[Lectin binding of psoriatic skin]

Area of Science:

• Dermatology and Glycobiology
• Investigating the molecular composition of the skin's outermost layer.

Context:

• Psoriasis is a chronic inflammatory skin condition.
• The skin's glycocalyx, composed of carbohydrates, plays a role in cell communication and differentiation.
• Alterations in glycocalyx may contribute to the pathogenesis of skin diseases.

Purpose:

• To characterize and compare epidermal lectin binding patterns in psoriatic versus non-psoriatic skin.
• To identify specific alterations in the glycocalyx composition of psoriatic keratinocytes.

Summary:

• This study utilized fluoroisothiocyanate-labeled lectins (Canavalia ensiformis - ConA, Phaseolus vulgaris - PHA, Lens culinaris - LCA, and Helix pomatia - HPA) to analyze skin samples.
• While ConA, PHA, and LCA binding patterns were similar in psoriatic and control skin, prominent HPA binding was observed in psoriatic skin at the dermo-epidermal junction and intercellularly in the upper epidermis.
• Seborrheic keratosis showed distinct HPA binding patterns, primarily perinuclear in the upper epidermis, differing from both psoriatic and control skin.

Impact:

• The findings suggest that altered keratinocyte maturation in psoriasis is associated with specific changes in glycocalyx composition, particularly involving HPA-binding carbohydrates.
• This research provides insights into the molecular differences between healthy and psoriatic skin, potentially opening avenues for novel diagnostic or therapeutic strategies.
• Understanding these glycocalyx alterations could contribute to a deeper comprehension of psoriasis pathogenesis.