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

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178 Chapter | 7 The Erythrocyte: Physiology, Metabolism, and Biochemical Disorders Rubriblast Prorubricyte Basophilic Polychromatic Metarubricyte Reticulocyte Rubricyte Rubricyte RBC FIGURE 7-1 Summary of metabolic activities of the erythroid series. Maturation progresses from left to right. The time intervals indicated are for cattle. From Kaneko, 1980 , with permission. Distribution Time
III. Developing Erythroid Cells 179 coordinate protoporphyrin IX formation with the availability of iron by increasing the synthesis of eALAS (rate limiting enzyme in porphyrin synthesis) when the LIP is high and decreasing eALAS synthesis when the LIP is low. 5 . Siderotic Inclusions in Erythroid Cells Anucleated RBCs containing siderotic (iron-positive) inclusions are called siderocytes. Nucleated siderocytes have been called sideroblasts in human hematology, in which terminology used for RBC precursors is generally different from that conventionally used in veterinary hematology ( Bottomley, 2004 ). Siderotic inclusions in erythroid cells may consist of cytoplasmic ferritin aggregates or ironloaded mitochondria. Ferritin aggregates can occur normally in nucleated erythroid cells of humans ( Cartwright and Deiss, 1975 ), dogs ( Feldman et al. , 1981 ), and pigs ( Deiss et al. , 1966 ), but the presence of iron-loaded mitochondria is a pathological finding ( Cartwright and Deiss, 1975 ). Electron microscopy is used to definitively identify the nature of siderotic inclusions ( Fresco, 1981 ; Hammond et al. , 1969 ); however, the location of iron-positive inclusions in a ring around the nucleus of a nucleated siderocyte (termed ringed sideroblast in human hematology) strongly suggests the presence of iron-loaded mitochondria ( Bottomley, 2004 ). Conditions resulting in the pathological iron accumulation in mitochondria may induce the synthesis of a novel mitochondrial ferritin ( Torti and Torti, 2002 ). Except for iron deficiency, disorders in heme synthesis have the potential to cause excess iron accumulation in mitochondria ( Beutler, 1995b ; Fairbanks and Beutler, 1995 ). Experimental pyridoxine deficiency and experimental chronic copper deficiency have both resulted in mitochondrial iron overload in nucleated erythroid cells in bone marrow of deficient pigs ( Hammond et al. , 1969 ; Lee et al. , 1968a ). Drugs or chemicals reported to cause siderocytes or nucleated siderocytes in dogs include chloramphenicol ( Harvey et al. , 1985 ), lead, hydroxyzine, zinc ( Harvey, 2001 ), and an oxazolidinone antibiotic ( Lund and Brown, 1997 ). Siderotic inclusions in erythroid cells have been recognized in some dogs and cats with myeloproliferative disorders ( Blue et al. , 1988 ; Weiss and Lulich, 1999 ). Acquired dyserythropoiesis with siderocytes have been reported in dogs in which specific etiologies could not be determined, although some of these animals had inflammatory disorders ( Canfield et al. , 1987 ; Weiss, 2005 ). Congenital anemias with ringed nucleated siderocytes have been reported in humans ( Bottomley, 2006 ). Persistent siderotic inclusions have been recognized in microcytic hypochromic erythrocytes from an English bulldog. Erythrocytes also contained Heinz bodies and rare hemoglobin crystals ( Harvey et al. , 2007 ). A congenital defect resulting in mitochondrial iron overload and secondary oxidant injury was suspected, but not identified. Refer to Chapter 9 for more information concerning iron metabolism. C . Hb Synthesis Hb is a tetrameric protein consisting of four polypeptide globin chains each of which contains a heme prosthetic group within a hydrophobic pocket. The molecule consists of two identical alpha and two nonalpha chains that are generally classified as beta chains in adults. 1 . Heme Synthesis and Metabolism Heme is a planar molecule composed of the tetrapyrrole protoporphyrin IX, containing a central ferrous molecule. The initial rate-controlling step in heme synthesis, the eALAS reaction, occurs within mitochondria (see Chapter 8) . Glycine and the Krebs cycle intermediate succinyl-CoA are utilized as substrates, and vitamin B 6 , as pyridoxal phosphate, is required as a cofactor. The ALA formed is transported to the cytoplasm where a series of reactions results in the formation of coproporphyrinogen III, which must enter the mitochondria, presumably using an ATPbinding cassette transporter ABCB6 ( Krishnamurthy et al. , 2006 ) for the final steps in heme synthesis. The final reaction, catalyzed by heme synthetase, involves the insertion of ferrous iron into protoporphyrin IX. Following synthesis, heme must be transferred from mitochondria to the cytoplasm for combination with globin chains to complete the synthesis of Hb. The mitochondrial heme exporter has not been identified at this time. Free heme is poorly soluble in water and can bind to and damage cellular components ( Kumar and Bandyopadhyay, 2005 ). It apparently is bound to cytosolic proteins for transport to sites of globin chain synthesis ( Kumar and Bandyopadhyay, 2005 ; Taketani et al. , 1998 ). Sometime after its synthesis, the iron moiety of heme is oxidized (presumably spontaneously) to the ferric state and is then more specifically called ferriheme ( Schulman et al. , 1974 ). Heme affects erythroid cell metabolism in different ways depending on the stage of maturation. It stimulates iron uptake and heme synthesis in early erythroid cells, but it inhibits iron uptake and heme synthesis in reticulocytes (Abraham, 1991 ; Battistini et al. , 1991 ). A cellular heme exporter termed feline leukemia virus subgroup C cellular receptor (FLVCR) is up-regulated on colony-forming unitserythroid (CFU-E) progenitor cells. It may provide a safety mechanism to prevent the accumulation of toxic amounts of cytoplasmic heme before globin synthesis is initiated. 2 . Globin Synthesis The synthesis of polypeptide globin monomers occurs in association with ribosomes and polyribosomes in the cytoplasm. Evidence has been provided indicating that binding of a partially unstructured apo- β chain to a tightly folded holo- α chain to form a heme-deficient dimer is the initial step of Hb assembly. Such binding locks the β chain in a highly ordered conformation, which allows for an efficient
