Pollen grains are ubiquitous triggers of allergic asthma and seasonal rhinitis. Proteolytic enzymes in pollen as well as other sources are capable of disrupting airway epithelial integrity in vivo and in vitro. This provides a plausible mechanism for the initiation of sensitisation of the respiratory immune system to inhaled pollen allergens, comparable to that suggested for Group 1 allergens from house dust mites and cat dander, which are known to possess intrinsic proteolytic activity. This thesis explores the relationship between pollen allergens and proteolytic enzymes. It describes the different strategies used for the characterisation, purification and identification of immunogenic and proteolytic proteins in the complex mixtures of pollen diffusates. The peptidases in the diffusates of Kentucky blue grass, ryegrass and Bermuda grass pollens were characterised by a sensitive fluorescence assay and gelatin zymography. Among these, Bermuda grass pollen demonstrated the presence of a serine peptidase at Mr ~30,000 Da, which corresponded to an intense band by Western blotting using a monoclonal antibody to the timothy grass (Phleum pratense) group 1 allergen, Phl p 1. Purification of this enzyme from Bermuda grass was complicated by the low levels of the enzyme present in the diffusate, as well as by its autohydrolysis. Partial purification of the serine peptidase activity by affinity chromatography using Concanavalin A Sepharose demonstrated that the diffusate contained a trypsin-like peptidase, detected by the fluorescent assay, in addition to the ~30,000 Da serine endopeptidase, detected on gelatin zymography. Proteomic analysis of the ~30,000 Da protein using one- and two-dimensional electrophoresis and mass spectrometry identified it as the major pollen allergen of Bermuda grass, Cyn d 1. The studies reported here provide, for the first time, evidence that a pollen allergen may possess intrinsic proteolytic activity. This activity may play a role in the initiation of airway inflammation and allergic sensitisation.

Pollen grains are ubiquitous triggers of allergic asthma and seasonal rhinitis. Proteolytic enzymes in pollen as well as other sources are capable of disrupting airway epithelial integrity in vivo and in vitro. This provides a plausible mechanism for the initiation of sensitisation of the respiratory immune system to inhaled pollen allergens, comparable to that suggested for Group 1 allergens from house dust mites and cat dander, which are known to possess intrinsic proteolytic activity. This thesis explores the relationship between pollen allergens and proteolytic enzymes. It describes the different strategies used for the characterisation, purification and identification of immunogenic and proteolytic proteins in the complex mixtures of pollen diffusates. The peptidases in the diffusates of Kentucky blue grass, ryegrass and Bermuda grass pollens were characterised by a sensitive fluorescence assay and gelatin zymography. Among these, Bermuda grass pollen demonstrated the presence of a serine peptidase at Mr ~30,000 Da, which corresponded to an intense band by Western blotting using a monoclonal antibody to the timothy grass (Phleum pratense) group 1 allergen, Phl p 1. Purification of this enzyme from Bermuda grass was complicated by the low levels of the enzyme present in the diffusate, as well as by its autohydrolysis. Partial purification of the serine peptidase activity by affinity chromatography using Concanavalin A Sepharose demonstrated that the diffusate contained a trypsin-like peptidase, detected by the fluorescent assay, in addition to the ~30,000 Da serine endopeptidase, detected on gelatin zymography. Proteomic analysis of the ~30,000 Da protein using one- and two-dimensional electrophoresis and mass spectrometry identified it as the major pollen allergen of Bermuda grass, Cyn d 1. The studies reported here provide, for the first time, evidence that a pollen allergen may possess intrinsic proteolytic activity. This activity may play a role in the initiation of airway inflammation and allergic sensitisation.

Pollen grains are ubiquitous triggers of allergic asthma and seasonal rhinitis. Proteolytic enzymes in pollen as well as other sources are capable of disrupting airway epithelial integrity in vivo and in vitro. This provides a plausible mechanism for the initiation of sensitisation of the respiratory immune system to inhaled pollen allergens, comparable to that suggested for Group 1 allergens from house dust mites and cat dander, which are known to possess intrinsic proteolytic activity. This thesis explores the relationship between pollen allergens and proteolytic enzymes. It describes the different strategies used for the characterisation, purification and identification of immunogenic and proteolytic proteins in the complex mixtures of pollen diffusates. The peptidases in the diffusates of Kentucky blue grass, ryegrass and Bermuda grass pollens were characterised by a sensitive fluorescence assay and gelatin zymography. Among these, Bermuda grass pollen demonstrated the presence of a serine peptidase at Mr ~30,000 Da, which corresponded to an intense band by Western blotting using a monoclonal antibody to the timothy grass (Phleum pratense) group 1 allergen, Phl p 1. Purification of this enzyme from Bermuda grass was complicated by the low levels of the enzyme present in the diffusate, as well as by its autohydrolysis. Partial purification of the serine peptidase activity by affinity chromatography using Concanavalin A Sepharose demonstrated that the diffusate contained a trypsin-like peptidase, detected by the fluorescent assay, in addition to the ~30,000 Da serine endopeptidase, detected on gelatin zymography. Proteomic analysis of the ~30,000 Da protein using one- and two-dimensional electrophoresis and mass spectrometry identified it as the major pollen allergen of Bermuda grass, Cyn d 1. The studies reported here provide, for the first time, evidence that a pollen allergen may possess intrinsic proteolytic activity. This activity may play a role in the initiation of airway inflammation and allergic sensitisation.

