE E S
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Appendix II Conversion Factors of S
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Appendix IV Stability of Serum Enzy
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Appendix VI Nomogram for Computing
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t0100 Appendix VIII Blood Analyte R
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884 Appendix | VIII Blood Analyte R
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890 Appendix | IX Blood Analyte Ref
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Appendix X Blood Analyte Reference
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Appendix XI Blood Analyte Reference
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Appendix XII Urine Analyte Referenc
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902 Appendix | XIII Cerebrospinal F
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904 Appendix | XIV Cerebrospinal Fl
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