elastin and Deficiency-Diseases

Copper, as a component of numerous cuproenzymes, plays a vital role in many physiologic functions in man and animals. From the stand-point of human health there are at least three functional areas of prime importance. Copper is involved in the development and maintenance of cardiovascular and skeletal integrity, central nervous system structure and function, and erythropoietic function including iron metabolism. Although there is no evidence for widespread copper deficiency in the human population, it does occur, owing to genetic defects and other precipitating factors. A clear understanding of the functions of copper and its mechanisms of action could prove highly beneficial in the solution of present and unforeseen problems in medicine.

Topics: Anemia; Animals; Bone Diseases; Brain Diseases; Cardiovascular Diseases; Central Nervous System Diseases; Collagen; Copper; Deficiency Diseases; Elastin; Enzymes; Female; Growth Disorders; Hair; Humans; Infant; Infant, Newborn; Metalloproteins; Pigmentation Disorders; Pregnancy; Pregnancy Complications; Protein-Lysine 6-Oxidase

Topics: Animals; Brain Diseases; Copper; Deficiency Diseases; Disease Models, Animal; Elastin; Electron Transport Complex IV; Female; Growth; Heart Diseases; Pregnancy; Pregnancy Complications; Rats

Topics: Animals; Arteriosclerosis; Chemical Phenomena; Chemistry; Chick Embryo; Copper; Deficiency Diseases; Elastic Tissue; Elastin; Fibroma; Guinea Pigs; Haplorhini; Histocytochemistry; Microscopy; Microscopy, Electron; Pseudoxanthoma Elasticum; Rats; Skin Neoplasms; Staining and Labeling; Swine

Topics: Aging; Amino Acids; Aneurysm; Animals; Arteriosclerosis; Brain Diseases; Copper; Deficiency Diseases; Elastic Tissue; Elastin; Endocardial Fibroelastosis; Growth Disorders; Hair; Humans; Inflammation; Lathyrism; Marfan Syndrome; Metabolic Diseases; Respiratory Tract Diseases; Skin Diseases

Topics: Amino Acids; Animals; Child; Collagen; Connective Tissue; Copper; Deficiency Diseases; Elastin; Humans; Iron; Nutrition Disorders; Nutritional Physiological Phenomena; Pellagra; Protein Precursors; Protein-Energy Malnutrition; Rats; Scurvy; Skin

Topics: Amino Acids; Animals; Aortic Rupture; Chickens; Copper; Deficiency Diseases; Elastin; Liver; Monoamine Oxidase; Swine

Topics: Anemia; Animals; Aorta; Aortic Diseases; Chick Embryo; Chickens; Collagen; Copper; Deficiency Diseases; Elastin; Female; Hemorrhage; Lysine; Pregnancy; Swine

Topics: Animals; Bone Diseases; Cardiovascular Diseases; Catalysis; Collagen; Connective Tissue; Copper; Deficiency Diseases; Elastic Tissue; Elastin; Female; Fibroblasts; Glycosaminoglycans; Growth; Humans; Nutritional Physiological Phenomena; Osteogenesis; Pregnancy

Ultrastructural analyses were performed on clinically normal skin from forearm and/or femoral regions of five subjects, all excreting high levels of gly-pro dipeptides into the urine and exhibiting very low prolidase activity on hemolyzed erythrocytes. In both regions, the overall organization of the dermis was normal. Stereological analysis, however, showed that collagen volume density was reduced when compared to that of age-matched controls. Collagen fibrils did not show ultrastructural alterations, but they were distributed into a higher number of small bundles, and their diameters shifted towards lower values compared to age-matched controls. The elastin volume density was slightly reduced in the patients, especially in the femoral areas. In both forearm and femoral dermis, elastin fibers were significantly more numerous and smaller than in controls. Furthermore, elastin fibers were apparently normal in the forearm dermis, whereas appeared polymorphic and cribriform in the femoral skin. The results focused on the importance of efficient proline re-utilization for normal collagen and elastin synthesis and deposition. The differences between femoral and forearm skin regions from both clinical and ultrastructural points of view, may depend on mechanisms that regulate circulation and, possibly, on other factors which modulate the phenotypic expression of mesenchymal cells.

Topics: Adult; Child; Collagen; Deficiency Diseases; Dipeptidases; Elastin; Epidermis; Erythrocytes; Female; Humans; Male; Microscopy, Electron; Middle Aged

Increased bone fragility was observed in chickens fed diets containing less than 1 ppm copper. Using a device that was designed to measure torsion during fracture, it could be demonstrated that bone from copper-deficient chicks fractured with less deformation and torque than bone from control chicks. The collagen of bone from copper-deficient chicks appeared to contain fewer cross-links than normal bone. The introduction of artificial cross-links into collagen from copper-deficient chick bone by formaldehyde and NaBH4 treatments improved bone strength and strain (deformation) so that it was comparable with normal bone. Copper deficiency blocks the formation of cross-links in collagens and elastin from various tissues. It is felt that the bone fragility related to nutritional copper deficiency is the result of decreased bone collagen cross linking. Arterial elastin metabolism was also investigated. By radioactively labeling arterial soluble elastin (tropoelastin) in vivo by an intraperitoneal injection of [G-3H]valine, it could be demonstrated that copper deficiency appeared to reduce its rate of metabolic turnover. Soluble elastin or tropoelastin is assumed to be the precursor of mature or insoluble elastin. The observations presented here are consistent with the view that by retarding the steps associated with elastin cross-link formation, the incorporation of soluble elastin into mature elastin may be retarded as well.

