Inhibition of Calcium-Induced Terminal Differentiation of Epidermal Cells by Ouabain and A23187

2015 ◽  
pp. 109-125 ◽  
Author(s):  
Henry Hennings ◽  
Stuart H. Yuspa ◽  
Karen A. Holbrook
Keyword(s):  
Terminal Differentiation ◽  
Epidermal Cells

Factors influencing calcium-induced terminal differentiation in cultured mouse epidermal cells

1983 ◽  
Vol 116 (3) ◽  
pp. 265-281 ◽  
Author(s):  
Henry Hennings ◽  
Karen A. Holbrook ◽  
Stuart H. Yuspa
Keyword(s):  
Terminal Differentiation ◽  
Epidermal Cells ◽  
Factors Influencing

Properties of carcinogen altered mouse epidermal cells resistant to calcium-induced terminal differentiation

1983 ◽  
Vol 4 (11) ◽  
pp. 1367-1377 ◽  
Author(s):  
Molly Kulesz-Martin ◽  
Anne E. Kilkenny ◽  
Karen A. Holbrook ◽  
Vemund Digernes ◽  
Stuart H. Yuspa
Keyword(s):  
Terminal Differentiation ◽  
Epidermal Cells

A sensitive method to quantify the terminal differentiation of cultured epidermal cells

1986 ◽  
Vol 167 (1) ◽  
pp. 252-256 ◽  
Author(s):  
Ivan King ◽  
Sharon L. Mella ◽  
Alan C. Sartorelli
Keyword(s):  
Terminal Differentiation ◽  
Epidermal Cells ◽  
Sensitive Method

scholarly journals Expression of CRABP-I and -II in human epidermal cells. Alteration of relative protein amounts is linked to the state of differentiation

1992 ◽  
Vol 287 (2) ◽  
pp. 383-389 ◽  
Author(s):  
G Siegenthaler ◽  
I Tomatis ◽  
D Chatellard-Gruaz ◽  
S Jaconi ◽  
U Eriksson ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Oral Mucosa ◽  
Terminal Differentiation ◽  
Physiological Role ◽  
Human Keratinocytes ◽  
Epidermal Cells ◽  
Psoriatic Skin ◽  
Cultured Keratinocytes ◽  
Crabp I ◽  
Crabp Ii

The physiological role of cellular retinoic acid-binding proteins (CRABPs) may be to influence the intracellular level of free retinoic acid in the cell. In the present study two isoforms of CRABP, CRABP-I and CRABP-II were partially characterized in various human Malpighian epithelia and in human cultured keratinocytes expressing various patterns of differentiation. We have developed a new sensitive radiobinding assay using a PAGE/autoradioblotting technique which effectively separates CRABP-I and CRABP-II. This method allows the simultaneous quantification of these proteins. We show that CRABP-I and -II have similar M(r) values (15,000), but differ in their dissociation constant towards retinoic acid (Kd of 16.6 nM and 50 nM respectively), in pI (4.86 and 5.13) and in their relative mobilities (RF) on PAGE under nondenaturating conditions (RF values 0.65 and 0.44). In addition, we show that CRABP-II is the major isoform expressed in human keratinocytes, in vivo as in vitro. Furthermore, we demonstrate that CRABP-II is actually the CRABP previously studied in epidermal cells by a PAGE assay (Siegenthaler & Saurat (1987) Eur. J Biochem. 166, 209-214) and whose levels are dramatically increased by retinoic acid and its analogues in human epidermis. Keratinocytes, in the absence of full terminal differentiation, as well as hyperplasia, such as cultured human differentiating keratinocytes, psoriatic plaques, and non-keratinized oral mucosa, contained high levels of CRABP-II. CRABP-I was not detected in cultured keratinocytes, whereas normal skin (at full terminal differentiation) expressed CRABP-I and CRABP-II at a ratio of approx. 1:1.4. This value was approx. 1:17 in lesional psoriatic skin and 1:8 in oral mucosa. These observations suggest that CRABP-I and -II are regulated differently in human keratinocytes. The sharp increases in CRABP-II levels are associated with an alteration in the differentiation programme, as well as with cell response to retinoic acid overload, whereas CRABP-I might be a marker for terminal differentiation.

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