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spelling todo:paper_03604012_v82_n6_p822_Ortiz2023-10-03T15:26:34Z Apotransferrin and the cytoskeleton of oligodendroglial cells Ortiz, E.H. Pasquini, L.A. Soto, E.F. Pasquini, J.M. Apotransferrin Clathrin vesicles Cytoskeleton Oligodendroglial maturation STOP protein apotransferrin buffer clathrin colchicine cytochalasin dynein adenosine triphosphatase glycoprotein kinesin paclitaxel polypeptide stable tubule only polypeptide tubulin tyrosine unclassified drug animal cell animal tissue article cell culture cellular distribution controlled study cytoskeleton immunoreactivity myelin sheath nonhuman oligodendroglia priority journal rat Animals Animals, Newborn Apoproteins Blotting, Western Cells, Cultured Cerebral Cortex Cytochalasins Cytoskeleton Gene Expression Regulation Humans Immunohistochemistry Microscopy, Confocal Microtubule-Associated Proteins Oligodendroglia Rats Rats, Wistar Receptors, Transferrin Transferrin Tubulin Apotransferrin (aTf), has been shown to accelerate the differentiation of oligodendroglial cells (OLGcs) in primary cultures and to increase the expression of different components of the myelin cytoskeleton (CSK). We examined the incorporation and distribution of human aTf (aTfh) exogenously added to OLGcs cultures and its effects on the CSK of the OLGcs. When OLGcs treated with aTfh were extracted with a CSK-stabilizing buffer containing detergent, aTfh was found in the soluble fraction. In vitro experiments showed that purified tubulin was not altered by the addition of aTfh. In OLGc primary cultures treated with aTfh, this glycoprotein showed a punctate distribution pattern along the OLGc processes. Treatment of the cultures with colchicine, cytochalasin, or taxol induced a displacement of the immunoreactivity of aTfh toward the OLGc soma. Analysis of the effects of aTfh on the cell distribution of tyrosinated and detyrosinated tubulin and STOP (stable tubule only polypeptide), showed that aTfh added to OLGc cultures promoted changes suggesting a stabilizing effect on the microtubules (MT) at the tip of the processes. Kinesin and dynein were found to colocalize with the aTfh, indicating that these motors participate in the transport of the added glycoprotein. Moreover, after treatment with aTfh, clathrin immunoreactivity was displaced from the OLGc body toward the cell processes. These results indicate that although aTfh added to OLGcs does not interact directly with CSK components, it seems to be transported in clathrin coated vesicles from the cell body to the tips of the OLGc processes where it promotes their stabilization. This mechanism may be of importance in the increased formation of the myelin membrane induced by aTf. © 2005 Wiley-Liss, Inc. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03604012_v82_n6_p822_Ortiz
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Apotransferrin
Clathrin vesicles
Cytoskeleton
Oligodendroglial maturation
STOP protein
apotransferrin
buffer
clathrin
colchicine
cytochalasin
dynein adenosine triphosphatase
glycoprotein
kinesin
paclitaxel
polypeptide
stable tubule only polypeptide
tubulin
tyrosine
unclassified drug
animal cell
animal tissue
article
cell culture
cellular distribution
controlled study
cytoskeleton
immunoreactivity
myelin sheath
nonhuman
oligodendroglia
priority journal
rat
Animals
Animals, Newborn
Apoproteins
Blotting, Western
Cells, Cultured
Cerebral Cortex
Cytochalasins
Cytoskeleton
Gene Expression Regulation
Humans
Immunohistochemistry
Microscopy, Confocal
Microtubule-Associated Proteins
Oligodendroglia
Rats
Rats, Wistar
Receptors, Transferrin
Transferrin
Tubulin
spellingShingle Apotransferrin
Clathrin vesicles
Cytoskeleton
Oligodendroglial maturation
STOP protein
apotransferrin
buffer
clathrin
colchicine
cytochalasin
dynein adenosine triphosphatase
glycoprotein
kinesin
paclitaxel
polypeptide
stable tubule only polypeptide
tubulin
tyrosine
unclassified drug
animal cell
animal tissue
article
cell culture
cellular distribution
controlled study
cytoskeleton
immunoreactivity
myelin sheath
nonhuman
oligodendroglia
priority journal
rat
Animals
Animals, Newborn
Apoproteins
Blotting, Western
Cells, Cultured
Cerebral Cortex
Cytochalasins
Cytoskeleton
Gene Expression Regulation
Humans
Immunohistochemistry
Microscopy, Confocal
Microtubule-Associated Proteins
Oligodendroglia
Rats
Rats, Wistar
Receptors, Transferrin
Transferrin
Tubulin
Ortiz, E.H.
