Enzymes of the Arterial Wall (eBook)

John Esben Kirk (Autor)

eBook Download: EPUB

2014 | 1. Auflage
508 Seiten
Elsevier Science (Verlag)
978-1-4832-6146-1 (ISBN)

Infos

Enzymes of the Arterial Wall is a comprehensive up-to-date monograph, and is the first publication dealing specifically with quantitative determinations of enzyme activities in human and animal vascular tissue. All available information concerning this subject is included. This summary of all current knowledge will be very useful to scientists who lack extensive library facilities and knowledge of foreign languages necessary for a thorough and time-consuming personal search of the original literature. A systematic description is made of 98 different enzymes; nearly all enzymes in the carbohydrate metabolic pathways are included. Brevity of discussion has made it possible to incorporate all available data. The results represent 27,200 quantitative biochemical assays performed with reliable analytical techniques on both normal and arteriosclerotic tissue; 70 enzymic procedures are described. The framework for the arrangement of facts throughout the book was designed to make information easily accessible. Each enzyme is described separately, using the sequence of The Commission on Enzymes of The International Union of Biochemistry, and is followed by literature references with full titles.

Inhalt

Front Cover 1
Enzymes of the Arterial Wall 4
Copyright Page 5
Table of Contents 10
Dedication 6
Preface 8
Introduction 16
Chapter 1. Oxidoreductases 20
a-Glycerophosphate Dehydrogenase (L-Glycerol-3-phosphate: NAD Oxidoreductase 1.1.1.8)
Sorbitol Dehydrogenase (L-Iditol : NAD Oxidoreductase 1.1.1.14)
Aldose Reductase (Alditol : NADP Oxidoreductase 1.1.1.21)
Lactic Dehydrogenase (L-Lactate : NAD Oxidoreductase 1.1.1.27)
a-Hydroxybutyric Dehydrogenase 44
NAD-Linked Adrenaline Dehydrogenase 48
ß-Hydroxyacyl-Coenzyme A Dehydrogenase (L-3-Hydroxyacyl-CoA : NAD Oxidoreductase 1.1.1.35)
Malic Dehydrogenase (L-Malate : NAD Oxidoreductase 1.1.1.37)
NADP-Malic Enzyme (L-Malate : NADP Oxidoreductase [Decarboxylating] 1.1.1.40)
Isocitric Dehydrogenase (NADP-specific) (threo-Ds-Isocitrate : NADP Oxidoreductase [Decarboxylating] 1.1.1.42)
6-Phosphogluconate Dehydrogenase (6-Phospho-D-gluconate : NADP Oxidoreductase [Decarboxylating] 1.1.1.44)
Glucose-6-phosphate Dehydrogenase (D-GIucose-6-phosphate : NADP Oxidoreductase 1.1.1.49)
GlyceraIdehyde-3-phosphate Dehydrogenase (D-Glyceraldehyde-3-phosphate : NAD Oxidoreductase [Phosphorylating] 1.2.1.12)
Aldehyde Oxidase 86
Succinic Dehydrogenase and Succinic Oxidase 87
Glutamic Dehydrogenase(L-Glutamate : NAD Oxidoreductase [Deaminating] 1.4.1.2)
