Molecular Changes in the Cell Surface of Differentiating Epidermal Keratinocytes *

2015 ◽  
pp. 243-251 ◽  
Author(s):  
J. D. Zieske ◽  
I. A. Bernstein
Keyword(s):  
Cell Surface ◽  
Epidermal Keratinocytes ◽  
Molecular Changes

Molecular changes in cell surface membranes resulting from trypsinization of sarcoma 180 tumor cells

1976 ◽  
Vol 426 (4) ◽  
pp. 630-637 ◽  
Author(s):  
John W. Huggins ◽  
Robert W. Chestnut ◽  
Norman N. Durham ◽  
Kermit L. Carraway
Keyword(s):  
Cell Surface ◽  
Tumor Cells ◽  
Sarcoma 180 ◽  
Molecular Changes

scholarly journals Intermediate filaments and the initiation of desmosome assembly.

1985 ◽  
Vol 101 (2) ◽  
pp. 506-517 ◽  
Author(s):  
J C Jones ◽  
R D Goldman
Keyword(s):  
Cell Surface ◽  
Intermediate Filaments ◽  
Ultrastructural Localization ◽  
Free Cell ◽  
Cell Protein ◽  
Epidermal Keratinocytes ◽  
Cell Contact ◽  
Cell Surfaces ◽  
Primary Mouse ◽  
And Function

The desmosome junction is an important component in the cohesion of epithelial cells, especially epidermal keratinocytes. To gain insight into the structure and function of desmosomes, their morphogenesis has been studied in a primary mouse epidermal (PME) cell culture system. When these cells are grown in approximately 0.1 mM Ca2+, they contain no desmosomes. They are induced to form desmosomes when the Ca2+ level in the culture medium is raised to approximately 1.2 mM Ca2+. PME cells in medium containing low levels of Ca2+, and then processed for indirect immunofluorescence using antibodies directed against desmoplakins (desmosomal plaque proteins), display a pattern of discrete fluorescent spots concentrated mainly in the perinuclear region. Double label immunofluorescence using keratin and desmoplakin antibodies reveals that the desmoplakin-containing spots and the cytoplasmic network of tonofibrils (bundles of intermediate filaments [IFB]) are in the same juxtanuclear region. Within 1 h after the switch to higher levels of Ca2+, the spots move toward the cell surface, primarily to areas of cell-cell contact and not to free cell surfaces. This reorganization occurs at the same time that tonofibrils also move toward cell surfaces in contact with neighboring cells. Once the desmoplakin spots have reached the cell surface, they appear to aggregate to form desmosomes. These immunofluorescence observations have been confirmed by immunogold ultrastructural localization. Preliminary biochemical and immunological studies indicate that desmoplakin appears in whole cell protein extracts and in Triton high salt insoluble residues (i.e., cytoskeletal preparations consisting primarily of IFB) prepared from PME cells maintained in medium containing both low and normal Ca2+ levels. These findings show that certain desmosome components are preformed in the cytoplasm of PME cells. These components undergo a dramatic reorganization, which parallels the changes in IFB redistribution, upon induction of desmosome formation. The reorganization depends upon both the extracellular Ca2+ level and the establishment of cell-to-cell contacts. Furthermore, the data suggests that desmosomes do not act as organizing centers for the elaboration of IFB. Indeed, we postulate that the movement of IFB and preformed desmosomal components to the cell surface is an important initiating event in desmosome morphogenesis.

scholarly journals Regulation of cell surface beta 1 integrin levels during keratinocyte terminal differentiation.

