血清钙结合S100蛋白A8和A9的水平升高可以反映银屑病角质形成细胞的异常分化和疾病的活动性

作     者：Benoit S. Toksoy A. Ahlmann M. M. Goebeler 李晓莉 

作者机构：Department of Dermatology University of Wü rzburgWü rzburg Germany 

出 版 物：《世界核心医学期刊文摘（皮肤病学分册）》 (Digest of the World Core Medical JOurnals:Dermatology)

年 卷 期：2006年第2卷第9期

页      面：29-30页

学科分类：1002[医学-临床医学] 100206[医学-皮肤病与性病学] 10[医学] 

主　　题：银屑病患者 S100蛋白 疾病活动性 血清水平 表皮分化 表达异常 血清钙 角质形成细胞 

摘      要：Background: The expression of calcium-binding S100 molecules organized within the epidermal differentiation complex on chromosome 1q21 is disturbed in hyperproliferative skin diseases such as psoriasis. Objectives: We studied whether serum levels of S100 proteins A8 (S100A8) and A9 (S100A9) are elevated in psoriasis, correlated their amounts with disease activity and identified potential cellular sources. Methods: Serum obtained from psoriasis patients or from healthy individuals was studied for S100A8 and S100A9 levels by enzyme-linked immunosorbent assay. Data were correlated to disease activity as reflected by the Psoriasis Area and Severity Index (PASI). Cellular sources of S100A8 and S100A9 were identified by in situ hybridization and immunohistochemistry of lesional psoriatic and nonlesional, nonpsoriatic skin. Results: A significant increase of S100A8/S100A9 serum levels was found in patients with psoriasis compared with healthy controls. Grading the patients into two groups of severity, individuals with a PASI of 15 showed serum levels of 705 ± 120 ng mL- 1 (mean ± SEM, n = 18), those with a PASI of ≥ 15 showed levels of 1315 ± 150 ng mL- 1 (n = 32) while controls presentedwith 365± 50 ng mL- 1. Performing in situ hybridization of lesional psoriatic skin we detected a dramatic induction of both S100A8 and S100A9 mRNA and protein primarily in the suprabasal layers of the epidermis while expression was negligible in nonlesional,nonpsoriatic interfollicular epidermis. Conclusions: Our data demonstrate that hyperproliferation and abnormal differentiation of psoriatic skin is associated with a massive upregulation and secretion of S100A8 and S100A9, suggesting not only a prominent role of these molecules during intracellular calcium-dependent signalling but also implying distinct extracellular functions.