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      Rapid Accumulation of Polymorphonuclear Neutrophils in the Corpus luteum during Prostaglandin F -Induced Luteolysis in the Cow

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          Abstract

          Prostaglandin F (PGF ) induces luteolysis within a few days in cows, and immune cells increase in number in the regressing corpus luteum (CL), implying that luteolysis is an inflammatory-like immune response. We investigated the rapid change in polymorphonuclear neutrophil (PMN) numbers in response to PGF administration as the first cells recruited to inflammatory sites, together with mRNA of interleukin-8 (IL-8: neutrophil chemoattractant) and P-selectin (leukocyte adhesion molecule) in the bovine CL. CLs were collected by ovariectomy at various times after PGF injection. The number of PMNs was increased at 5 min after PGF administration, whereas IL-8 and P-selectin mRNA increased at 30 min and 2 h, respectively. PGF directly stimulated P-selectin protein expression at 5–30 min in luteal endothelial cells (LECs). Moreover, PGF enhanced PMN adhesion to LECs, and this enhancement by PGF was inhibited by anti-P-selectin antibody, suggesting that P-selectin expression by PGF is crucial in PMN migration. In conclusion, PGF rapidly induces the accumulation of PMNs into the bovine CL at 5 min and enhances PMN adhesion via P-selectin expression in LECs. It is suggested that luteolytic cascade by PGF may involve an acute inflammatory-like response due to rapidly infiltrated PMNs.

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          Most cited references51

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          Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction.

          A new method of total RNA isolation by a single extraction with an acid guanidinium thiocyanate-phenol-chloroform mixture is described. The method provides a pure preparation of undegraded RNA in high yield and can be completed within 4 h. It is particularly useful for processing large numbers of samples and for isolation of RNA from minute quantities of cells or tissue samples.
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            Leukocyte-endothelial adhesion molecules.

            In the 9 years since the last review on leukocyte and endothelial interactions was published in this journal many of the critical structures involved in leukocyte adherence to and migration across endothelium have been elucidated. With the advent of cell and molecular biology approaches, investigations have progressed from the early descriptions by intravital microscopy and histology, to functional and immunologic characterization of adhesion molecules, and now to the development of genetically deficient animals and the first phase I trial of "anti-adhesion" therapy in humans. The molecular cloning and definition of the adhesive functions of the leukocyte integrins, endothelial members of the Ig gene superfamily, and the selectins has already provided sufficient information to construct an operative paradigm of the molecular basis of leukocyte emigration. The regulation of these adhesion molecules by chemoattractants, cytokines, or chemokines, and the interrelationships of adhesion pathways need to be examined in vitro and, particularly, in vivo. Additional studies are required to dissect the contribution of the individual adhesion molecules to leukocyte emigration in various models of inflammation or immune reaction. Certainly, new adhesion structures will be identified, and the current paradigm of leukocyte emigration will be refined. The promise of new insights into the biology and pathology of the inflammatory and immune response, and the potential for new therapies for a wide variety of diseases assures that this will continue to be an exciting area of investigation.
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              Expression cloning of a functional glycoprotein ligand for P-selectin.

              The initial adhesive interactions between circulating leukocytes and endothelia are mediated, in part, by P-selectin. We now report the expression cloning of a functional ligand for P-selectin from an HL-60 cDNA library. The predicted amino acid sequence reveals a novel mucin-like transmembrane protein. Significant binding of transfected COS cells to P-selectin requires coexpression of both the protein ligand and a fucosyltransferase. This binding is calcium dependent and can be inhibited by a neutralizing monoclonal antibody to P-selectin. Cotransfected COS cells express the ligand as a homodimer of 220 kd. A soluble ligand construct, when coexpressed with fucosyltransferase in COS cells, also mediates P-selectin binding and is immunocrossreactive with the major HL-60 glycoprotein that specifically binds P-selectin.

                Author and article information

                Contributors
                Role: Editor
                Journal
                PLoS One
                plos
                plosone
                PLoS ONE
                Public Library of Science (San Francisco, USA )
                1932-6203
                2012
                3 January 2012
                : 7
                : 1
                : e29054
                Affiliations
                [1 ]Graduate School of Animal and Food Hygiene, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Japan
                [2 ]Clinic for Cattle, University of Veterinary Medicine Hannover, Hannover, Germany
                [3 ]Institute of Immunology, University of Veterinary Medicine Hannover, Hannover, Germany
                Institut Jacques Monod, France
                Author notes

                Conceived and designed the experiments: KS AM. Performed the experiments: KS SJ SR AN. Analyzed the data: KS SJ SR AN. Contributed reagents/materials/analysis tools: HJS HB TS. Wrote the paper: KS.

                Article
                PONE-D-11-17653
                10.1371/journal.pone.0029054
                3250407
                22235260
                8a7f0123-e700-494d-9739-e0a989993888
                Shirasuna et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
                History
                : 7 September 2011
                : 19 November 2011
                Page count
                Pages: 9
                Categories
                Research Article
                Biology
                Anatomy and Physiology
                Endocrine System
                Endocrine Physiology
                Reproductive Endocrinology
                Reproductive System
                Reproductive Physiology
                Immunology
                Immunity
                Inflammation
                Immunologic Subspecialties
                Reproductive Immunology
                Zoology
                Animal Physiology
                Medicine
                Anatomy and Physiology
                Endocrine System
                Endocrine Physiology
                Reproductive Endocrinology
                Reproductive System
                Reproductive Physiology
                Clinical Immunology
                Immunity
                Inflammation
                Immunologic Subspecialties
                Reproductive Immunology
                Endocrinology
                Endocrine Physiology
                Reproductive Endocrinology
                Reproductive Endocrinology
                Veterinary Science
                Animal Types
                Large Animals

                Uncategorized
                Uncategorized

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