Topics: Animal Nutritional Physiological Phenomena; Animals; Aorta; Biomechanical Phenomena; Bone and Bones; Calcium, Dietary; Chemical Phenomena; Chemistry; Chickens; Collagen; Connective Tissue; Copper; Deficiency Diseases; Elastin; Male; Milk; Proteins; Valine

Topics: Animals; Animals, Newborn; Aorta; Cells, Cultured; Chromatography, Gel; Copper; Deficiency Diseases; Elastin; Electrophoresis, Disc; Hydroxyproline; Proline; Solubility; Swine; Tritium; Valine

Topics: Amino Acid Sequence; Animals; Aorta; Chromatography, Gas; Copper; Deficiency Diseases; Elastin; Peptides; Solubility; Swine; Trypsin

Topics: Amino Acids; Animals; Aorta; Chickens; Cholesterol; Circular Dichroism; Copper; Deficiency Diseases; Elastin; Lysine; Pancreatic Elastase; Phosphatidylcholines; Protein Binding; Protein Conformation; Protein Precursors; Pyridoxal Phosphate; Schiff Bases; Sodium Dodecyl Sulfate; Solubility; Temperature

Topics: Animal Nutritional Physiological Phenomena; Animals; Animals, Newborn; Aorta; Carbon Radioisotopes; Centrifugation; Chromatography, Gel; Collagen; Copper; Deficiency Diseases; Elastin; Electrophoresis, Disc; Molecular Weight; Protein Biosynthesis; Protein Precursors; Solubility; Swine; Urea; Valine

Topics: Animals; Aorta; Chickens; Copper; Deficiency Diseases; Elastin; Valine

Topics: Alanine; Amino Acids; Animals; Aorta; Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Copper; Deficiency Diseases; Elastin; Electrophoresis, Paper; Lysine; Peptides; Protein Conformation; Protein Precursors; Solubility; Subtilisins; Swine; Trypsin

Topics: Aldehydes; Amino Acid Oxidoreductases; Amino Acids; Ammonium Sulfate; Animals; Aorta; Body Weight; Chickens; Chromatography, Gel; Collagen; Copper; Deficiency Diseases; Elastin; Electrophoresis, Disc; Formates; Lysine; Monoamine Oxidase; Solubility; Tendons

1. Insoluble elastin has been prepared by several different methods from adult bovine and calf ligamentum nuchae. Highly purified tropoelastin has been prepared from copper-deficient porcine aorta. 2. Amino acid analyses indicated that all preparations, except that obtained from calf ligamentum nuchae by using an EDTA extraction followed by collagenase digestion (preparation E6), were typical of pure elastin having high concentrations of hydrophobic and low concentrations of hydrophilic amino acids. Preparation E6 was found to contain approx. 40% collagen. 3. The determination and composition of the carbohydrates associated with these preparations is reported. With the exception of preparation E6, the insoluble elastins contained only trace amounts of neutral sugars (0.13-0.35%, w/w) and amino sugars (0.01-0.06%, w/w). The porcine tropoelastin contained virtually no carbohydrate. 4. The results suggest that carbohydrate analyses can yield valuable information about the purity of elastin preparations.

Topics: Amino Acids; Animals; Aorta; Carbohydrates; Cattle; Chromatography; Collagen; Copper; Deficiency Diseases; Edetic Acid; Elastin; Hexosamines; Ligaments; Neck; Neuraminic Acids; Swine

Topics: Amino Acids; Animals; Aorta, Thoracic; Choline; Deficiency Diseases; Diet; Elastin; Fatty Acids, Essential; Haplorhini; Hydrolysis; Lysine; Pyridinium Compounds; Time Factors; Vitamin B 6 Deficiency

Topics: Amino Acids; Animal Nutritional Physiological Phenomena; Animals; Aorta; Aortic Rupture; Arginine; Ascorbic Acid; Collagen; Copper; Deficiency Diseases; Depression, Chemical; Elastin; Hot Temperature; Hydroxyproline; Male; Metabolism; Microscopy, Electron; Proteins; Solubility; Stimulation, Chemical; Turkeys

Topics: Alanine; Amino Acid Sequence; Amino Acids; Animals; Aorta; Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Copper; Deficiency Diseases; Elastin; Lysine; Models, Structural; Peptides; Proteins; Spectrum Analysis; Sulfonic Acids; Swine; Thiocyanates; Trypsin

Topics: 1-Propanol; Alcohols; Amino Acids; Animals; Aorta; Chemical Precipitation; Chloroform; Chromatography, Gel; Copper; Deficiency Diseases; Diet; Elastin; Freeze Drying; Methods; Quaternary Ammonium Compounds; Solubility; Sulfates; Swine; Ultracentrifugation

