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1.
Biol. Res ; 40(2): 231-249, 2007. ilus
Article in English | LILACS | ID: lil-468194

ABSTRACT

Peroxisomes are thought to be formed by division of pre-existing peroxisomes after the import of newly synthesized proteins. However, it has been recently suggested that the endoplasmic reticulum (ER) provides an alternative de novo mechanism for peroxisome biogenesis in some cells. To test a possible role of the ER-Golgi transit in peroxisome biogenesis in mammalian cells, we evaluated the biogenesis of three peroxisomal membrane proteins (PMPs): ALDRP (adrenoleukodystrophy related protein), PMP70 and Pex3p in CHO cells. We constructed chimeric genes encoding these PMPs and green fluorescent protein (GFP), and transiently transfected them to wild type and mutant CHO cells, in which normal peroxisomes were replaced by peroxisomal membrane ghosts. The expressed proteins were targeted to peroxisomes and peroxisomal ghosts correctly in the presence or absence of Brefeldin A (BFA), a drug known to block the ER-Golgi transit. Furthermore, low temperature did not disturb the targeting of Pex3p-GFP to peroxisomes. We also constructed two chimeric proteins of PMPs containing an ER retention signal "DEKKMP": GFP-ALDRP-DEKKMP and myc- Pex3p-DEKKMP. These proteins were mostly targeted to peroxisomes. No colocalization with an ER maker was found. These results suggest that the classical ER-Golgi pathway does not play a major role in the biogenesis of mammalian PMPs.


Subject(s)
Animals , Cricetinae , Endoplasmic Reticulum/physiology , Golgi Apparatus/physiology , Mutation , Membrane Proteins/metabolism , Peroxisomes/metabolism , CHO Cells , Cricetulus , Endoplasmic Reticulum/metabolism , Membrane Proteins/genetics
2.
J Environ Biol ; 2005 Apr; 26(2): 265-8
Article in English | IMSEAR | ID: sea-113282

ABSTRACT

Impact of temperature related seasonal changes in density of Golgi complex were studied in brain, heart and intestine of the freshwater catfish, Clarias batrachus (Linnaeus). The density of Golgi complex was more in these organs of the fish acclimatized to a lower temperature (20 degrees C) than that to a higher temperature (29 degrees C). This suggests that lower temperature induces secretory activity in cells to cope up with the changes in surrounding environment. It could be a kind of histophysiological adaptation in poikilothermic animal.


Subject(s)
Acclimatization , Animals , Brain/anatomy & histology , Catfishes/anatomy & histology , Golgi Apparatus/physiology , Heart/anatomy & histology , Intestines/anatomy & histology , Seasons , Temperature
3.
Biocell ; 27(3): 329-346, Dec. 2003.
Article in English | LILACS | ID: lil-384237

ABSTRACT

The fine structure of the binucleate, parasitic protist Giardia lamblia during interphase and divisional stages was studied by serial thin sectioning and three-dimensional reconstructions. The earlier sign of nuclear division is the development of a few peripheral areas of densely packed chromatin directly attached to the inner nuclear envelope. An intracytoplasmic sheet of ventral disk components grows from the cell periphery towards one of the nuclei, apparently constricting this nucleus, which becomes located at a ventral bulge. After the basal bodies become duplicated, a full nuclear division occurs in trophozoites, giving two pairs of parent-daughter nuclei. This full division occurs in a dorsal-ventral direction, with the resulting nuclear pairs located at the sides of the two sets of basal bodies. A new ventral disk is formed from the disk-derived sheets in the cell harboring the four nuclei. Cytokinesis is polymorphic, but at early stages is dorsal-to-dorsal. Encysting trophozoites show the development of Golgi cisternae stacks and dense, specific secretory granules. 3-D reconstructions show that cysts contain a single pair of incompletely strangled nuclei. The dividing Giardia lacks a typical, microtubular spindle either inside or outside the nuclei. The nuclear envelope seems to be the only structure involved in the final division of the parent-daughter nuclei.


Subject(s)
Giardia lamblia/ultrastructure , Nuclear Envelope , Cell Nucleus/ultrastructure , Golgi Apparatus/physiology , Golgi Apparatus/ultrastructure , Cytoplasm/physiology , Cytoplasm/ultrastructure , Chromatin/physiology , Chromatin/ultrastructure , Cell Division/physiology , Giardia lamblia/physiology , Microscopy, Electron , Nuclear Envelope , Cell Nucleus/physiology , Organelles/physiology , Organelles/ultrastructure , Secretory Vesicles/physiology , Secretory Vesicles/ultrastructure
4.
Biocell ; 27(2): 181-187, Aug. 2003.
Article in English | LILACS | ID: lil-384245

ABSTRACT

The present study analyzed several characters of the red seaweed Gymnogongrus torulosus, such as cellular structure of the thallus, cuticle, pit plug and cell wall ultrastructure, and morphology of some organelles like plastids, Golgi bodies and mitochondria. Also, anomalous chloroplasts with thylakoid disorganization were found in medullary cells. The significance of this thylakoid disposition is still unclear. This is one of the first studies focused on the fine structure of a red alga recorded in Argentina.


Subject(s)
Seaweed/ultrastructure , Rhodophyta/ultrastructure , Organelles/ultrastructure , Seaweed/physiology , Rhodophyta/physiology , Golgi Apparatus/physiology , Golgi Apparatus/ultrastructure , Chloroplasts/physiology , Chloroplasts/ultrastructure , Microscopy, Electron , Mitochondria/physiology , Mitochondria/ultrastructure , Organelles/physiology , Cell Wall/physiology , Cell Wall/ultrastructure , Plastids/physiology , Plastids/ultrastructure , Thylakoids/physiology , Thylakoids/ultrastructure
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