Human eosinophil major basic protein induces airway constriction and airway hyperresponsiveness in primates.

Gundel, Robert H.; Letts, L. Gordon; Gleich, Gerald J.

doi:10.1172/jci115155

Cited by 296 publications

(162 citation statements)

References 16 publications

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“…Parasite killing and tissue damage found in allergic lesions are both linked to production of toxic oxygen metabolites and to the release of eosinophil granule proteins by degranulation or exocytosis [2][3][4]. Eosinophil-derived cytotoxic proteins include major basic protein (MBP), eosinophil peroxidase (EPO), eosinophil cationic protein (ECP), and eosinophil-derived neurotoxin (EDN) [1,5].…”

Section: Introductionmentioning

confidence: 99%

C/EBP regulates the promoter of the eosinophil-derived neurotoxin/RNS2 gene in human eosinophilic cells

Baltus¹,

Buitenhuis²,

Dijk³

et al. 1999

Journal of Leukocyte Biology

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Section: Introductionmentioning

confidence: 99%

C/EBP regulates the promoter of the eosinophil-derived neurotoxin/RNS2 gene in human eosinophilic cells

Baltus¹,

Buitenhuis²,

Dijk³

et al. 1999

Journal of Leukocyte Biology

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“…Sheep offer a unique experimental system in which large numbers of eosinophils can be obtained using the relatively non-invasive procedure of mammary infusion of allergens followed by "milking" of the mammary gland to obtain the inflammatory cells recruited into the lumen (5,6). Using this experimental system, the present study describes the identification of a novel galectin (galectin-14) specifically expressed by eosinophils.…”

mentioning

confidence: 99%

Isolation and Characterization of a Novel Eosinophil-specific Galectin Released into the Lungs in Response to Allergen Challenge

Dunphy¹,

Barcham²,

Bischof³

et al. 2002

Journal of Biological Chemistry

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A novel galectin cDNA (galectin-14) was cloned from ovine eosinophil-rich leukocytes by low stringency reverse transcriptase-PCR and cDNA library screening. Data base searches indicate that this gene encodes a novel prototype galectin that contains one putative carbohydrate recognition domain and exhibits most identity to galectin-9/ecalectin, a potent eosinophil chemoattractant. The sugar binding properties of the recombinant molecule were confirmed by a hemagglutination assay and lactose inhibition. The mRNA and protein of galectin-14 are expressed at high levels in eosinophilrich cell populations. Flow cytometry and cytospot staining demonstrate that the protein localizes to the cytoplasmic, but not the granular, compartment of eosinophils. In contrast, galectin-14 mRNA and protein were not detected in neutrophils, macrophages, or lymphocytes. Western blot analysis of bronchoalveolar lavage fluid indicates that galectin-14 is released from eosinophils into the lumen of the lungs after challenge with house dust mite allergen. The restricted expression of this novel galectin to eosinophils and its release into the lumen of the lung in a sheep asthma model indicates that it may play an important role in eosinophil function and allergic inflammation.The immune response of mammals to multicellular parasite infections and allergens is characterized by the recruitment of eosinophils (1, 2). The role eosinophils play in both parasite infections and allergic reactions remains controversial, and little is known of the specific function of eosinophil constituents in combating multicellular parasites or exacerbating allergic responses. The presence of eosinophils and eosinophil-derived products in the respiratory tract does, however, correlate with the pathological manifestations of allergic asthma (2-4).One of the limitations in the study of eosinophils is the scarcity of this cell population in normal individuals and the difficulty in obtaining sufficient numbers of unmanipulated cells from allergic tissues. Sheep offer a unique experimental system in which large numbers of eosinophils can be obtained using the relatively non-invasive procedure of mammary infusion of allergens followed by "milking" of the mammary gland to obtain the inflammatory cells recruited into the lumen (5, 6). Using this experimental system, the present study describes the identification of a novel galectin (galectin-14) specifically expressed by eosinophils. The expression of galectin-14 was up-regulated in the lung tissue of sensitized sheep challenged with house dust mite extract (HDM), 1 and the protein was released into the bronchoalveolar lavage (BAL) fluid.Galectins are carbohydrate binding proteins that have been increasingly implicated in both adaptive and innate immune responses. The eosinophil-specific expression of galectin-14 and its secretion into the lumen of the lung in a sheep asthma model indicates that it may play an important role in regulating the activity of eosinophils during allergic responses and further highlights the i...

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“…The correlative association between AHR and MBP-1 (and therefore eosinophils) has been documented in several mammalian species, including humans (15)(16)(17)(18). Several studies have defined a potential causative mechanism resulting in AHR by linking eosinophil effector function, mediated by MBP-1 release, and muscarinic receptor dysfunction (17)(18)(19)(20).…”

mentioning

confidence: 99%

Eosinophil Major Basic Protein-1 Does Not Contribute to Allergen-Induced Airway Pathologies in Mouse Models of Asthma

Denzler

Farmer

Crosby

et al. 2000

The Journal of Immunology

114

105

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The relationship between eosinophils and the development of Ag-induced pulmonary pathologies, including airway hyper-responsiveness, was investigated using mice deficient for the secondary granule component, major basic protein-1 (mMBP-1). The loss of mMBP-1 had no effect on OVA-induced airway histopathologies or inflammatory cell recruitment. Lung function measurements of knockout mice demonstrated a generalized hyporeactivity to methacholine-induced airflow changes (relative to wild type); however, this baseline phenotype was observable only with methacholine; no relative airflow changes were observed in response to another nonspecific stimulus (serotonin). Moreover, OVA sensitization/aerosol challenge of wild-type and mMBP-1−/− mice resulted in identical dose-response changes to either methacholine or serotonin. Thus, the airway hyper-responsiveness in murine models of asthma occurs in the absence of mMBP-1.

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Human eosinophil major basic protein induces airway constriction and airway hyperresponsiveness in primates.

Cited by 296 publications

References 16 publications

C/EBP regulates the promoter of the eosinophil-derived neurotoxin/RNS2 gene in human eosinophilic cells

C/EBP regulates the promoter of the eosinophil-derived neurotoxin/RNS2 gene in human eosinophilic cells

Isolation and Characterization of a Novel Eosinophil-specific Galectin Released into the Lungs in Response to Allergen Challenge

Eosinophil Major Basic Protein-1 Does Not Contribute to Allergen-Induced Airway Pathologies in Mouse Models of Asthma

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