1995 ◽  
Vol 128 (6) ◽  
pp. 1209-1219 ◽  
Author(s):  
N A Hotchin ◽  
A Gandarillas ◽  
F M Watt
Keyword(s):  
Cell Surface ◽  
Intracellular Transport ◽  
De Novo ◽  
Terminal Differentiation ◽  
Epidermal Keratinocytes ◽  
Human Epidermal Keratinocytes ◽  
Confocal Immunofluorescence Microscopy ◽  
Affinity Modulation ◽  
Confocal Immunofluorescence ◽  
Beta 1 Integrin

Integrins of the beta 1 family play a central role in controlling adhesion and terminal differentiation within the epidermis. When human epidermal keratinocytes undergo terminal differentiation, intracellular transport of newly synthesized integrins is inhibited, and mature receptors are lost from the cell surface. We have examined the mechanisms underlying these processes, using an experimental model in which keratinocytes are placed in suspension to induce terminal differentiation. The block in intracellular transport was keratinocyte- and integrin-specific since it was not observed when fibroblasts were placed in suspension and did not affect E-cadherin synthesis in suspended keratinocytes. Newly synthesized beta 1 integrins associated with an endoplasmic reticulum resident protein, calnexin; the association was prolonged when keratinocytes were placed in suspension, suggesting a role for calnexin in the inhibition of transport. After 24 h, the level of beta 1 integrin mRNA declines in suspended keratinocytes, reflecting inhibition of gene transcription, but in fibroblasts, the level remained constant. Transport of integrins could be blocked in both adherent keratinocytes and fibroblasts by inhibiting total protein synthesis, raising the possibility that transport is coupled to de novo integrin synthesis. The fate of receptors on the surface of keratinocytes was followed by confocal immunofluorescence microscopy, immunoelectron microscopy, and biochemical analysis: with the onset of terminal differentiation, endocytosed receptors were transported to the lysosomes. These experiments reveal novel mechanisms by which integrin levels can be controlled. Together with our earlier evidence for transcriptional regulation and affinity modulation of integrins, they highlight the complexity of the mechanisms which ensure that the onset of terminal differentiation is linked to detachment of keratinocytes from the underlying basement membrane.

Production of scatter factor by ndk, a strain of epithelial cells, and inhibition of scatter factor activity by suramin

1991 ◽  
Vol 98 (3) ◽  
pp. 385-394
Author(s):  
J.C. Adams ◽  
R.A. Furlong ◽  
F.M. Watt
Keyword(s):  
Cell Surface ◽  
Single Cells ◽  
Terminal Differentiation ◽  
Epidermal Keratinocytes ◽  
Factor Activity ◽  
Cell Type ◽  
Activity Assay ◽  
Scatter Factor ◽  
Human Epidermal Keratinocytes ◽  
3T3 Fibroblasts

ndk are a strain of human epidermal keratinocytes that do not undergo terminal differentiation and which grow as single cells rather than compact colonies. We show that ndk are motile and secrete an epithelial scatter factor that has the same biochemical and immunological properties as the scatter factor previously purified from ras-transformed 3T3 fibroblasts. We have found that suramin, a polyanionic detergent, will reverse the activity of scatter factor from either cell type in the standard MDCK activity assay. When added to ndk cultures, suramin causes the cells to grow in coherent patches. This morphological change is accompanied by alterations in the distribution of actin and integrins, but not by stratification or terminal differentiation. The effect is reversed upon removal of suramin. We propose that the motile phenotype of ndk is due, at least in part, to autocrine production of scatter factor and that suramin may be useful for further studies of scatter factor binding to the cell surface.

scholarly journals Cell Surface Expression of HLA-Cw6 by Human Epidermal Keratinocytes: Positive Regulation by Cytokines, Lack of Correlation to a Variant Upstream of HLA-C

2016 ◽  
Vol 136 (9) ◽  
pp. 1903-1906 ◽  
Author(s):  
Ellen H. van den Bogaard ◽  
Henk J. Tijssen ◽  
Diana Rodijk-Olthuis ◽  
Kjeld P. van Houwelingen ◽  
Marieke J. Coenen ◽  
...  
Keyword(s):  
Cell Surface ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Epidermal Keratinocytes ◽  
Positive Regulation ◽  
Human Epidermal Keratinocytes
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