Calgranulin C is Overexpressed in Lesional Psoriasis

Mirmohammadsadegh, Alireza; Tschakarjan, Etiena; Ljoljic, Antonia; Bohner, Katja; Michel, G; Ruzicka, Thomas; Goos, M.; Hengge, Ulrich R.

doi:10.1046/j.1523-1747.2000.00005-2.x

Cited by 39 publications

(30 citation statements)

References 17 publications

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“…S100A12 and S100A15 S100A12 (calgranulin C, EN-RAGE) is a pro-inflammatory protein that interacts with the receptor for advanced glycation endproducts (RAGE). S100A12 is markedly overexpressed in various inflammatory diseases (Yang et al, 2001;Rouleau et al, 2003;Foell et al, 2003a, b) including psoriasis (Mirmohammadsadegh et al, 2000;Semprini et al, 2002). In involved psoriatic epidermis, S100A12 is expressed in the suprabasal epidermal layers (Mirmohammadsadegh et al, 2000;Semprini et al, 2002).…”

Section: S100a7 Interacts With Epidermal-fatty Acid Binding Proteinmentioning

confidence: 99%

S100 Proteins in the Epidermis

Eckert

Broome

Ruse

et al. 2004

Journal of Investigative Dermatology

398

407

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The S100 proteins comprise a family of 21 low molecular weight (9-13 kDa) proteins that are characterized by the presence of two calcium-binding EF-hand motifs. Fourteen S100 protein genes are located within the epidermal differentiation complex on human chromosome 1q21 and 13 S100 proteins (S100A2, S100A3, S100A4, S100A6, S100A7, S100A8, S100A9, S100A10, S100A11, S100A12, S100A15, S100B, and S100P) are expressed in normal and/or diseased epidermis. S100 proteins exist in cells as anti-parallel hetero- and homodimers and upon calcium binding interact with target proteins to regulate cell function. S100 proteins are of interest as mediators of calcium-associated signal transduction and undergo changes in subcellular distribution in response to extracellular stimuli. They also function as chemotactic agents and may play a role in the pathogenesis of epidermal disease, as selected S100 proteins are markedly overexpressed in psoriasis, wound healing, skin cancer, inflammation, cellular stress, and other epidermal states.

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Section: S100a7 Interacts With Epidermal-fatty Acid Binding Proteinmentioning

confidence: 99%

S100 Proteins in the Epidermis

Eckert

Broome

Ruse

et al. 2004

Journal of Investigative Dermatology

398

407

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“…After several washes with 1% BSA in PBS, a secondary anti-mouse-IgG (1:30) was added with the staining being completed according to the alkaline phosphatase/antialkaline phosphatase method. 36 …”

Section: Immunohistologymentioning

confidence: 99%

Uptake and trafficking of DNA in keratinocytes: evidence for DNA-binding proteins

et al. 2004

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The skin is an interesting organ for human gene therapy due to accessibility, immunologic potential and synthesis capabilities. In this study, we attempted to visualize and measure the uptake of naked FITC-labeled plasmid by FACS analysis detecting up to 15% internalization in a doseand time-dependent manner. Cycloheximide treatment inhibited the uptake by 490%, suggesting a protein-mediated uptake. The inhibition of different internalization pathways demonstrated that blocking macropinocytosis (by amiloride and N,N-dimethylamylorid) reduced DNA uptake by 485%, while the inhibition of clathrin-coated pits (by chlorpromazine) and caveolae (by nystatin/filipin III) did not limit the uptake. Colocalization studies using confocal laser microscopy revealed a time-dependent accumulation of plasmid DNA in endosomes and lysosomes. When a green fluorescent protein (GFP) expression vector was used, specific GFP-RNA became detectable by reverse transcriptase-PCR, whereas measurable amounts of protein could not be identified in FACS experiments. To detect the potential DNA receptors on the keratinocyte surface, membrane proteins were extracted and subjected to South-Western blotting using digoxigenin-labeled calf thymus and l-phage DNA. Two DNA-binding proteins, ezrin and moesin, known as plasma membrane-actin linkers, were identified by one-and two-dimensional-South-Western blots and matrix-assisted laser desorption and ionizationmass spectrometry. Ezrin and moesin are functionally associated with a number of transmembrane receptors such as the EGF, CD44 or ICAM-1 receptor. Taken together, naked plasmid DNA seems to enter human keratinocytes through different pathways, mainly by macropinocytosis. Two DNA-binding proteins were identified that seemed to be involved in binding/trafficking of internalized DNA.

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“…Normal skin epithelium was negative for S100A12 but psoriatic skin stained positive mainly in the upper layers of the inflammatory skin (Robinson and Hogg, 2000). Overexpression of S100A12 in lesional psoriasis was also reported (Mirmohammadsadegh et al, 2000(Mirmohammadsadegh et al, , 2001). Another S100 protein, psoriasin (S100A7), is selectively expressed in skin under inflammation conditions (Madsen et al, 1992).…”

Section: Expression Of S100a12 In Normal Andmentioning

confidence: 89%

Multiple structural states of S100A12: A key to its functional diversity

Moroz

Dodson

Wilson

et al. 2003

Microscopy Res & Technique

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S100A12 is a member of the S100 family of EF-hand calcium-binding proteins. Together with two other calgranulins, S100A8 and S100A9, it is mostly expressed in human granulocytes, although there is increasing evidence of expression in keratinocytes and psoriatic lesions. It is involved in host-parasite response, and linked to corneal autoimmune diseases connected with filarial parasite infestation. Interaction of S100A12 with a multiligand receptor for advanced glycation end products (RAGE) mediates inflammation. Human recombinant S100A12 was found to induce neuritogenesis of cultured hippocampal cells, similar to two other S100 proteins, S100B and S100A4. X-ray structure of S100A12 has been solved in two crystal forms: R3 and P2(1). In the R3 crystal form S100A12 is a dimer, and in the P2(1) crystal form the dimers are arranged as a hexamer. The hexameric form suggests its role in receptor oligomerisation. S100A12 binds copper at the predicted zinc/copper binding site, which is located close to the surface of the protein. We propose copper-mediated generation of reactive oxygen species by S100A12 as its function in host-parasite response.

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Calgranulin C is Overexpressed in Lesional Psoriasis

Cited by 39 publications

References 17 publications

S100 Proteins in the Epidermis

S100 Proteins in the Epidermis

Uptake and trafficking of DNA in keratinocytes: evidence for DNA-binding proteins

Multiple structural states of S100A12: A key to its functional diversity

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