CD44 exhibits a cell type dependent interaction with triton X-100 insoluble, lipid rich, plasma membrane domains

1995 ◽  
Vol 108 (9) ◽  
pp. 3127-3135 ◽  
Author(s):  
S.J. Neame ◽  
C.R. Uff ◽  
H. Sheikh ◽  
S.C. Wheatley ◽  
C.M. Isacke
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membrane ◽  
Transmembrane Domain ◽  
Direct Interaction ◽  
Membrane Domains ◽  
Cell Type ◽  
Transmembrane Glycoprotein ◽  
Morphological Studies ◽  
Plasma Membrane Domains ◽  
Triton X

CD44 is an abundant, widely expressed transmembrane glycoprotein which can act as a receptor for the extracellular matrix glycosaminoglycan, hyaluronan. Biochemical and morphological studies have demonstrated that in fibroblasts a significant of the CD44 population is resistant to Triton X-100 extraction and that the detergent insoluble protein is co-localized with components of the cortical cytoskeleton. Surprisingly, this distribution is not abrogated upon deletion of the CD44 cytoplasmic tail indicating that mechanisms other than a direct interaction with the cytoskeleton can regulate CD44. In this manuscript, the mechanisms underlying this detergent-insoluble association are further investigated. There was no evidence that the Triton X-100 insolubility of CD44 resulted from homotypic aggregation, an association with hyaluronan or from a direct, or indirect, association with the cytoskeleton. Instead, evidence is presented that the detergent insolubility of fibroblast CD44 at 4 degrees C results from an association of the CD44 transmembrane domain with Triton X-100 resistant, lipid rich, plasma membrane domains. The proportion of the CD44 found in these Triton X-100 insoluble structures is dependent upon cell type and cannot be altered by changing cell motility or extracellular matrix associations. These studies provide evidence for a novel mechanism regulating this adhesion protein in the plasma membrane.

scholarly journals Rapid Nonvesicular Transport of Sterol between the Plasma Membrane Domains of Polarized Hepatic Cells

2002 ◽  
Vol 277 (33) ◽  
pp. 30325-30336
Author(s):  
Daniel Wüstner ◽  
Andreas Herrmann ◽  
Mingming Hao ◽  
Frederick R. Maxfield
Keyword(s):  
Plasma Membrane ◽  
Membrane Domains ◽  
Hepatic Cells ◽  
Plasma Membrane Domains

scholarly journals Synergistic Assembly of Linker for Activation of T Cells Signaling Protein Complexes in T Cell Plasma Membrane Domains

2003 ◽  
Vol 278 (22) ◽  
pp. 20389-20394 ◽  
Author(s):  
Lorian C. Hartgroves ◽  
Joseph Lin ◽  
Hanno Langen ◽  
Tobias Zech ◽  
Arthur Weiss ◽  
...  
Keyword(s):  
T Cells ◽  
Plasma Membrane ◽  
T Cell ◽  
Protein Complexes ◽  
Membrane Domains ◽  
Cell Plasma Membrane ◽  
Signaling Protein ◽  
Cell Plasma ◽  
Plasma Membrane Domains

Molecular events in the organization of renal tubular epithelium: from nephrogenesis to regeneration

1989 ◽  
Vol 257 (6) ◽  
pp. F913-F924 ◽  
Author(s):  
R. Bacallao ◽  
L. G. Fine
Keyword(s):  
Plasma Membrane ◽  
Spatial Organization ◽  
Cell Interaction ◽  
Acute Injury ◽  
External Signal ◽  
Renal Tubular Cell ◽  
Membrane Domains ◽  
Sequence Of Events ◽  
Plasma Membrane Domains ◽  
Renal Tubular

Information from studies of embryonic nephrons and established renal tubular cell lines in culture can be integrated to derive a picture of how the renal tubule develops and regenerates after acute injury. During development, the formation of a morphologically polarized epithelium from committed nephric mesenchymal cells requires an external signal for mitogenesis and differentiation. Polypeptide growth factors, in some cases mediated through oncogene expression, act in an autocrine or paracrine fashion to stimulate the production of extracellular matrix proteins that probably provide the earliest orientation signal for the cell. Interaction of these proteins with cell surface receptors leads to early organization of the cytoskeletal actin network, which is the major scaffolding for further differentiation and for definition of plasma membrane domains. The formation of cell-cell contacts via specialized adhesion molecules integrates the epithelium into a polarized monolayer and maintains its fence function, i.e., separation of plasma membrane domains. Microtubules probably participate in the delivery of vesicles to specific plasma membrane domains and in the spatial organization of intracellular organelles. Following acute renal injury, this sequence of events appears to be reversed, resulting in partial or complete loss of differentiated features. Regeneration seems to follow the same pattern of sequential differentiation steps as nephrogenesis. The integrity of the epithelium is restored by reestablishing only those stages of differentiation that have been lost. Where cell death occurs, mitogenesis in adjacent cells restores the continuity of the epithelium and the entire sequence of differentiation events is initiated in the newly generated cells.

scholarly journals An Apical-Type Trafficking Pathway Is Present in Cultured Oligodendrocytes but the Sphingolipid-enriched Myelin Membrane Is the Target of a Basolateral-Type Pathway

1998 ◽  
Vol 9 (3) ◽  
pp. 599-609 ◽  
Author(s):  
Hans de Vries ◽  
Cobi Schrage ◽  
Dick Hoekstra
Keyword(s):  
Plasma Membrane ◽  
Apical Membrane ◽  
Basolateral Membrane ◽  
Insoluble Fraction ◽  
Membrane Domains ◽  
Myelin Membrane ◽  
Influenza Virus Hemagglutinin ◽  
Polarized Cells ◽  
Vesicular Stomatitis ◽  
Triton X

Myelin sheets originate from distinct areas at the oligodendrocyte (OLG) plasma membrane and, as opposed to the latter, myelin membranes are relatively enriched in glycosphingolipids and cholesterol. The OLG plasma membrane can therefore be considered to consist of different membrane domains, as in polarized cells; the myelin sheet is reminiscent of an apical membrane domain and the OLG plasma membrane resembles the basolateral membrane. To reveal the potentially polarized membrane nature of OLG, the trafficking and sorting of two typical markers for apical and basolateral membranes, the viral proteins influenza virus–hemagglutinin (HA) and vesicular stomatitis virus–G protein (VSVG), respectively, were examined. We demonstrate that in OLG, HA and VSVG are differently sorted, which presumably occurs upon their trafficking through the Golgi. HA can be recovered in a Triton X-100-insoluble fraction, indicating an apical raft type of trafficking, whereas VSVG was only present in a Triton X-100-soluble fraction, consistent with its basolateral sorting. Hence, both an apical and a basolateral sorting mechanism appear to operate in OLG. Surprisingly, however, VSVG was found within the myelin sheets surrounding the cells, whereas HA was excluded from this domain. Therefore, despite its raft-like transport, HA does not reach a membrane that shows features typical of an apical membrane. This finding indicates either the uniqueness of the myelin membrane or the requirement of additional regulatory factors, absent in OLG, for apical delivery. These remarkable results emphasize that polarity and regulation of membrane transport in cultured OLG display features that are quite different from those in polarized cells.

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