Benzylamine Oxidase 104
Glutathione Reductase (Reduced-NAD(P) : Oxidized Glutathione Oxidoreductase 1.6.4.2)
Diaphorase (Reduced-NAD : Lipoamide Oxidoreductase 1.6.4.3)
Cytochrome c Reductase (NADH-linked) (Reduced-NAD : [Acceptor] Oxidoreductase 1.6.99.3)
Cytochrome c Oxidase (Ferrocytochrome c : Oxygen Oxidoreductase 1.9.3.1)
Catalase (Hydrogen Peroxide : Hydrogen Peroxide Oxidoreductase 1.11.1.6)
Peroxidase (Donor: Hydrogen Peroxide Oxidoreductase 1.11.1.7)
REFERENCES 126
Chapter II. Transferases 127
Catechol-O-methyltransferase (S-Adenosylmethionine : Catechol O-methyltransferase 2.1.1.6)
Transketolase (D-Sedoheptulose-7-phosphate : D-Glyceraldehyde-3-phosphate Glycolaldehyde-Transferase 2.2.1.1)
Transaldolase (Sedoheptulose-7-phosphate : D-Glyceraldehyde-3-phosphate Dihydroxyacetonetransferase 2.2.1.2)
Glycogen Phosphorylase (a-1, 4-Glucan : Orthophosphate Glucosyltransferase 2.4.1.1)
Purine Nucleoside Phosphorylase (Purine Nucleoside : Orthophosphate Ribosyltransferase 2.4.2.1)
Glutamic-Oxalacetic Transaminase (L-Aspartate : 2-Oxoglutarate Aminotransferase 2.6.1.1) and Glutamic-Pyruvic Transaminase (L-Alanine : 2-Oxoglutarate Aminotransferase
Hexosamine-Synthesizing Enzyme (L-GIutamine : D-Fructose-6-phosphate Aminotransferase 2.6.1.16)
Hexokinase (ATP : D-Hexose 6-Phosphotransferase 2.7.1.1)
Phosphofructokinase (ATP : D-Fructose-6-phosphate 1-Phosphotransferase 2.7.1.11)
Pyruvate Kinase (ATP : Pyruvate Phosphotransferase 2.7.1.40)
Phosphoglyceric Kinase (ATP : 3-Phospho-D-glycerate 1-Phosphotransferase 2.7.2.3)
Creatine Phosphokinase (ATP : Creatine Phosphotransferase 2.7.3.2)
Myokinase (ATP : AMP Phosphotransferase 2.7.4.3)
Phosphoglucomutase (a-D-Glucose-1, 6-diphosphate : a-D-Glucose-1-phosphate Phosphotransferase 2.7.5.1)
Phosphoglyceric Acid Mutase (2, 3-Diphospho-D-glycerate : 2-Phospho-D-glycerate Phosphotransferase 2.7.5.3)
Uridine Diphosphate Glucose Pyrophosphorylase (UTP : a-D-Glucose-1-phosphate Uridyltransferase 2.7.7.9)
Ribonuclease (Ribonucleate Pyrimidine-nucleotido-2'-transferase [Cyclizing] 2.7.7.16)
Rhodanese (Thiosulfate : Cyanide Sulfurtransferase 2.8.1.1)
REFERENCES 222
Chapter Ill. Hydrolases 223
Carboxylic Esterases (Carboxylic Ester Hydrolases 3.1.1)
Lipase (Glycerol Ester Hydrolase 3.1.1.3)
Lipoprotein Lipase 237
Phospholipase A (Phosphatide Acyl-hydrolase 3.1.1.4)
Phospholipase B (Lysolecithin Acyl-hydrolase 3.1.1.5)
Sphingomyelin Cholinephosphohydrolase 250
Acetylcholinesterase (Acetylcholine Hydrolase 3.1.1.7) and Cholinesterase (Acylcholine Acyl-hydrolase
Cholesterol Esterase (Sterol Ester Hydrolase 3.1.1.13)
Alkaline Phosphatase (Orthophosphoric Monoester Phosphohydrolase 3.1.3.1) and Acid Phosphatase (Orthophosphoric Monoester Phosphohydrolase