Topics: Animals; Collagen Diseases; Copper; Deficiency Diseases; Elastin; Lysine

Topics: Animals; Aorta; Carbon Isotopes; Chickens; Chromatography; Copper; Deficiency Diseases; Elastin; In Vitro Techniques; Lysine; Riboflavin Deficiency; Vitamin B 6 Deficiency

Topics: Aneurysm; Animals; Aorta, Thoracic; Arteries; Arteriosclerosis; Cardiovascular Diseases; Collagen; Copper; Deficiency Diseases; Elastin; Pedigree; Rupture; Swine; Vascular Diseases

Topics: Amino Acids; Animals; Aorta; Copper; Deficiency Diseases; Elastin; Hydrogen-Ion Concentration; Methods; Proteins; Sodium Chloride; Solubility; Swine

Topics: Acrylates; Amino Acid Sequence; Amino Acids; Animals; Aorta; Chemical Precipitation; Chromatography, Ion Exchange; Copper; Deficiency Diseases; Detergents; Elastin; Electrophoresis, Disc; Glycine; Hot Temperature; Lysine; Methods; Molecular Weight; Pancreatic Elastase; Peptides; Proteins; Solubility; Sulfates; Swine

Topics: Amino Acids; Animals; Aorta; Copper; Deficiency Diseases; Elastin; Electrophoresis, Disc; Proteins; Solubility; Swine

Topics: Amino Acids; Animals; Aorta; Cartilage; Cattle; Chemical Phenomena; Chemistry; Copper; Deficiency Diseases; Elastin; Ligaments; Molecular Weight; Solubility; Swine

Topics: Animals; Aorta; Chick Embryo; Copper; Deficiency Diseases; Elastin; Microscopy; Microscopy, Electron

Topics: Amino Acids; Animals; Aorta; Chickens; Copper; Deficiency Diseases; Elastin; In Vitro Techniques; Lysine; Monoamine Oxidase; Potassium Deficiency; Vitamin B 6 Deficiency

Topics: Amino Acids; Animals; Aorta; Copper; Deficiency Diseases; Elastin; Hexosamines; Hydroxyproline; In Vitro Techniques; Nitrogen; Poultry

Elastin fibers in the aortas of control, lathyritic, copper-supplemented, and copper-deficient chicks were examined histochemically and chemically for aldehyde content. Diminished staining for aldehydes was obtained in the fibers from the aortas of lathyritic and copper-deficient chicks. Chemical studies of elastin isolated from the aortas of control and lathyritic chicks showed an apparent loss of lysine residues in control elastin to be associated with an increase in aldehyde content providing evidence that lysine is converted to an aldehyde-containing intermediate during biosynthesis of desmosine and isodesmosine. Approximately 6 aldehyde groups were present for every 1000 amino acids in elastin isolated from the aortas of control animals, while the corresponding number in lathyritic elastin was 4. At least two types of aldehydes, saturated and alpha,beta-unsaturated, appear to be associated with elastin, suggesting the presence of more than one intermediate between lysine and the desmosines.

Topics: Aldehydes; Animals; Aorta; Copper; Deficiency Diseases; Elastin; Histocytochemistry; Lathyrism; Poultry

Topics: Amino Acids; Animals; Aorta; Copper; Deficiency Diseases; Elastin; In Vitro Techniques; Liver; Lysine; Poultry

Topics: Aniline Compounds; Animals; Aorta; Ascorbic Acid; Chickens; Copper; Deficiency Diseases; Diet; Digestion; Dimercaprol; Elastic Tissue; Elastin; Iron; Liver; Meat; Mortality; Pharmacology; Poultry; Radiometry; Reducing Agents; Research; Zinc

Topics: Animals; Aorta; Aorta, Thoracic; Chromatography; Copper; Deficiency Diseases; Diet; Elastin; Formates; Histocytochemistry; Pancreatic Elastase; Proteins; Research; Swine

Topics: Animals; Aorta; Aorta, Thoracic; Collagen; Copper; Deficiency Diseases; Diet; Elastic Tissue; Elastin; Histological Techniques; Histology; Pancreatic Elastase; Physiology; Research; Skin; Swine

Topics: Amino Acids; Aminopropionitrile; Animals; Aorta; Chick Embryo; Copper; Culture Techniques; Cyanides; Deficiency Diseases; Elastic Tissue; Elastin; Lathyrism; Lysine; Penicillamine

Topics: Animals; Aorta; Aortic Rupture; Copper; Deficiency Diseases; Elastic Tissue; Elastin; Research; Swine

Topics: Amino Acids; Animals; Aorta; Carbon Isotopes; Chemistry Techniques, Analytical; Copper; Deficiency Diseases; Elastic Tissue; Elastin; Meat; Metabolism; Poultry; Research; Valine

Topics: Animals; Aorta; Collagen; Copper; Deficiency Diseases; Elastin; Hexosamines; Histocytochemistry; Proteins; Research; Solubility; Swine

Topics: Animals; Aorta, Thoracic; Copper; Coronary Disease; Coronary Vessels; Deficiency Diseases; Elastic Tissue; Elastin; Iron; Pathology; Proteins; Research; Swine