The stimulus-dependent release of eosinophil cationic protein and eosinophil protein x increases in apoptotic eosinophils. 2003

K Seton, and L Håkansson, and M Karawajczyk, and P Venge
Department of Medical Sciences, Unit of Clinical Chemistry, University Hospital, Uppsala University, Sweden. kristina.seton@medsci.uu.se

Apoptotic cells are regarded as inert bodies that turn off intracellular processes and functional abilities. To study the changes in the ability of eosinophils to release their granule proteins while undergoing apoptosis. Eosinophils were cultured for up to 72 h. Living cells were separated from the apoptotic cells and their release of eosinophil cationic protein (ECP) and eosinophil protein X (EPX) was measured in response to serum-opsonized sephadex particles and phorbol 12-myristate 12-acetate (PMA). Changes in cell structure were examined by electron microscopy, and surface receptor expression of beta1- and beta2-integrins was investigated by flow cytometry. Stimulus-dependent release of the granule proteins ECP and EPX was found to increase in apoptotic eosinophils, whereas surface expression of beta1- and beta2-integrins was downregulated. Ultrastructural examination revealed that the granules of apoptotic eosinophils were translocated to the periphery of the cell, just beneath the plasma membrane. Apoptotic eosinophils are able to release their toxic granule proteins, which is probably because of the rearrangement of the cytoskeleton and spontaneous translocation of granules to the membrane. Our results suggest that apoptotic eosinophils are potentially harmful cells that have retained their ability to react to certain extracellular stimuli. The findings point to unexpected consequences of eosinophil apoptosis.

UI MeSH Term Description Entries
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D001798 Blood Proteins Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins. Blood Protein,Plasma Protein,Plasma Proteins,Serum Protein,Serum Proteins,Protein, Blood,Protein, Plasma,Protein, Serum,Proteins, Blood,Proteins, Plasma,Proteins, Serum
D004804 Eosinophils Granular leukocytes with a nucleus that usually has two lobes connected by a slender thread of chromatin, and cytoplasm containing coarse, round granules that are uniform in size and stainable by eosin. Eosinophil
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012260 Ribonucleases Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-. Nucleases, RNA,RNase,Acid Ribonuclease,Alkaline Ribonuclease,Ribonuclease,RNA Nucleases,Ribonuclease, Acid,Ribonuclease, Alkaline
D013755 Tetradecanoylphorbol Acetate A phorbol ester found in CROTON OIL with very effective tumor promoting activity. It stimulates the synthesis of both DNA and RNA. Phorbol Myristate Acetate,12-Myristoyl-13-acetylphorbol,12-O-Tetradecanoyl Phorbol 13-Acetate,Tetradecanoylphorbol Acetate, 4a alpha-Isomer,12 Myristoyl 13 acetylphorbol,12 O Tetradecanoyl Phorbol 13 Acetate,13-Acetate, 12-O-Tetradecanoyl Phorbol,Acetate, Phorbol Myristate,Acetate, Tetradecanoylphorbol,Myristate Acetate, Phorbol,Phorbol 13-Acetate, 12-O-Tetradecanoyl,Tetradecanoylphorbol Acetate, 4a alpha Isomer
D015550 Cell Degranulation The process of losing secretory granules (SECRETORY VESICLES). This occurs, for example, in mast cells, basophils, neutrophils, eosinophils, and platelets when secretory products are released from the granules by EXOCYTOSIS. Degranulation, Cell
D017209 Apoptosis A regulated cell death mechanism characterized by distinctive morphologic changes in the nucleus and cytoplasm, including the endonucleolytic cleavage of genomic DNA, at regularly spaced, internucleosomal sites, i.e., DNA FRAGMENTATION. It is genetically programmed and serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth. Apoptosis, Extrinsic Pathway,Apoptosis, Intrinsic Pathway,Caspase-Dependent Apoptosis,Classic Apoptosis,Classical Apoptosis,Programmed Cell Death,Programmed Cell Death, Type I,Apoptoses, Extrinsic Pathway,Apoptoses, Intrinsic Pathway,Apoptosis, Caspase-Dependent,Apoptosis, Classic,Apoptosis, Classical,Caspase Dependent Apoptosis,Cell Death, Programmed,Classic Apoptoses,Extrinsic Pathway Apoptoses,Extrinsic Pathway Apoptosis,Intrinsic Pathway Apoptoses,Intrinsic Pathway Apoptosis
D047091 Eosinophil Granule Proteins Proteins found in EOSINOPHIL granules. They are primarily basic proteins that play a role in host defense and the proinflammatory actions of activated eosinophils. EG2 Antigen,Antigen, EG2,Granule Proteins, Eosinophil
D047208 Eosinophil-Derived Neurotoxin A 19-kDa cationic peptide found in EOSINOPHIL granules. Eosinophil-derived neurotoxin is a RIBONUCLEASE and may play a role as an endogenous antiviral agent. Eosinophil Protein X,RNS2 Neurotoxin,Serum Eosinophil Protein X,s-EPX,Eosinophil Derived Neurotoxin,Neurotoxin, Eosinophil-Derived,Neurotoxin, RNS2

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