Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0004153 (atherosclerosis)
 77,401 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Amyloid diseases include a widely dispersed group of conditions. A part from secondary, primary, and familial amyloid diseases, and those due to endocrine tumours of the APUD system, there is a tendency to isolate a group of senile amyloid diseases affecting mainly the heart. A study in a series of 923 elderly subjects demonstrated a negative correlation between amyloid disease and atheromatosis. As certain secondary amyloid diseases, particularly those secondary to myeloma, are, inversely, sometimes associated with rapidly developing atherosclerosis, this suggests the need for further studies to define the relationship between the two processes.
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PMID:[Senile cardiac amyloidosis: study of possible relationship between amyloid and atheromatous processes in 923 cases (author's transl)]. 710 1

Amyloid deposits in the aortic intima are very common in association with atherosclerosis and aging. In the present study, a major fibril protein purified from amyloid present in human atherosclerotic plaques was shown to be a 69-amino acid N-terminal fragment of apolipoprotein AI. Although senile form of localized apolipoprotein AI-derived amyloidosis has recently been documented in pulmonary vessels of dogs, this is the first example of a localized human amyloid derived from this apolipoprotein.
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PMID:Apolipoprotein A1-derived amyloid in human aortic atherosclerotic plaques. 748 81

Serum amyloid A (SAA) proteins comprise a family of apolipoproteins coded for by at least three genes with allelic variation and a high degree of homology between species. The synthesis of certain members of the family is greatly increased in inflammation. However, SAA is not often used as an acute-phase marker despite being at least as sensitive as C-reactive protein. SAA proteins can be considered as apolipoproteins since they associate with plasma lipoproteins mainly within the high density range, perhaps through amphipathic alpha-helical structure. It is not known why certain subjects expressing SAA develop secondary systemic amyloidosis. There is still no specific function attributed to SAA; however, a popular hypothesis suggests that SAA may modulate metabolism of high density lipoproteins (HDL). This may impede the protective function of HDL against the development of atherosclerosis. The potential significance of the association between SAA and lipoproteins needs further evaluation.
Atherosclerosis 1993 Sep
PMID:Serum amyloid A (SAA): an acute phase protein and apolipoprotein. 750 91

The 1000-fold induction of acute phase serum amyloid A (A-SAA) in the liver during inflammation indicates that this protein plays an important, though ill-defined, role in host defence. Paradoxically, prolonged overproduction of A-SAA is a causative factor in secondary amyloidosis and possibly other diseases such as atherosclerosis; the ability to down-regulate A-SAA synthesis is therefore of considerable clinical importance. We have successfully generated anti-SAA hammerhead ribozymes and we report that they are capable of cleaving A-SAA mRNA in vitro.
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PMID:Ribozyme mediated cleavage of acute phase serum amyloid A (A-SAA) mRNA in vitro. 758 44

Cardiovascular complications are the main cause of mortality in patients with chronic renal failure. Hypertension and lipid abnormalities which often lead to left ventricular hypertrophy and accelerated atherosclerosis as well as coronary artery disease are a common cause of death. On the other hand uremia often causes pericarditis and thereby may lead to cardiac tamponade and constrictive pericarditis. Renal failure can also cause secondary hyperparathyroidism, amyloidosis, hemosiderosis and oxalosis which can produce visceral infiltrations and lead to a variety of disturbances of cardiovascular functions. Life-threatening arrhythmias are one of the major cardiovascular complications during maintenance dialysis as their occurrence might result in sudden death. The aim of cardiologic management which includes the complex of preventive and therapeutic measures is to reduce the morbidity and mortality and to improve the quality of life.
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PMID:[Cardiologic management in patients on a long-term dialysis program]. 763 9

A prominent feature in several diseases is the accumulation of connective tissue. The ultimate result of high levels of extracellular matrix is organ failure and death, evident in diseases such as liver fibrosis, diabetes and amyloidosis. Among the extracellular matrix components, proteoglycans play a basic role in several pathological conditions. In the development of atherosclerosis they provide an anchor for lipoprotein lipase on the endothelial wall, sequester lipoproteins in the subendothelial matrix and present lipoproteins to macrophages. In diabetes these proteoglycans have a lower charge, such that the network has a reduced capacity to retain negatively charged proteins. In fibrosis and amyloidosis the synthesis of proteoglycans and matrix is increased and large amounts are deposited at the expense of tissue-specific cells. Some of the conditions mentioned can be ameliorated by changes in the diet.
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PMID:[The significance of proteoglycans in several diseases]. 799 94

