2 resultados para Problèmes de localisation
em Repositório Institucional UNESP - Universidade Estadual Paulista "Julio de Mesquita Filho"
Resumo:
This work relates the occurrence and distribution of collenchyma in Panicum maximum Jacq. P. maximum leaves were collected at different phases of development and sampled from both the base of the sheath and from the sheath-leaf blade transition area. For the stems, the study was made by using hand-cut sections of the internodal base. In the leaves, analyses of serial sections showed, at the base and sheath-leaf blade transition area, a sudden change of tissue at vascular bundle. The vascular bundles are surrounded by sclerenchyma, both in the sheath and the leaf blade, as well as by fibrous threads that occur on the adaxial side of the central bundles. However, at the base of the sheath and at the sheath-leaf blade transition area, sclerenchyma was substituted for collenchyma. In the stem, the substitution of sclerenchyma associated with vascular bundles for collenchyma occurs at the base of the internode, in the pulvinus region. The analyses from transmission electron microscopy showed the presence of lamellated cell wall and active protoplast in collenchyma cells.
Resumo:
BACKGROUND: Human and rodent leukocytes express high levels of the glucocorticoid-inducible protein annexin 1 ( ANXA1) ( previously referred to as lipocortin 1). Neutrophils and monocytes have abundant ANXA1 levels.Aim: We have investigated, for the first time, ANXA1 ultrastructural expression in rat eosinophils and compared it with that of extravasated neutrophils. The effect of inflammation ( carrageenin peritonitis) was also monitored.Methods: Electron microscopy was used to define the sub-cellular localisation of ANXA1 in rat eosinophils and neutrophils extravasated in the mesenteric tissue. A pair of antibodies raised against the ANXA1 N-terminus (i.e. able to recognise intact ANXA1, termed LCPS1) or the whole protein ( termed LCS3) was used to perform the ultrastructural analysis.Results: the majority of ANXA1 was localised in the eosinophil cytosol (similar to 60%) and nucleus (30-40%), whereas a small percentage was found on the plasma membrane (< 10%). Within the cytosol, the protein was equally distributed in the matrix and in the granules, including those containing the typical crystalloid. The two anti-ANXA1 antibodies gave similar results, with the exception that LCPS1 gave a lower degree of immunoreactivity in the plasma membrane. Inflammation (i.e. carrageenin injection) produced a modest increase in eosinophil-associated ANXA1 reactivity ( significant only in the cytoplasm compartment). Extravasated neutrophils, used for comparative purposes, displayed a much higher degree of immunoreactivity for the protein.Conclusion: We describe for the first time ANXA1 distribution in rat eosinophil by ultrastructural analysis, and report a different protein mobilisation from extravasated neutrophils, at least in this acute model of peritonitis.