p63 is a useful marker for cutaneous spindle cell squamous cell carcinoma

Dotto, Jorge; Glusac, Earl J.

doi:10.1111/j.0303-6987.2006.00477.x

Cited by 116 publications

(114 citation statements)

References 16 publications

(24 reference statements)

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“…An interaction of the two proteins with S100A2 could be part of a feedback loop mechanism. Further, this interaction may be relevant in the development of cancer, because S100A2 and p63 have been linked to squamous cell carcinomas Lauriola et al, 2000;Yamaguchi et al, 2000;Pelosi et al, 2002;Pruneri et al, 2002;Dotto and Glusac, 2006).…”

Section: Discussionmentioning

confidence: 99%

Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73

et al. 2010

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S100 proteins modulate p53 activity by interacting with its tetramerization (p53TET, residues 325-355) and transactivation (residues 1-57) domains. In this study, we characterized biophysically the binding of S100A1, S100A2, S100A4, S100A6 and S100B to homologous domains of p63 and p73 in vitro by fluorescence anisotropy, analytical ultracentrifugation and analytical gel filtration. We found that S100A1, S100A2, S100A4, S100A6 and S100B proteins bound different p63 and p73 tetramerization domain variants and naturally occurring isoforms with varying affinities in a calcium-dependent manner. Additional interactions were observed with peptides derived from the p63 and p73 N-terminal transactivation domains. Importantly, S100 proteins bound p63 and p73 with different affinities in their different oligomeric states, similarly to the differential modes of binding to p53. On the basis of our data, we hypothesize that S100 proteins regulate the oligomerization state of all three p53 family members and their isoforms, with a potential physiological relevance in developmental and disease-related processes. The regulation of the p53 family by S100 is complicated and depends on the target preference of each individual S100 protein, the concentration of the proteins and calcium, as well as the splicing variation of p63 or p73. Our results outlining the complexity of the interaction should be considered when studying the functional effects of S100 proteins in their biological context.

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Section: Discussionmentioning

confidence: 99%

Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73

et al. 2010

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“…In many studies of human cutaneous SCCs, p63 levels are high and now used as diagnostic markers (Dotto et al 2006). A large majorityof these studies have been performed using pan-p63 antibodies that bind in the DBD of the protein and do not distinguish between the TA and DN isoforms.…”

Section: P63 In Skin Cancermentioning

confidence: 99%

p53/p63/p73 in the Epidermis in Health and Disease

Botchkarev

Flores

2014

Cold Spring Harbor Perspectives in Medicine

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Although p53 has long been known as the "guardian of the genome" with a role in tumor suppression in many tissues, the discovery of two p53 ancestral genes, p63 and p73, more than a decade ago has triggered a considerable amount of research into the role of these genes in skin development and diseases. In this review, we primarily focus on mechanisms of action of p53 and p63, which are the best-studied p53 family members in the skin. The existence of multiple isoforms and their roles as transcriptional activators and repressors are key to their function in multiple biological processes including the control of skin morphogenesis, regeneration, tumorigenesis, and response to chemotherapy. Last, we provide directions for further research on this family of genes in skin biology and pathology.

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“…The present tumor is carcinoma. Atypical fibroxanthoma and desmoplastic melanoma was excluded because the present tumor expressed various CKs and did not express HMB45, Melan-A, SOX10, MITF; [3][4][5][6][7][8][9][10] the specificity of S100 protein is low, [3][4][5][6][7][8][9][10] the possibility of desmoplastic melanoma is quite unlikely. Because the present tumor expressed CKs, it is carcinoma.…”

Section: Discussionmentioning

confidence: 99%

“…[4][5][6][7][8][9][10] These two variants of skin SCC lack keratinization and intercellular bridge, thus causing diagnostic problems. [1][2][3][4][5][6][7][8][9][10] The author herein reports a case of desmoplastic SCC composed predominantly of spindle cells.…”

Section: Introductionmentioning

confidence: 99%

Desmoplastic spindle cell squamous cell carcinoma of skin

Terada

2016

CRCP

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Desmoplastic squamous cell carcinoma (SCC) and spindle cell SCC is very rare in skin. An 86-year-old woman presented a skin tumor of face. The tumor measured 1.8 cm × 1.6 cm × 0.6 cm. An excisional biopsy was performed. Histologically, malignant spindle cells with hyperchromatic nuclei and nucleoli were seen to proliferate together with marked solar elastosis and desmoplasia. Mitotic figures were scattered. Immunohistochemically, the malignant cells were positive for pancytokeratin AE1/3, pancytokeratin WSS, cytokeratin (CK) 5/6, CK34BE12, CK14, vimentin, S100 protein, α-smooth muscle actin, p53, p63, and Ki-67 (labeling = 70%). They were negative for EMA, pancytokeratin CAM5.2, CK7, CK8, CK18, CK19, CK20, desmin, HMB45, Melan-A, SOX10, MITF, myoglobin, CEA, CA19-9 and CD34. The lesion recurred two times and showed neck lymph node metastasis during the following 2 years. The patient died of other diseases 3 years after the first presentation.

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p63 is a useful marker for cutaneous spindle cell squamous cell carcinoma

Abstract: In the given differential diagnosis, p63 appears relatively specific to SCSCC and adds a useful nuclear marker to the available repertoire. The findings also suggest that cytokeratins MNF116 and CK34betaE12 may be more useful than standard cytokeratins in labeling SCSCC.

Cited by 116 publications

References 16 publications

Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73

Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73

p53/p63/p73 in the Epidermis in Health and Disease

Desmoplastic spindle cell squamous cell carcinoma of skin

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