Diss. (sammanfattning) Stockholm : Karol. inst., 2001. / Härtill 5 uppsatser.

Diss. (sammanfattning) Stockholm : Karol. inst., 2000. / Härtill 5 uppsatser.

No description available.

A Thesis submitted to The University of Arizona College of Medicine - Phoenix in partial fulfillment of the requirements for the Degree of Doctor of Medicine. / Aeroallergens are implicated in the pathogenesis of eosinophilic esophagitis, which has a recurrent or relapsing nature. We aim to determine the incidence of seasonal disease recurrence, referred to as flares, of eosinophilic esophagitis in patients in Arizona with eosinophilic esophagitis in remission, and to characterize the presence of allergy and other disease co‐morbidities in patients that experience disease flare. A retrospective study was performed by analyzing data from visits of patients aged 5 to 18 years coded for eosinophilic esophagitis in remission seen by the Phoenix Children’s Hospital Pediatric Gastroenterology Department between June 2010 and June 2011. The data included 148 patients and 326 clinical visits. Data identified demographic information, allergy, and other disease co‐morbidities. Arizona seasons were defined as: spring from February 15 to June 15, and fall from September 1 to November 30, according to the typical pattern of allergen pollination. To analyze incidence and season of flares, statistical methods used included the Chi‐square tests and logistic regressions. Ninety‐four of 148 patients (63.5%) flared during the study period. An increased incidence of flares in the fall compared with other seasons was statistically significant (p = 0.041). Flares in the spring also had an increased incidence. Of the 94 patients that flared, 70 patients (74.5%) had environmental allergy, 83 (88.3%) had food allergy, and 66 (70.2%) had both environmental and food allergy. Our findings suggest a role for seasonal environmental allergens in the pathogenesis of eosinophilic esophagitis and disease flares in children in Arizona, particularly those with food allergy, environmental allergy, or both.

Introduction: Exposure to airborne natural rubber latex proteins has become an important occupational health concern, particularly among healthcare workers. The main purpose of this study was to investigate the levels of latex aeroallergens in South African dental schools. Methods: Area (n=95) and personal (n=369) samples as well as rubber containing gloves and dental devices (n=19) were collected in 5 dental schools. The air samples were collected at a flow rate of 2.5L/min using polycarbonate (PC) filters. Latex allergens (hev b 1, hev b 3, hev b 5 and hev b 6.02) were quantified in filters and rubber extracts by a capture enzyme immunoassay. Data was analysed using STATA 9 computer software (StataCorp, 1984-2007, Texas, USA). Non parametric tests were applied as the data was skewed. The data was interpreted as ‘low’ with less than 10ng/m3; ‘moderate’ with levels between 10-50ng/m3 and ‘high’ with greater than 50ng/m3. Results: Aeroallergen concentrations varied among institutions in our study, ranging from 1.84 to 46.1ng/m3 for personal and 1.33 to 14.97ng/m3 for area samples. Hev b 6.02 was below the detection limit for 86.5% of air samples. This study also found that exposure levels differed by departments and job type. Powdered latex products showed higher allergen concentrations compared to the non-powdered products (p=0.035) and also differed significantly by the type of brands (p=0.022). Hev b 6.02 was the most prominent allergen in powdered gloves and dams. Conclusion: The air sampling method and capture enzyme immunoassay used in this study offer means for evaluation of airborne allergen concentrations. The initiative to use non-powdered low protein latex gloves and dams should be implemented as a preventive measure.

Thesis (M.S.)--Florida State University, 2004. / Advisor: Dr. Shridhar K. Sathe, Florida State University, College of Human Sciences, Dept. of Nutrition, Food and Exercise Sciences. Title and description from dissertation home page (viewed June 15, 2004). Includes bibliographical references.

Diss. (sammanfattning) Stockholm : Karol. inst., 2004. / Härtill 4 uppsatser.