Serum amyloid A (SAA) is a plasma protein which has been associated with several diseases, including amyloidosis, arthritis, and atherosclerosis, and its abnormal expression, particularly in nonhepatic cells, is implicated in the pathogenesis of these diseases. Transfection and DNA-binding studies were performed to investigate the mechanism controlling cytokine-induced, nonhepatic expression of the SAA gene. We have identified a novel promoter, located between positions -280 and 224, that confers interleukin-6 (IL-6) inducibility to an SAA-chloramphenicol acetyltransferase reporter gene in both nonhepatic and hepatic cells. DNase I protection assays revealed, within this region, three homologous highly pyrimidine rich octanucleotide sequence motifs, termed SAA-activating sequences (SAS). Specific mutations within these three SAS motifs severely reduced IL-6-mediated induction of the reporter gene in transfected nonhepatic cells but not in liver cells. A nuclear factor activated by IL-6 in both hepatic and nonhepatic cells efficiently interacts with the SAS. The induction kinetics and cycloheximide sensitivity of this SAS-binding factor (SAF) suggested that de novo synthesis of this factor itself or an activator protein is essential. Loss of DNA-binding ability as a result of in vitro dephosphorylation, induction of SAA-chloramphenicol acetyltransferase reporter gene activity in the presence of genistein, a protein kinase inhibitor, further indicate that a phosphorylation step is necessary for the activation of SAF. Our results suggest that SAF is a key regulator of cytokine-mediated SAA gene expression in some nonhepatic cells.
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PMID:A novel cis-acting element is essential for cytokine-mediated transcriptional induction of the serum amyloid A gene in nonhepatic cells. 865 33

Advanced glycation end-products (AGEs) are formed by spontaneous chemical reactions between carbohydrates and tissue proteins. The accumulation of AGEs in long-lived proteins contributes to the age-related increase in brown colour, fluorescence and insolubilisation of lens crystallins and to the gradual crosslinking and decrease in elasticity of connective tissue collagens with age. These nonenzymatic reactions, known collectively as Maillard or browning reactions, are also implicated in the development of pathophysiology in age-related diseases such as diabetes mellitus, atherosclerosis, Alzheimer's disease, and in dialysis-related amyloidosis. Oxygen and oxidation reactions accelerates Maillard reactions in vitro, and the structurally characterised AGEs that accumulate in long-lived tissue proteins are in fact glycoxidation products, formed by sequential glycation and oxidation reactions. In addition to their immediate effects on protein structure and function, AGEs also induce oxidative stress, leading to inflammation and propagation of tissue damage. Thus, glycation of protein, formation of AGEs and resultant oxidative stress, which accelerate Maillard reactions, can initiate an autocatalytic cycle of deleterious reactions in tissues. Pharmacological inhibition of the Maillard reaction should improve the prognosis for a broad range of age-related diseases. The role of oxidative stress as a catalyst and the consequences of Maillard reaction damage in tissues suggests that antioxidant therapy may also retard the progression of age-related pathology.
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PMID:Role of the Maillard reaction in diabetes mellitus and diseases of aging. 882 Jul 92

Long-term incubation of proteins with glucose leads to the formation of advanced glycation end products (AGEs), which are characterized by fluorescence, brown color, and cross-linking. Formation of AGEs in vitro requires oxygen and is dependent on transition metal-catalyzed oxidation of glucose or Amadori products. AGEs are thought to be involved in aging and age-enhanced diseases such as diabetic complications, atherosclerosis, dialysis-related amyloidosis, and Alzheimer's disease. Chronic exposure of the skin to sunlight induces hyperplasia of the elastic tissue in the upper dermis known as actinic elastosis. Herein we used a monoclonal anti-AGE antibody (6D12) whose epitope is N(epsilon)-(carboxymethyl)lysine (CML), one of the glycoxidation products of AGEs, and demonstrated that the lesions of actinic elastosis were modified by CML. Further immunohistochemical and immunoelectron microscopic examination with 6D12 demonstrated CML accumulates predominantly in elastic fibers especially in the amorphous electron-dense materials corresponding to photo-induced degenerated area rather than the electron-lucent region. Immunochemical analyses with enzyme-linked immunosorbent assay (ELISA) of elastase-soluble fractions demonstrated that the CML levels of the sun-exposed area were significantly higher than those of the sun-unexposed area. We conclude that ultraviolet-induced oxidation may accelerate CML formation in actinic elastosis of photoaged skin.
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PMID:Photo-enhanced modification of human skin elastin in actinic elastosis by N(epsilon)-(carboxymethyl)lysine, one of the glycoxidation products of the Maillard reaction. 912 35

Serum amyloid A (SAA) is a plasma protein that is associated with many inflammatory diseases including amyloidosis, arthritis, and atherosclerosis. SAA level is significantly increased during inflammatory condition, and such abnormal expression of this protein is linked to the pathogenesis of the above-mentioned diseases. A promoter element, designated as SAA-activating sequence (SAS), located between -280 and -226 has been implicated in the induction mechanism and a nuclear factor, SAS-binding factor (SAF), has been shown to bind to this region. In this report, using a cloned SAF gene in transient transfection assay, we provide evidence that SAF potentiates SAA gene expression through SAS element. Furthermore, we show that during lipopolysaccharide-mediated induction of SAF, heteromeric complex with transcription factor Sp1 is formed. Transfection assays using both transcription factor genes have demonstrated that SAF-Sp1 heteromer is a highly potent transactivator of SAA expression.
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PMID:Induction of serum amyloid A (SAA) gene by SAA-activating sequence-binding factor (SAF) in monocyte/macrophage cells. Evidence for a functional synergy between SAF and Sp1. 936 Sep 66


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