Immunohistochemical localization by monoclonal antibodies of S-100 α and β proteins in mixed tumours and adenomas of the skin

Noda, Yoko; Horike, H.; Tanimura, Takahumi; Tsujimura, Takahiro; Mori, Masahiko

doi:10.1007/bf02899236

Cited by 18 publications

(4 citation statements)

References 25 publications

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“…Therefore, we decided to screen for full length cDNA probes of human S100a and CAPL. A partial cDNA clone of SlOOa was obtained by screening fusion proteins of a human heart cDNA library (Stratagene) with a monoclonal antibody directed against bovine SlOOa (JIMRO, Japan) (Noda et al" 1988). This incomplete clone was used to rescreen the same library.…”

Section: Resultsmentioning

confidence: 99%

“…After 3.5 h preincubation at 42 °C, dishes were overlayed with the pretreated nitrocellulose filters and incubated for an additional 3.5 h at 37 °C. The removed filters were screened using a monoclonal antibody directed against bovine S100a (JIMRO, Japan) (Noda et al, 1988) and the Proto Blot kit (Promega). After blocking with 1% FCS (fetal calf serum) and 3% BSA (bovine serum albumin) in TBST (10 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM CaaCl, 0.05% Tween 20) for 15 min at 37 °C, the filters were incubated with monoclonal antibodies (1:100 dilution in TBST) for 1 h at room temperature.…”

Section: Consimentioning

confidence: 99%

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S100.alpha., CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart

Engelkamp¹,

Bw²,

Erné³

et al. 1992

Biochemistry

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Elevated levels of intracellular calcium are a major cause of myocardial dysfunction. To find possible mediators of the deregulated calcium we searched for EF-hand calcium-binding proteins of the S100 family. By PCR technology we identified three members of the S100 protein family (S100 alpha, CACY, and CAPL) in the human heart. We cloned the corresponding cDNAs and examined their expression levels in various human tissues by Northern blot analysis. All three proteins are expressed at high levels in the human heart. Whereas CACY and CAPL mRNAs are expressed ubiquitously, S100 alpha mRNA is restricted to heart, skeletal muscle, and brain. Interestingly, the expression pattern of S100 alpha, CACY, and CAPL in human tissues differs significantly from that in rodent tissues.

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Section: Resultsmentioning

confidence: 99%

Section: Consimentioning

confidence: 99%

S100.alpha., CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart

Engelkamp¹,

Bw²,

Erné³

et al. 1992

Biochemistry

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“…In most previous immunohistochemical studies on salivary pleomorphic adenomas [9,11], skin mixed tumours [4,10,12,13] and many other tumour types, commercially available antisera raised against an ill defined mixture of bovine brain S100 proteins were used for the classification of tumours. Recently we demonstrated that these antisera against bovine S100 proteins reacted mostly against S100A1 and A100B but not against the novel S100A2, S100A4, or S100A6 proteins.…”

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confidence: 99%

Localization of Ca 2+ -binding S100 proteins in epithelial tumours of the skin

et al. 1998

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The Ca(2+)-binding proteins S100A1, S100A2, S100A4, S100A6 and S100B were evaluated immunohistochemically in normal skin and skin appendage tumours. Epidermal basal cells, epithelial cells of sebaceous glands, hair follicle sheet epithelia and eccrine duct reacted strongly with an antiserum against human S100A2 but were nonreactive or weakly reactive to S100A1, S100A4, S100A6 and S100B. Varying types of skin appendage tumours and most peripheral cells in tumour nests of basal cell carcinoma and squamous cell carcinoma showed positive S100A2 immunoreactivity in neoplastic cells corresponding to basal cells but were nonreactive or faintly reactive for other S100 proteins. Langerhan's cells and melanocytes were labelled by S100B. Basophilic cells of calcifying epithelioma were occasionally stained with S100A2 antiserum. Eccrine poroma did not react with any S100 antiserum. Mixed tumours of the skin containing neoplastic myoepithelial cells stained strongly for S100A2 and S100B but only faintly for S100A1, S100A4, S100A6. This is the first report on selective evaluation of different S100 proteins in normal skin. These antibodies are valuable tools for better characterization of skin appendage tumours.

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“…Immunohistochemieal studies of intermediate-sized proteins in these different types of tumor cells have shown that keratin proteins arc present in the epithelial tubulo-ductal structures (1)(2)(3)(4)(5)(6)(7)(8), whereas vimentin is localized in the spindle-shaped and myoepithelium-derived cells (1,7,8). Modified myoepithelial cells in pleomorphie adenomas also display positive staining for S-100 protein and its subunits a and (3, as well as those in skin mixed tumors (9)(10)(11)(12)(13)(14). It has been pointed out that stromal tissue and modified myoepithelial cells contain elastins as one of their mesenchymal properties (15)(16)(17).…”

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Monoclonal antibody‐detected vimentin distribution in pleomorphic adenomas of salivary glands

Yamada

Shinohara

Takai

et al. 1988

J Oral Pathology Medicine

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To evaluate the participation of myoepithelial components in pleomorphic adenomas, an immunohistochemical study was carried out using monoclonal antibodies to vimentin. Of a total of 80 cases, 50 tumors gave positive staining, 5 tumors very slight, and 25 tumors negative staining for vimentin. Localization patterns for vimentin were divided into 3 classes: 1) vimentin staining in fibrous stromal tissue; 2) variable intensities of vimentin staining were found in the outer layers of tumor cells in tubuloductal structures (some of which were spindle cells connected to modified myoepithelial cells which also gave variable vimentin staining); and 3) modified myoepithelial cells and chondroidlike cells displayed strongly positive staining for vimentin. Typical histologic features of pleomorphic ademomas, i.e., tubulo‐ductal or duct‐like structures were characterized by positive vimentin staining in outer tumor cells and by a positive keratin reaction in the luminal tumor cells. In tumors devoid of stromal connective tissues and the near absence of well‐developed, or modified myoepithelial cells, vimentin staining was absent.

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Immunohistochemical localization by monoclonal antibodies of S-100 α and β proteins in mixed tumours and adenomas of the skin

Cited by 18 publications

References 25 publications

S100.alpha., CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart

S100.alpha., CAPL, and CACY: molecular cloning and expression analysis of three calcium-binding proteins from human heart

Localization of Ca 2+ -binding S100 proteins in epithelial tumours of the skin

Monoclonal antibody‐detected vimentin distribution in pleomorphic adenomas of salivary glands

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