Role of protein and calcium in stratum corneum cell cohesion

Bissett, Donald; McBride, James F.; Patrick, Larry F.

doi:10.1007/bf00413255

Cited by 37 publications

(15 citation statements)

References 25 publications

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“…However, detergent extraction studies have shown that not only CD, but also extracellular lipids regulate SC cohesion [117,119]. We have applied the term SC 'integrity' as a measure of resistance to the dissociation of adjacent corneocytes, quantified as the number of D-Squame ® tape strippings required to raise the transepidermal water loss to defined levels (e.g.…”

Section: Sc Integrity/cohesionmentioning

confidence: 99%

Stratum corneum pH: Formation and Function of the ‘Acid Mantle’

Fluhr¹,

Elias²

2002

Exog Dermatol

169

112

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Although the acidic surface pH of the skin has been known for over a century, the stratum corneum (SC) pH gradient has been discovered only recently. After removal of SC layers with sequential tape strips, in humans, surface pH starts at 4.5–5.3, increasing by about 2–3 units until it reaches 6.8 in the lower SC. Both exogenous [free fatty acids (FFA) from sebaceous lipid, microbial metabolites, lactic acid from eccrine glands] and endogenous epidermal (enzymatic; membrane antiporters/pumps) mechanisms have been hypothesized to contribute to SC acidification. Three endogenous mechanisms have been identified to date that not only could influence SC pH, but also regulate one or more key SC functions: (1) the histidine-to-urocanic-acid pathway; (2) the phospholipid-to-FFA pathway, and (3) the sodium proton antiporter (NHE1). Additional factors that influence human surface pH have been detected. Endogenous factors, unrelated to pathological features, such as racial differences, topographical variation, gender differences, developmental and age-related changes have been reported. In contrast to adults, human newborn SC displays a near-neutral surface pH, which declines rapidly over the first postnatal month. Furthermore, endogenous factors have been described, as in atopic dermatitis, seborrheic dermatitis, diabetes, renal insufficiency and ichthyosis associated with an increased pH. Exogenous factors, like the use of detergents and cleansing products as well as SC hydration, can modify the surface pH. The consequences of SC acidification for several key SC functions are becoming clear, including (1) the role of an acidic pH for SC permeability barrier homeostasis, (2) the pH dependence of extracellular lipid processing and (3) SC integrity/cohesion. Integrity is defined as a measure of resistance to dissociation of adjacent corneocytes by tape stripping (cohesion is a related index defined as the amount of protein removed per stripping). (4) Proteolytic processes leading to desquamation are pH dependent, and (5) an acidic pH provides important antimicrobial resistance.

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Section: Sc Integrity/cohesionmentioning

confidence: 99%

Stratum corneum pH: Formation and Function of the ‘Acid Mantle’

Fluhr¹,

Elias²

2002

Exog Dermatol

169

112

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“…In order to determine whether the 40-kilodalton glycoprotein molecule can persist whole in the degradative environment of the stratum corneum or whether it may be partially cleaved but yet recognized by the antibody, we have exposed desquamin to several pro téinases that are routinely used to generate peptide maps, at concentrations that are typically used for that purpose. Trypsin has been reported to promote squame disso ciation of isolated stratum corneum [7,9], When we reacted desquamin with trypsin ( fig. la-e), we found that it was resistant to proteolytic degradation.…”

Section: Resultsmentioning

confidence: 99%

Sensitivity of Desquamin to Proteolytic Degradation

Brysk

Bell²,

Rajaraman³

1991

Pathobiology

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The stratum corneum is both a desquamating and degradative tissue; cell contacts become weaker in the outer lamellae and a variety of proteolytic and glycolytic enzymes cleave many macromolecules into free amino acids and saccharides. We have reported on a 40-kilodalton glycoprotein from human stratum corneum; because of its unique lectin-like properties, we believe that it plays a major role in desquamation and have named it desquamin. If desquamin is to function as a lectin during desquamation, it must survive enzymatic degradation in the outer stratum corneum. Accordingly, we treated this glycoprotein with a number of proteinases and found that desquamin is resistant in vitro to most of the types of proteinases that have been reported in the stratum corneum as well as several others that have not been identified as present in the tissue. In the stratum corneum, the lipids of the intercorneal mortar shield the glycoproteins; hence, desquamin is even less likely to be susceptible to endogenous proteolysis in vivo than in vitro.

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“…In the early 90 th , emerging data suggested that the lipids, crucial for the barrier's impermeability, played only a limited part in tissue cohesion, whereas the integrity of the SC depended mostly on the corneocytes and associated intercellular junctions. In particular, the finding that protease activity was necessary for desquamation to take place [1,2], as well as the identification of corneodesmosin (CDSN) as the only protein specifically localized in the extracellular part of corneodesmosomes [3], the modified desmosomes in the SC, contributed to reconsider the place of proteins in the barrier function of the SC.…”

Section: Introductionmentioning

confidence: 99%

Corneodesmosin: Structure, Function and Involvement in Pathophysiology

Jonca¹,

Caubet²,

Guerrin³

et al. 2010

TODJ

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Corneodesmosin (CDSN) was identified in the early 90 th by raising monoclonal antibodies against human plantar stratum corneum. It is a protein specific to desmosomes that will undergo transformation into corneodesmosomes, i.e. in man, desmosomes of the epidermis, of the three epithelial layers of the inner root sheath of the hair follicles and of the hard palate epithelium. After its secretion by granular keratinocytes via the lamellar bodies, CDSN is incorporated into the desmoglea of the desmosomes shortly before their transformation into corneodesmosomes. CDSN displays adhesive properties, mostly attributable to its N-terminal glycine-rich domain, and is sequentially proteolyzed as corneocytes migrate towards the skin surface. The recent inactivation of Cdsn in mice induced a lethal epidermal barrier disruption and hair follicle degeneration related to desmosome dysfunction, confirming the essential role of the protein in epidermis and hair follicle integrity. CDSN is located on chromosome 6, in the major psoriasis susceptibility locus PSORS1. Intriguingly, the only monogenic disease identified so far associated with nonsense mutations in CDSN, leading to the formation of a truncated protein, is a rare autosomal dominant disease, hypotrichosis simplex of the scalp. In this review, we expose data from the discovery of the protein to the most recent findings related to the relationship between its structure and function. In particular, the important benefits of mouse models and human diseases for the comprehension of CDSN role in the epidermis and hair follicles are reported in details.

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Role of protein and calcium in stratum corneum cell cohesion

Cited by 37 publications

References 25 publications

Stratum corneum pH: Formation and Function of the ‘Acid Mantle’

Stratum corneum pH: Formation and Function of the ‘Acid Mantle’

Sensitivity of Desquamin to Proteolytic Degradation

Corneodesmosin: Structure, Function and Involvement in Pathophysiology

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