Data being collected on product-related accidents.
Explore the source record for details and available documents.
Accidents, Home↗
Biomedical subjects
E B Cook
Publications and source records attributed to E B Cook.
Total contractile protein contents and gene expression in skeletal muscle in response to chronic ethanol consumption in the rat.
An investigation was carried out to determine changes in the contents of skeletal muscle myofibrillary proteins (i.e., the contractile fraction composed principally of actin and myosin) and gene expression in skeletal muscle in response to ethanol feeding. Male Wistar rats were fed a nutritionally complete liquid diet, which contained 35% of total calories as ethanol. Controls were pair-fed isocaloric amounts of the same diet, in which ethanol was replaced by isocaloric glucose. Total mixed and contractile protein contents of the gastrocnemius in ethanol-fed rats were rapidly reduced by ethanol feeding: a response was discernible as early as 1 week after the commencement of the ethanol feeding regimen (approx. -10%, p < 0.025 and p = 0.05 for mixed and myofibrillary proteins, respectively). At 2, 4, and 6 weeks, mixed and myofibrillary protein contents were further reduced in alcohol-fed rats, by between 12% and 22%, compared to pair-fed controls. Similar changes occurred in the soluble (i.e., sarcoplasmic) protein fractions of skeletal muscle. At 2 weeks the composition of total messenger RNA and individual messenger RNA species was measured. Total messenger RNA content per muscle was reduced by 35% (p < 0.05). Messenger RNA levels for alpha-actin, beta-myosin heavy chain, and carbonic anhydrase III were not significantly altered. In conclusion, skeletal muscle protein contents are rapidly reduced by ethanol feeding, compared to pair-fed controls, though mRNA species encoding specific isoforms of myosin and actin are not affected. It is possible that chronic ethanol feeding may significantly alter the stability of mRNAs encoding other contractile proteins, or alternatively, defects in translation may predominate.
Actins↗
Antihistamines and epithelial cells.
Antihistamines have long been utilized in the symptomatic management (antihistaminic effects) of allergic rhinitis and conjunctivitis. Investigation into the nonsedating second-generation antihistamines suggests that they also possess antiinflammatory activity, and may be useful in the management of inflammation associated with allergic airway disease. In vitro studies have shown that these antihistamines decrease the migration and activation of eosinophils and diminish the release of pro-inflammatory mediators from mast cells and basophils after induction by immunological and nonimmunological stimuli. In vivo studies have also demonstrated that these antihistamines decrease inflammatory cell infiltration in allergic airway disease, and mediator release from mast cells and basophils. Epithelial cells, due to their spatial arrangement and predominance in the airways, play a pivotal role in the etiology of airway disease. There is evidence that antihistamines may modulate airway inflammation by influencing the activity of these airway epithelial cells. Studies have shown that expression of adhesion molecules on epithelial cells is decreased by second-generation antihistamines. Collectively, these studies suggest that second-generation H1-histamine receptor antagonists have potential use either as safe antiinflammatory alternatives to corticosteroids or as rescue medication in combination with corticosteroids for the management of severe airway disease.
Anti-Inflammatory Agents, Non-Steroidal↗
Conjunctival mast cells in ocular allergic disease.
Allergic eye disease is a common clinical problem adversely affecting the quality of life for millions of sufferers. This ocular process is associated with IgE-mediated conjunctival inflammation leading to signs of immediate hypersensitivity including redness, itching, and tearing. Pathologic studies have shown that the conjunctiva contains mast cells that when sensitized with IgE antibody and exposed to environmental allergens can release mediators of allergic inflammation. The type, release kinetics, and concentration of these mediators in the conjunctiva have not been completely characterized. The ability to isolate and purify mast cells and epithelial cells from human conjunctival tissue has permitted the study of mediator release and cell-to-cell signaling in this tissue. Our laboratory has developed in vitro and in vivo models to better understand how inflammatory cells are recruited to and infiltrate conjunctival tissues. These models demonstrate that mast cell activation may supply sufficient cytokine signaling to initiate and direct the well-orchestrated trafficking of eosinophils to the ocular surface, facilitate their adhesion, and cause release of potent mediators of ocular inflammation.
Conjunctiva↗
Eotaxin: what we know, and what we would like to know.
Explore the source record for details and available documents.
Animals↗
Epithelial cells are a major cellular source of the chemokine eotaxin in the guinea pig lung.
Eotaxin is the major eosinophil chemoattractant found in bronchoalveolar lavage (BAL) fluid from sensitized guinea pigs after antigen challenge. In this study we have performed immunostaining for eotaxin in airways obtained from challenged animals and examined purified guinea pig lung cells (epithelial cells > 98% purity, mast cells > 90% purity) for eotaxin mRNA and protein. In the airways of antigen (ovalbumin) challenged animals, significant amounts of epithelial cell eotaxin immunostaining were observed. Northern analysis of total RNA obtained from unchallenged, freshly isolated airway epithelial cells contained high levels of eotaxin mRNA. Semi-pure and high purity lung mast cell preparations (challenged or unchallenged) did not express eotaxin mRNA. Western analysis of supernatant fluids obtained from incubated airway epithelial cells demonstrated detectable amounts of eotaxin protein, with the majority of the protein being cell-associated. Thus, airway epithelial cells are identified as a major cellular source of eotaxin in the guinea pig pulmonary system.
Animals↗
Cytokines, chemokines, RANTES, and eotaxin.
Over the past several years, a number of cytokines with chemoattractive properties (chemokines) have been identified. These low molecular weight molecules have been shown to be important leukocyte chemical attractants to sites of inflammation and infection. Chemokines act on leukocytes through selective receptors and are now known to function also in leukocyte maturation, trafficking, and homing of these cells. RANTES and eotaxin (among other chemokines) are important chemoattractants for eosinophils. Since eosinophils seem to play a critical role in the production of allergic inflammation, an understanding of the mechanism of action of these chemokines may lead to new therapies for asthma and other allergic processes.
Animals↗
Severe cold agglutinin disease and cryoglobulinemia secondary to a monoclonal anti-Pr2 IgM lambda cryoagglutinin.
OBJECTIVE: To present a case of cold agglutinin disease/cryoglobulinemia secondary to a monoclonal anti-Pr2 IgM lambda antibody, and review the literature on the occurrence of this antibody in cold-induced disease and the clinical disease associated with it. METHODS: Cryoantibody characteristics were evaluated by cold precipitation. The antigen specificity of the monoclonal IgM lambda antibody was evaluated using techniques of selective red blood cell absorption. RESULTS: In our patient, we were able to identify an antibody with both cryoglobulinemic and cold agglutinin (cryoagglutinin) properties. This antibody was found to be monoclonal IgM lambda with specificity to the Pr2 antigen on red blood cells. CONCLUSIONS: Monoclonal IgM lambda anti-Pr is a rarely found cold agglutinin antibody. In this report we describe the clinical course of a patient who had this antibody, which not only agglutinated red cells in the cold but also had cryoglobulin properties. The clinical illness of this man was characterized by severe acrocyanosis and digital necrosis with eventual organ necrosis and death. We also review the literature on cold induced disease due to monoclonal anti-Pr IgM lambda antibody. Our patient was found to be unique among the reports reviewed. Our case is the first to report both cold agglutinin and cryoglobulinemic properties with the evaluation of the thermal amplitudes of these activities of the antibody. Also, unlike the lymphoproliferative malignancy observed in the cold agglutinin-associated disease in the other reports, our patient's disease was associated with a monoclonal B-cell expansion on the spectrum between benign monoclonal gammopathy and a low grade lymphoproliferative disorder.
Aged↗