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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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I. Introduction 33 of genomes of va
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36 Chapter | 2 Comparative Medical
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46 Chapter | 3 Carbohydrate Metabol
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IX. Disorders of Carbohydrate Metab
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X. Disorders of Ruminants Associate
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X. Disorders of Ruminants Associate
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References 79 Kaneko , J. J. , Luic
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Chapter 4 Lipids and Ketones Michae
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II. Long Chain Fatty Acids 83 FIGUR
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II. Long Chain Fatty Acids 85 Plasm
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IV. Phospholipids 87 The regulation
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V. Cholesterol 89 V. CHOLESTEROL A.
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VI. Lipoproteins 91 TABLE 4-1 Compo
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VI. Lipoproteins 93 TABLE 4-2 Apoli
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96 Chapter | 4 Lipids and Ketones B
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98 Chapter | 4 Lipids and Ketones
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Chapter 5 Proteins, Proteomics, and
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III. Metabolism of Proteins 119 C .
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IV. Plasma Proteins 121 NH 4 HCO
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V. Methodology 123 molecule. The gl
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V. Methodology 125 has occurred wil
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Page 219 and 220: described in people. They include a
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References 229 Knight , A. P. , Las
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References 231 Martinovich , D. , a
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References 235 Shadduck , R. K. ( 1
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References 237 Tennant , B. , Dill
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References 239 Williams , D. M. , L
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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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392 Chapter | 13 Hepatic Function T
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394 Chapter | 13 Hepatic Function 2
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398 Chapter | 13 Hepatic Function 2
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408 Chapter | 13 Hepatic Function K
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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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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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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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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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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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References 555 plasma water, electr
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References 557 Krzywanek , H. ( 197
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562 Chapter | 18 Pituitary Function
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624 Chapter | 20 Thyroid Function a
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632 Chapter | 20 Thyroid Function a
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664 Chapter | 22 Trace Minerals the
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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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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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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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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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II. Serum Tumor Markers 753 also be
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III. Flow Cytometry 755 cancer of t
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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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