Differential expression of CRABP II, psoriasin and cytokeratin 1 mRNA in human skin diseases

Algermissen, Bernd; Sitzmann, Jörg; LeMotte, Peter K.; Czarnetzki, Beate M.

doi:10.1007/bf02505229

Cited by 48 publications

(46 citation statements)

References 18 publications

(16 reference statements)

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“…The presented sweat protein pattern summarizes the dominant proteins in human eccrine sweat and thus provides useful information for further investigations concerning skin diseases such as atopic dermatitis or psoriasis in which some of the proteins are involved, e.g. psoriasin genes are markedly up-regulated in psoriatic versus normal skin, whereas the expression of the cytokeratin I gene is, in contrast, high in normal skin and decreased in psoriatic skin (34). Regarding apolipoprotein D it has been suggested as a new prognostic factor for cutaneous malignant melanoma (35).…”

Section: Discussionmentioning

confidence: 99%

Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L

Baechle

Flad

Cansier

et al. 2006

Journal of Biological Chemistry

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The protein pattern of healthy human eccrine sweat was investigated and 10 major proteins were detected from which apolipoprotein D, lipophilin B, and cathepsin D (CatD) were identified for the first time in human eccrine sweat. We focused our studies on the function of the aspartate protease CatD in sweat. In vitro digestion experiments using a specific fluorescent CatD substrate showed that CatD is enzymatically active in human sweat. To identify potential substrates of CatD in human eccrine sweat LL-37 and DCD-1L, two antimicrobial peptides present in sweat, were digested in vitro with purified CatD. LL-37 was not significantly digested by CatD, whereas DCD-1L was cleaved between Leu 44 and Asp 45 and between Leu 29 and Glu 30 almost completely. The DCD-1L-derived peptides generated in vitro by CatD were also found in vivo in human sweat as determined by surface-enhanced laser desorption/ionization (SELDI) mass spectrometry. Furthermore, besides the CatD-processed peptides we identified additionally DCD-1L-derived peptides that are generated upon cleavage with a 1,10-phenanthroline-sensitive carboxypeptidase and an endoprotease. Taken together, proteolytic processing generates 12 DCD-1L-derived peptides. To elucidate the functional significance of postsecretory processing the antimicrobial activity of three CatDprocessed DCD-1L peptides was tested. Whereas two of these peptides showed no activity against Gram-positive and Gram-negative bacteria, one DCD-1L-derived peptide showed an even higher activity against Escherichia coli than DCD-1L. Functional analysis indicated that proteolytic processing of DCD-1L by CatD in human sweat modulates the innate immune defense of human skin.

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Section: Discussionmentioning

confidence: 99%

Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L

Baechle

Flad

Cansier

et al. 2006

Journal of Biological Chemistry

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“…As already noted, these include inflammatory dermatoses (34) and the response to UV-B-related stress (24), resistance to anoikis, and response to wound healing, where altered signaling pathways have been relatively well defined (23,(35)(36)(37). In these circumstances, induction of Akt, NF-nB, and AP-1 are often critical components.…”

Section: S100a7-and S100a7mentioning

confidence: 99%

The S100A7-c-Jun Activation Domain Binding Protein 1 Pathway Enhances Prosurvival Pathways in Breast Cancer

et al. 2005

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S100A7 is among the most highly expressed genes in preinvasive breast cancer, is a marker of poor survival when expressed in invasive disease, and promotes breast tumor progression in experimental models. To explore the mechanism of action, we examined the role of S100A7 in cell survival and found that overexpression of S100A7 in MDA-MB-231 cell lines promotes survival under conditions of anchorageindependent growth. This effect is paralleled by increased activity of nuclear factor-KB (3-fold) and phospho-Akt (4-fold), which are known to mediate prosurvival pathways. S100A7 and phospho-Akt are also correlated in breast tumors examined by immunohistochemistry (n = 142; P < 0.0001; r = 0.34). To explore the underlying mechanism, we examined the role of a putative c-Jun activation domain-binding protein 1 (Jab1)-binding domain within S100A7 using a panel of MDA-MB-231 breast cell lines stably transfected with either S100A7 or S100A7 mutated at the Jab1 domain. Structural analysis by three-dimensional protein modeling, immunoprecipitation, and yeast two-hybrid assay and functional analysis using transfected reporter gene and Western blot assays revealed that the in vitro effects of S100A7 on phospho-Akt and the nuclear factor-KB pathway are dependent on the Jab1-binding site and the interaction with Jab1. Enhanced epidermal growth factor receptor signaling was also found to correlate with the increased phospho-Akt. Furthermore, the Jab1-binding domain is also necessary for the enhanced tumorigenicity conferred by S100A7 expression in murine xenograft tumors in vivo. We conclude that the S100A7-Jab1 pathway acts to enhance survival under conditions of cellular stress, such as anoikis, which may promote progression of breast cancer. (Cancer Res 2005; 65(13): 5696-702)

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“…Various studies have reported a significant increase in psoriasin, hBD-2 and LL-37 in both diseases [51,[68][69][70].…”

Section: Clinical Relevance Of Amps In Inflammatory Skin Disordersmentioning

confidence: 94%

“…Several studies acknowledged the theory [13,16]. Psoriasin, hBD-2 and hBD-3, LL-37, RNase 7 and calprotectin are induced in the psoriatic skin [50,51]. The up-regulation of AMPs expression in the skin of psoriasis patients is considered to contribute to a low rate of infections in psoriatic lesions.…”

Section: Clinical Relevance Of Amps In Inflammatory Skin Disordersmentioning

confidence: 99%

The role of antimicrobial peptides in chronic inflammatory skin diseases

Marcinkiewicz¹,

Majewski²

2016

pdia

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A b s t r a c tAntimicrobial peptides (AMPs) are effector molecules of the innate immune system of the skin. They present an activity against a broad spectrum of Gram-positive and Gram-negative bacteria as well as some fungi, parasites and enveloped viruses. Several inflammatory skin diseases including psoriasis, atopic dermatitis, acne vulgaris and rosacea are characterized by a dysregulated expression of AMPs. Antimicrobial peptides are excessively produced in lesional psoriatic scales or rosacea in contrast to the atopic skin that shows lower AMP levels when compared with psoriasis. The importance of the AMPs contribution to host immunity is indisputable as alterations in the antimicrobial peptide expression have been associated with various pathologic processes. This review discusses the biology and clinical relevance of antimicrobial peptides expressed in the skin and their role in the pathogenesis of inflammatory skin diseases.

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Differential expression of CRABP II, psoriasin and cytokeratin 1 mRNA in human skin diseases

Cited by 48 publications

References 18 publications

Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L

Cathepsin D Is Present in Human Eccrine Sweat and Involved in the Postsecretory Processing of the Antimicrobial Peptide DCD-1L

The S100A7-c-Jun Activation Domain Binding Protein 1 Pathway Enhances Prosurvival Pathways in Breast Cancer

The role of antimicrobial peptides in chronic inflammatory skin diseases

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