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1.
EJHaem ; 1(2): 394-395, 2020 Nov.
Article in English | MEDLINE | ID: mdl-35845002

ABSTRACT

A 13-year-old patient was admitted to our hospital with severe respiratory distress, fever, and signs of meningeal infection. A positive result of swine flu was obtained by RT-PCR. All bacterial cultures were negative. Due to a worsening progression, the patient required mechanical ventilation. Leucocytosis with neutrophilia was observed with an absence of immature granulocytes and thrombocytopenia. A blood film was therefore examined, observing 85% of botryoid neutrophils, hypersegmented, and radially distributed nuclear lobs, and a large number of apoptotic cells. There was an elevated nucleus-cytoplasm ratio and neutrophils presented as slightly degranulated. The detection of botryoid nuclei in the neutrophils is a very infrequent finding and are usually found in cases of severe burns, hyperthermia, abuse of cocaine and methamphetamine, and encephalitis. Current studies also suggest that some morphometric measurements (cell population data [CPD]) can be altered in the case of sepsis and serious infection. In this particular case, [NE-SSC] = 159.9, [NE-FSC] = 94.6, and [NE-SFL] = 65.5, which correspond to measures of cellular complexity, size, and fluorescence and were above normal threshold values (performed by Sysmex XN20). Current studies directly relate the increase of NE-SSC > 149 in patients presenting with sepsis. The CPD and abnormal neutrophil morphology improved as the patient recovered. Results normalized by day 30 postdischarge.

2.
Hum Immunol ; 74(9): 1219-24, 2013 Sep.
Article in English | MEDLINE | ID: mdl-23756164

ABSTRACT

Cytotoxic T lymphocyte antigen 4 (CTLA-4) plays a key inhibitory role during T lymphocyte activation. The CTLA4 gene is translated into two proteic isoforms: a full-length protein (flCTLA-4) and a soluble counterpart. We explored the expression of both isoforms on healthy subjects. Whereas in non-stimulated cells the flCTLA-4 isoform is predominant, after stimulation the expression of the soluble form rapidly increases, reaching its maximum 24h after and falling again to the basal levels 72 h after stimulation. In contrast, the flCTLA-4 mRNA levels increase is slower, reaching the maximum level 72 h after stimulation. The presence of the T allele in the promoter positions -1722 and -318 is associated with an increased transcriptional activity and this effect seems to be synergic. We conclude that the kinetics of CTLA-4 isoform expression are sequential, and that the promoter polymorphisms -1722(C/T) and -318(C/T) are involved in the control of the CTLA4 transcription.


Subject(s)
CTLA-4 Antigen/metabolism , Protein Isoforms/metabolism , T-Lymphocytes/immunology , CTLA-4 Antigen/immunology , Cells, Cultured , Cloning, Molecular , Enzyme-Linked Immunosorbent Assay , Gene Expression Regulation/genetics , Genotype , Humans , Lymphocyte Activation , Polymorphism, Genetic , Promoter Regions, Genetic/genetics , Protein Isoforms/immunology , Spain , Transgenes/genetics
3.
J Comp Neurol ; 442(1): 23-34, 2002 Jan 01.
Article in English | MEDLINE | ID: mdl-11754364

ABSTRACT

During a developmental study of the expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) -type glutamate receptor subunits in rat spinal cord, we observed the existence of cytoplasmic inclusion bodies with positive immunoreactivity to glutamate receptor subunit 1 (GluR1) but not to other glutamate receptor subunits. GluR1-positive bodies have a diameter of between 1 and 3 microm and can be seen widely distributed throughout spinal cord gray matter, with the exception of the ventral horn region. They transiently appear within a definite developmental time-period between embryonic day 19 and postnatal day 17 and are only associated with neuronal cells. Ultrastructural analysis revealed that these inclusions were located adjacent to the nucleus and consisted of amorphous material without any limiting membrane. Immunocytochemical analysis revealed that the inclusions displayed positive immunoreactivity to ubiquitin, HSP70, and 20S proteasome. All these data indicate that GluR1-containing inclusions display all the ultrastructural and immunocytochemical characteristics of the recently described structure, which have been given the name aggresomes. Further studies are needed to determine the biological significance of these normally occurring aggresome-like inclusions, because aggresomes are usually considered in a pathologic context.


Subject(s)
Aging/metabolism , Cytoplasm/metabolism , Inclusion Bodies/metabolism , Interneurons/metabolism , Protein Folding , Receptors, AMPA/metabolism , Spinal Cord/growth & development , Animals , Animals, Newborn , Calcium-Binding Proteins/metabolism , Calcium-Binding Proteins/ultrastructure , Cysteine Endopeptidases/metabolism , Cysteine Endopeptidases/ultrastructure , Cytoplasm/ultrastructure , Cytoskeletal Proteins/metabolism , Cytoskeletal Proteins/ultrastructure , Glutamic Acid/metabolism , HSP70 Heat-Shock Proteins/metabolism , HSP70 Heat-Shock Proteins/ultrastructure , Immunohistochemistry , Inclusion Bodies/ultrastructure , Interneurons/ultrastructure , Microscopy, Electron , Multienzyme Complexes/metabolism , Multienzyme Complexes/ultrastructure , Neurodegenerative Diseases/metabolism , Neurodegenerative Diseases/physiopathology , Organelles/metabolism , Organelles/ultrastructure , Proteasome Endopeptidase Complex , Rats , Rats, Sprague-Dawley , Spinal Cord/metabolism , Spinal Cord/ultrastructure , Synaptic Transmission/physiology , Ubiquitin/metabolism , Ubiquitin/ultrastructure
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