muramidase and Disease

The ability of proteins to fold to their functional states following synthesis in the intracellular environment is one of the most remarkable features of biology. Substantial progress has recently been made towards understanding the fundamental nature of the mechanism of the folding process. This understanding has been achieved through the development and concerted application of a variety of novel experimental and theoretical approaches to this complex problem. The emerging view of folding is that it is a stochastic process, but one biased by the fact that native-like interactions between residues are, on average, more stable than non-native ones. The sequences of natural proteins have emerged through evolutionary processes such that their unique native states can be found very efficiently even in the complex environment inside a living cell. But under some conditions proteins fail to fold correctly, or to remain correctly folded, in living systems, and this failure can result in a wide range of diseases. One group of diseases, known as amyloidoses, which includes Alzheimer's disease and the transmissible spongiform encephalopathies, involves deposition of aggregated proteins in a variety of tissues. These diseases are particularly intriguing because evidence is accumulating that the formation of the highly organized amyloid aggregates is a generic property of polypeptides, and not simply a feature of the few proteins associated with recognized pathological conditions. That such aggregates are not normally found in properly functional biological systems is again a testament to evolution, in this case of a variety of mechanisms inhibiting their formation. Understanding the nature of such protective mechanisms is a crucial step in the development of strategies to prevent and treat these debilitating diseases.

Topics: Amyloid; Amyloidosis; Disease; Humans; Macromolecular Substances; Models, Molecular; Muramidase; Protein Folding

The purpose of this investigation was to study oral health and salivary aspects of the frail elderly. The study hypothesis was that elderly patients with many concomitant diseases and drugs would have different salivary secretion rates and biochemical constituents than healthier patients.. The stimulated flow, pH buffering capacity, and biochemical constituents were analyzed from salivas of 169 elderly subjects (51 men and 118 women, mean age 81.2 years, range 69 to 96 years) admitted to an acute geriatric ward because of sudden worsening of their health. Common statistical methods were used to analyze the differences among patient groups. The patients were grouped according to the number of concomitant diseases and daily used drugs and on the basis of salivary flow rate values.. Reduced salivary flow (< 0.7 ml/min) was found in 48% of the men and 62.5% of the women, and a low buffering capacity was found in 31.9% of the men and 36.7% of the women. Age did not significantly affect the salivary flow rate. The factors that showed the strongest influence on salivary flow were endocrinologic diseases, ophthalmologic and respiratory drugs, and potassium chloride. Salivary immunoglobulin A and immunoglobulin M concentrations were significantly higher in older patients. Immunoglobulin A, lysozyme, and amylase concentrations were significantly higher in older patients taking many drugs. Patients with many concomitant diseases had significantly higher salivary urea concentrations than healthier patients. Edentulous patients had significantly higher salivary immunoglobulin A, immunoglobulin M, lysozyme, and amylase concentrations.. In this study, hyposalivation was a frequent observation, and the elderly who took many drugs and had several systemic diseases had higher concentrations of most of the analyzed biochemical constituents.

Topics: Aged; Aged, 80 and over; Amylases; Buffers; Disease; Drug-Related Side Effects and Adverse Reactions; Endocrine System Diseases; Female; Frail Elderly; Geriatrics; Health Status; Hospital Units; Humans; Hydrogen-Ion Concentration; Immunoglobulin A, Secretory; Immunoglobulin M; Male; Mouth, Edentulous; Muramidase; Ophthalmic Solutions; Potassium Chloride; Referral and Consultation; Respiratory System Agents; Saliva; Salivation; Secretory Rate; Sex Factors; Urea; Xerostomia

Topics: Alanine; Aminopeptidases; Clinical Laboratory Techniques; Disease; Enzymes; Glucuronidase; Humans; Kidney Diseases; Muramidase; Proteinuria

Topics: Anti-Infective Agents, Local; Cervix Uteri; Disease; Female; Humans; Muramidase

Topics: Anti-Infective Agents, Local; Antiviral Agents; C-Reactive Protein; Dermatologic Agents; Disease; Eubacterium; Female; Humans; Inflammation; Muramidase; Pelvic Inflammatory Disease; Pelvis

Topics: Disease; Gastrointestinal Diseases; Humans; Lymphatic Diseases; Muramidase; Palatine Tonsil; Pharyngeal Diseases