5'-NucIeotidase (5'-Ribonucleotide Phosphohydrolase 3.1.3.5)
Fructose-l, 6-diphosphatase (D-Fructose-l, 6-diphosphate 1-PhosphohydroIase 3.1.3.11)
Arylsulfatase A + B and Arylsulfatase C (Aryl-sulfate Sulfohydrolase 3.1.6.1)
Chondroitin-4-sulfatase 298
a-Glucosidase (a-D-Glucoside Glucohydrolase 3.2.1.20) and ß-Glucosidase (ß-D-Glucoside Glucohydrolase
ß-Galactosidase (ß-D-Galactoside Galactohydrolase 3.2.1.23)
a-Mannosidase (a-D-Mannoside Mannohydrolase 3.2.1.24)
a-N-AcetylgIucosaminidase 306
ß-N-Acetylglucosaminidase (ß-2-Acetamide-2-deoxy-D-glucoside Acetamidodeoxyglucohydrolase 3.2.1.30)
ß-GIucuronidase (ß-D-Glucuronide Glucuronohydrolase 3.2.1.31)
Hyaluronidase (Hyaluronate Glycanohydrolase 3.2.1.35)
ß-Xylosidase (ß-D-Xyloside Xylohydrolase 3.2.1.37)
NAD Nucleosidase (NAD Glycohydrolase 3.2.2.5)
Leucine Aminopeptidase (L-Leucyl-peptide Hydrolase 3.4.1.1)
Tripeptidase (Amino-acyl-dipeptide Hydrolase 3.4.1.3)
Carboxypeptidase (A peptidyl-amino-acid Hydrolase 3.4.2 Subgroup)
Glycyl-glycine Dipeptidase (Glycyl-glycine Hydrolase 3.4.3.1) and Leucyl-leucine Dipeptidase
Elastase 336
Thromboplastin 339
Vasculokinase 346
Plasmin (3.4.4.14) and Associated Factors 347
Cathepsin (3.4.4.23), Total Proteolysis and Autolysis 353
Adenosine Deaminase (Adenosine Aminohydrolase 3.5.4.4) and Adenylic Acid Deaminase (AMP Aminohydrolase
Inorganic Pyrophosphatase (Pyrophosphate Phosphohydrolase 3.6.1.1)
Adenosinetriphosphatases (ATP Phosphohydrolase 3.6.1.3, and ATP Pyrophosphohydrolase
FAD-Hydrolyzing Enzyme 404
REFERENCES 405
Chapter IV. Lyases 406
Aldolase (Fructose-1, 6-diphosphate D-glyceraldehyde-3-phosphate-lyase 4.1.2.13)
Citrate Condensing Enzyme (Citrate Oxaloacetate-lyase CoA-Acetylating 4.1.3.7)
Carbonic Anhydrase (Carbonate Hydro-lyase, 4.2.1.1) 417
Fumarase (L-Malate Hydro-lyase 4.2.1.2)
Aconitase (Citrate [Isocitrate]Hydro-lyase 4.2.1.3)
Enolase (2-Phospho-D-glycerate Hydro-lyase 4.2.1.11)
Glyoxalase I (S-Lactoyl-glutathione Methylglyoxal-lyase [Isomerizing] 4.4.1.5)
REFERENCES 442
Chapter V. Isomerases 443
Triosephosphate Isomerase (D-Glyceraldehyde-3-phosphate Ketol-isomerase 5.3.1.1)
Ribose-5-phosphate Isomerase (D-Ribose-5-phosphate Ketol-isomerase 5.3.1.6)
Phosphomannose Isomerase (D-Mannose-6-phosphate Ketol-isomerase 5.3.1.8)
Phosphoglucoisomerase (D-GIucose-6-phosphate Ketol-isomerase 5.3.1.9)
REFERENCES 462
Chapter VI. Comparison of Enzyme Activities in Vascular Samples from Male and Female Subjects 463
REFERENCES 472
Chapter VII. Enzyme Activities of Arterial Grafts 473
REFERENCES 480
Chapter VIII. Concluding Remarks 481
REFERENCES 484
Author Index 486
Subject Index 495

