| Human versus mouse eosinophils: "that which we call an eosinophil, by any other name would stain as red". | |
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MedLine Citation:
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PMID: 22935586 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The respective life histories of human subjects and mice are well defined and describe a unique story of evolutionary conservation extending from sequence identity within the genome to the underpinnings of biochemical, cellular, and physiologic pathways. As a consequence, the hematopoietic lineages of both species are invariantly maintained, each with identifiable eosinophils. This canonical presence nonetheless does not preclude disparities between human and mouse eosinophils, their effector functions, or both. Indeed, many books and reviews dogmatically highlight differences, providing a rationale to discount the use of mouse models of human eosinophilic diseases. We suggest that this perspective is parochial and ignores the wealth of available studies and the consensus of the literature that overwhelming similarities (and not differences) exist between human and mouse eosinophils. The goal of this review is to summarize this literature and in some cases provide experimental details comparing and contrasting eosinophils and eosinophil effector functions in human subjects versus mice. In particular, our review will provide a summation and an easy-to-use reference guide to important studies demonstrating that although differences exist, more often than not, their consequences are unknown and do not necessarily reflect inherent disparities in eosinophil function but instead species-specific variations. The conclusion from this overview is that despite nominal differences, the vast similarities between human and mouse eosinophils provide important insights as to their roles in health and disease and, in turn, demonstrate the unique utility of mouse-based studies with an expectation of valid extrapolation to the understanding and treatment of patients. |
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Authors:
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James J Lee; Elizabeth A Jacobsen; Sergei I Ochkur; Michael P McGarry; Rachel M Condjella; Alfred D Doyle; Huijun Luo; Katie R Zellner; Cheryl A Protheroe; Lian Willetts; William E Lesuer; Dana C Colbert; Richard A Helmers; Paige Lacy; Redwan Moqbel; Nancy A Lee |
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Publication Detail:
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Type: Journal Article; Review |
Journal Detail:
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Title: The Journal of allergy and clinical immunology Volume: 130 ISSN: 1097-6825 ISO Abbreviation: J. Allergy Clin. Immunol. Publication Date: 2012 Sep |
Date Detail:
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Created Date: 2012-08-31 Completed Date: 2012-11-07 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 1275002 Medline TA: J Allergy Clin Immunol Country: United States |
Other Details:
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Languages: eng Pagination: 572-84 Citation Subset: AIM; IM |
Copyright Information:
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Copyright © 2012 American Academy of Allergy, Asthma & Immunology. Published by Mosby, Inc. All rights reserved. |
Affiliation:
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Division of Pulmonary Medicine, Department of Biochemistry and Molecular Biology, Mayo Clinic Arizona, Scottsdale, AZ, USA. jjlee@mayo.edu |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Degranulation Eosinophil Cationic Protein / physiology Eosinophil Peroxidase / physiology Eosinophils / physiology* Evolution, Molecular Glycoproteins / physiology Hematopoiesis Humans Lysophospholipase / physiology Mice |
| Grant Support | |
ID/Acronym/Agency:
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R01 AR061567/AR/NIAMS NIH HHS; R01 HL058723/HL/NHLBI NIH HHS; R01 HL060793/HL/NHLBI NIH HHS; R01 HL065228/HL/NHLBI NIH HHS; R56 HL058723/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Glycoproteins; 0/lysolecithin acylhydrolase; EC 1.11.1.-/Eosinophil Peroxidase; EC 3.1.1.5/Lysophospholipase; EC 3.1.27.-/Eosinophil Cationic Protein |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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