Calcium-dependent complex assembly of the myeloic differentiation proteins MRP-8 and MRP-14

Teigelkamp, Stefan; Bhardwaj, Ranjit; Roth, Johannes; Meinardus‐Hager, Georg; Karas, Michael; Sorg, Clemens

doi:10.1016/s0021-9258(18)98862-9

Cited by 212 publications

(40 citation statements)

References 30 publications

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“…The loading control b-actin was used to confirm that similar amounts of protein were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). As reported previously (Teigelkamp et al, 1991;Goebeler et al, 1994;Rammes et al, 1997), the two S100-specific antibodies crossreact as well as exhibiting different affinities for their antigens. Therefore, the different staining intensities did not reflect different amounts of protein.…”

Section: Nadph Oxidase Activity In Epithelial Cells After S100a8/a9 Complementationsupporting

confidence: 72%

HaCaT Keratinocytes Overexpressing the S100 Proteins S100A8 and S100A9 Show Increased NADPH Oxidase and NF-κB Activities

Benedyk

Sopalla

Nacken

et al. 2007

Journal of Investigative Dermatology

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The calcium- and arachidonic acid (AA)-binding proteins S100A8 and S100A9 are involved in nicotinamide adenine dinucleotide phosphate (NADPH) oxidase activation in phagocytes. They are specifically expressed in myeloid cells, and are also found in epithelial cells in various (patho)physiological conditions. We have investigated the consequences of S100A8/A9 overexpression in epithelial cell lines on reactive oxygen species (ROS) generation and downstream signaling. Epithelial carcinoma HeLa cells, which exclusively express Nox2, showed dramatically increased activation of NADPH oxidase by phorbol 12-myristate 13-acetate after S100A8/A9 gene transfection. HaCaT keratinocytes overexpressing S100A8/A9 showed enhanced, transient ROS generation in response to the calcium ionophore A23187 compared to mock-transfected cells. Polymerase chain reaction analysis revealed mRNA transcripts for Nox1, Nox2, and Nox5 in HaCaT keratinocytes. Detailed transfection studies confirmed that NADPH oxidase activities in Nox1- and Nox5-transfected HeLa cells were enhanced after S100A8/A9 gene complementation. Furthermore, mutational analysis revealed that AA binding and Thr113 phosphorylation are important for S100A8/A9-enhanced activation of NADPH oxidase. Nuclear factor-kappaB (NF-kappaB) activation and interleukin-8 mRNA levels were increased in S100A8/A9-HaCaT keratinocytes, consistent with the view that NF-kappaB is a redox-sensitive transcription factor. Because they are expressed in epithelia under specific conditions, S100A8 and S100A9 might be involved in skin pathogenesis by modulating aspects of downstream signaling.

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Section: Nadph Oxidase Activity In Epithelial Cells After S100a8/a9 Complementationsupporting

confidence: 72%

HaCaT Keratinocytes Overexpressing the S100 Proteins S100A8 and S100A9 Show Increased NADPH Oxidase and NF-κB Activities

Benedyk

Sopalla

Nacken

et al. 2007

Journal of Investigative Dermatology

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“…S100A8 and S100A9 are expressed at minimal levels in normal epidermis, although occasional expression is observed in the granular layer. Co-expression is expected, because these S100 proteins function as a heterodimer (Teigelkamp et al 1991). Both proteins are highly overexpressed in psoriasis.…”

Section: Discussionmentioning

confidence: 99%

S100 Protein Subcellular Localization During Epidermal Differentiation and Psoriasis

Broome

Ryan

Eckert

2003

J Histochem Cytochem.

224

183

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S U M M A R Y S100 proteins are calcium-activated signaling proteins that interact with target proteins to modulate biological processes. Our present studies compare the level of expression, and cellular localization of S100A7, S100A8, S100A9, S100A10, and S100A11 in normal and psoriatic epidermis. S100A7 and S100A11 are present in the basal and spinous layers in normal epidermis. These proteins appear in the nucleus and cytoplasm in basal cells but are associated with the plasma membrane in spinous cells. S100A10 is present in basal and spinous cells, in the cytoplasm, and is associated with the plasma membrane. S100A8 and S100A9 are absent or are expressed at minimal levels in normal epidermis. In involved psoriatic tissue, S100A10 and S100A11 levels remain unchanged, whereas, S100A7, S100A8, and S100A9 are markedly overexpressed. The pattern of expression and subcellular localization of S100A7 is similar in normal and psoriatic tissue. S100A8 and S100A9 are strongly expressed in the basal and spinous layers in psoriasis-involved tissue. In addition, we demonstrate that S100A7, S100A10, and S100A11 are incorporated into detergent and reducing agent-resistant multimers, suggesting that they are in vivo transglutaminase substrates. S100A8 and S100A9 did not form these larger complexes. These results indicate that S100 proteins localize to the plasma membrane in differentiated keratinocytes, suggesting a role in regulating calcium-dependent, membrane-associated events. These studies also indicate, as reported previously, that S100A7, S100A8, and S100A9 expression is markedly altered in psoriasis, suggesting a role for these proteins in disease pathogenesis.

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“…S100A8 is primarily expressed in oocytes within cysts/plasmodia where it induces oocytes or ovarian somatic cells to form primordial follicles ( Teng et al, 2015 ). S100A9 forms a heterodimer with S100A8 under calcium ( Teigelkamp et al, 1991 ) and the resultant complex contributes to inflammatory processes ( Hessian et al, 1993 ). mRNA expression of S100A9 is upregulated in both granulosa cells and residual ovarian cells 6 h after hCG injection and then sharply declines by 12 h post-hCG injection.…”

Section: Discussionmentioning

confidence: 99%

Ovarian transcriptome profile from pre-laying period to broody period of Xupu goose

Qin

Wang

et al. 2021

Poultry Science

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Xupu goose, a breed from Hunan province, produces high quality and quantity of meat and liver. However, its egg production rate is low, with poor reproductive traits but strong broody performance. These characteristics decrease the economic value of Xupu goose significantly. Here, RNA-seq was used to analyze the transcriptome changes of ovaries of Xupu goose at different stages to explore the molecular mechanism of reproduction from the pre-laying period to the broody period. A total of 258 genes were differentially expressed in the 3 stages. These genes are associated with inflammation, reproduction, mutual recognition and adhesion between cells, and cytoskeleton formation, and so on. In particular, we report, for the first time, the expression patterns of MRP126, serglycin, TXNIP, and FZD2 during the pre-laying, egg-laying, and broody periods of goose ovaries. Functional analysis by GO annotation revealed that GO terms were mainly involved in actin, cell signal transduction and regulation, and cellular components. Three pathways, including focal adhesion (gga04510), ECM-receptor interaction (gga04512), and N-Glycan biosynthesis (gga00510), were significantly enriched in the three groups. These findings provide a basis for further exploration of profiles of goose ovaries to improve egg production of Xupu goose.

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Calcium-dependent complex assembly of the myeloic differentiation proteins MRP-8 and MRP-14

Cited by 212 publications

References 30 publications

HaCaT Keratinocytes Overexpressing the S100 Proteins S100A8 and S100A9 Show Increased NADPH Oxidase and NF-κB Activities

HaCaT Keratinocytes Overexpressing the S100 Proteins S100A8 and S100A9 Show Increased NADPH Oxidase and NF-κB Activities

S100 Protein Subcellular Localization During Epidermal Differentiation and Psoriasis

Ovarian transcriptome profile from pre-laying period to broody period of Xupu goose

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