Textauszug

Oxidoreductases

Publisher Summary

This chapter focuses on oxidoreductases, which are the enzymes concerned with biological oxidation and reduction and participate in respiration and fermentation processes. In the oxidation of biological substances, three factors are involved—the hydrogen donator, the hydrogen acceptor, and the catalyst. The oxidoreductase section of enzymes has 14 subgroups. Some of the tissue oxidases catalyze the reduction of molecular oxygen to water, whereas the functioning of monoamine oxidase leads to the formation of hydrogen peroxide. Because an appreciable catalase activity has been demonstrated in human aortic tissue, it may be assumed that hydrogen peroxide produced by monoamine oxidase is quickly converted to oxygen and water.

 

Oxidoreductases are the enzymes concerned with biological oxidation and reduction and therefore participate in respiration and fermentation processes. In the oxidation of biological substances 3 factors are involved : the hydrogen donator, the hydrogen acceptor, and the catalyst. As pointed out by Baldwin (1963), the NAD- and NADP-linked dehydrogenases have outstanding properties of specificity toward their substrate and toward their hydrogen acceptor; they are apparently all capable of acting reversibly.

The oxidoreductase section of enzymes has 14 subgroups. In the present chapter activities of 24 arterial enzymes of the following subgroups are reported : 1.1 (No. = 12); 1.2 (No. = 2); 1.3 (No. = 1); 1.4 (No. = 3); 1.6 (No. = 3); 1.9 (No. = 1); and 1.11 (No. = 2).

The 1.1 and 1.2 enzymes act, respectively, on the CH-OH group and on aldehyde or keto groups as donors with NAD or NADP as acceptors; for the 1.3 enzymes the CH-CH group of the substrate is the hydrogen donor. The 1.4 subsection consists of enzymes which bring about oxidative deamination. The 1.6 subgroup distinguishes itself by the fact that the reduced forms of the coenzymes are named as donors.

Subgroup 1.9 contains important aerobic enzymes (e.g., cytochrome c oxidase, 1.9.3.1) which function as the terminal steps of the hydrogen transport chains; they act on heme groups of donors with oxygen as acceptor. The 1.11 enzymes (catalase, 1.11.1.6; peroxidase, 1.11.1.7) use hydrogen peroxide as oxidant.

For biological reasons it should be mentioned that some of the tissue oxidases (e.g., cytochrome c oxidase) catalyze the reduction of molecular oxygen to water, whereas the functioning of monoamine oxidase (1.4.3.4) leads to the formation of hydrogen peroxide. Because an appreciable catalase activity has been demonstrated in human aortic tissue (see pp. 109–111), it may be assumed that hydrogen peroxide produced by monoamine oxidase is quickly converted to oxygen and water.

REFERENCE

Baldwin, E. “Dynamic Aspects of Biochemistry,”, 4th ed. London and New York: Cambridge Univ. Press, 1963.

α-Glycerophosphate Dehydrogenase (L-Glycerol-3-phosphate : NAD Oxidoreductase; 1.1.1.8)

Publisher Summary

This chapter focuses on α-glycerophosphate dehydrogenase, which is a NAD-dependent enzyme located in the cellular cytoplasm that catalyzes the interconversion of α-glycerophosphate and dihydroxyacetone phosphate. The chapter presents research on the α-glycerophosphate dehydrogenase activity in human vascular tissue. The final millimolar concentrations employed in the test were dihydroxyacetone phosphate, 0.35; NADH, 0.155; and triethanolamine-EDTA buffer, pH 7.5, 50.0. The average α-glycerophosphate dehydrogenase activities recorded for various types of blood vessels show conspicuously higher values for the pulmonary artery, coronary artery, and inferior vena cava than for the thoracic descending aorta. Both the aorta, pulmonary artery, and vena cava samples from children displayed notably lower activities than samples from adults. Assays performed on normal and arteriosclerotic aortic tissue portions showed significantly reduced activities for the pathological specimens.