Pasquini, L.A.
Soto, E.F.
Pasquini, J.M.
Apotransferrin and the cytoskeleton of oligodendroglial cells
topic_facet Apotransferrin
Clathrin vesicles
Cytoskeleton
Oligodendroglial maturation
STOP protein
apotransferrin
buffer
clathrin
colchicine
cytochalasin
dynein adenosine triphosphatase
glycoprotein
kinesin
paclitaxel
polypeptide
stable tubule only polypeptide
tubulin
tyrosine
unclassified drug
animal cell
animal tissue
article
cell culture
cellular distribution
controlled study
cytoskeleton
immunoreactivity
myelin sheath
nonhuman
oligodendroglia
priority journal
rat
Animals
Animals, Newborn
Apoproteins
Blotting, Western
Cells, Cultured
Cerebral Cortex
Cytochalasins
Cytoskeleton
Gene Expression Regulation
Humans
Immunohistochemistry
Microscopy, Confocal
Microtubule-Associated Proteins
Oligodendroglia
Rats
Rats, Wistar
Receptors, Transferrin
Transferrin
Tubulin
description Apotransferrin (aTf), has been shown to accelerate the differentiation of oligodendroglial cells (OLGcs) in primary cultures and to increase the expression of different components of the myelin cytoskeleton (CSK). We examined the incorporation and distribution of human aTf (aTfh) exogenously added to OLGcs cultures and its effects on the CSK of the OLGcs. When OLGcs treated with aTfh were extracted with a CSK-stabilizing buffer containing detergent, aTfh was found in the soluble fraction. In vitro experiments showed that purified tubulin was not altered by the addition of aTfh. In OLGc primary cultures treated with aTfh, this glycoprotein showed a punctate distribution pattern along the OLGc processes. Treatment of the cultures with colchicine, cytochalasin, or taxol induced a displacement of the immunoreactivity of aTfh toward the OLGc soma. Analysis of the effects of aTfh on the cell distribution of tyrosinated and detyrosinated tubulin and STOP (stable tubule only polypeptide), showed that aTfh added to OLGc cultures promoted changes suggesting a stabilizing effect on the microtubules (MT) at the tip of the processes. Kinesin and dynein were found to colocalize with the aTfh, indicating that these motors participate in the transport of the added glycoprotein. Moreover, after treatment with aTfh, clathrin immunoreactivity was displaced from the OLGc body toward the cell processes. These results indicate that although aTfh added to OLGcs does not interact directly with CSK components, it seems to be transported in clathrin coated vesicles from the cell body to the tips of the OLGc processes where it promotes their stabilization. This mechanism may be of importance in the increased formation of the myelin membrane induced by aTf. © 2005 Wiley-Liss, Inc.
format JOUR
author Ortiz, E.H.
Pasquini, L.A.
Soto, E.F.
Pasquini, J.M.
author_facet Ortiz, E.H.
Pasquini, L.A.
Soto, E.F.
Pasquini, J.M.
author_sort Ortiz, E.H.
title Apotransferrin and the cytoskeleton of oligodendroglial cells
title_short Apotransferrin and the cytoskeleton of oligodendroglial cells
title_full Apotransferrin and the cytoskeleton of oligodendroglial cells
title_fullStr Apotransferrin and the cytoskeleton of oligodendroglial cells
title_full_unstemmed Apotransferrin and the cytoskeleton of oligodendroglial cells
title_sort apotransferrin and the cytoskeleton of oligodendroglial cells
url http://hdl.handle.net/20.500.12110/paper_03604012_v82_n6_p822_Ortiz
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