This dehydrogenase is a NAD-dependent enzyme located in the cellular cytoplasm which catalyzes the interconversion of α-glycerophosphate and dihydroxyacetone phosphate. Several biological functions of this enzyme have been considered. Because of its linkage with NAD, it has been suggested that under anaerobic conditions it exerts an influence on the ratio of lactate/pyruvate contents in the tissue. Evidence has been presented that the α-glycerophosphate compound derived from dihydroxyacetone phosphate is a major fatty acid acceptor in arterial tissue. This biochemical process in which synthesized fatty acids are converted to neutral fat has been studied in detail by Stein and co-workers (1962, 1963); the fatty acids penetrating into the arterial wall may similarly be converted to neutral fat. It should also be mentioned that the equilibrium constant of the α-glycerophosphate dehydrogenase reaction greatly favors the reduction of dihydroxyacetone phosphate and thus the formation of α-glycerophosphate.

HUMAN VASCULAR TISSUE

Analytical Procedure

Research on the α-glycerophosphate dehydrogenase activity in human vascular tissue has been done by Kirk and Ritz (1967). The enzymic assays were performed by spectrophotometric measurement of oxidation of NADH by dihydroxyacetone phosphate. Aqueous 2% homogenates were prepared at 0°C; the homogenates were subsequently centrifuged, and the supernatants immediately used for enzyme determination.

The final millimolar concentrations employed in the test (total volume, 3.0 ml) were: dihydroxyacetone phosphate, 0.35; NADH, 0.155; and triethanolamine-EDTA buffer, pH 7.5, 50.0. The reaction was conducted at 37°C using a Beckman DU spectrophotometer provided with thermospacer equipment. The buffer solution, NADH reagent, and 0.1–0.5 ml homogenate supernatant were first placed in a silica cuvette and the volume adjusted to 2.9 ml. After 20 minutes’ preincubation, 0.1 ml dihydroxyacetone phosphate solution was added to the sample and optical density readings at 340 mµ were then made at 5- to 10-minute intervals against a tissue blank over a 30-minute period. Under these conditions, zero order kinetics were usually obtained for 20 minutes; the enzyme activity was calculated on the basis of the linear part of the curve. A close relationship was observed between quantity of tissue utilized and recorded values. A reagent blank was run with each test; no notable changes in optical density were found for the blank.

Results

The average α-glycerophosphate dehydrogenase activities recorded for various types of blood vessels show conspicuously higher values for the pulmonary artery, coronary artery, and inferior vena cava than for the thoracic descending aorta (Tables I-1 and I-2). In view of the fact that the α-glycerophosphate compound produced in the reaction catalyzed by this enzyme may be an important factor in the formation of triglycerides in arterial tissue, the very high α-glycerophosphate dehydrogenase level in human coronary artery tissue deserves attention pertaining to the pathogenesis of atherosclerosis.

TABLE I-1

MEAN α-GLYCEROPHOSPHATE DEHYDROGENASE ACTIVITIES OF HUMAN VASCULAR TISSUEa

Aorta, normalb,c

0-1

3

0.0087

–

0.193

–

2–9

3

0.0087

–

0.200

–

10–19

5

0.0138

0.0063

0.304

0.142

20–29

5

0.0242

0.0084

0.560

0.212

30–39

8

0.0218

0.0177

0.520

0.398

40–49

11

0.0167

0.0099

0.439

0.265

50–59

19

0.0133

0.0091

0.362

0.264

60–69

9

0.0085

0.0040

0.244

0.114

70–89

11

0.0122

0.0078

0.349

0.246

Mean values

0–89

74

0.0144

0.0096

0.370

0.262

20–89

63

0.0150

0.0097

0.392

0.268

Aorta,...

Produkt-Details

• Erscheint lt. Verlag: 28.6.2014
• Sprache: englisch
• Themenwelt: Studium ► 1. Studienabschnitt (Vorklinik) ► Physiologie
• Themenwelt: Naturwissenschaften ► Biologie ► Humanbiologie
• Themenwelt: Technik
• ISBN-10: 1-4832-6146-8 / 1483261468
• ISBN-13: 978-1-4832-6146-1 / 9781483261461