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Differential expression of calcyclin and its accessible ligands in various types of cutaneous tumors
U Brinck1, H J Gabius, F Y Zeng
1Department of Pathology, University of Göttingen, Germany.
Abstract:
Calcyclin is the product of a gene that is regulated in dependence of the cell cycle in fibroblasts in vitro. It has recently been proven to be a sialic acid-binding protein in vitro and in the case of mammalian tissues to bind specifically to annexin II, annexin VI, annexin XI, and glyceraldehyde-3-phosphate dehydrogenase in a Ca(2+)-dependent manner. Since calcyclin can be labelled without impairment of its binding activity, it can be employed as a histochemical tool to localize its accessible ligands. Concomitantly, immunohistochemical localization of calcyclin with a specific antibody is warranted. By using histochemical and immunohistochemical techniques, the expression of calcyclin and its accessible binding sites are demonstrated in serial sections of normal skin and benign, pre-cancerous and malignant tumors of the skin, namely in verruca vulgaris, papillary hidradenoma, syringoma, keratoacanthoma, Bowen's disease, squamous cell carcinoma, melanocytic naevi, primary and metastatic malignant melanoma and non-Hodgkin lymphoma (NHL) of the skin. Cytoplasmic and nuclear expression of calcyclin and its ligands is unexceptionally found in normal skin, epithelial tumors and benign melanocytic tumors. Presence of calcyclin and calcyclin-binding sites is detected in more than 80% of tumor cells in the epithelial lesions. In the group of melanomas and lymphomas heterogeneity is obvious. The application of annexin-specific antibodies raises evidence that members of this protein family co-localize with calcyclin in situ to some extent. These findings suggest that calcyclin and accessible calcyclin-binding molecules, like certain annexins, may be differentially regulated in melanomas and lymphomas in contrast to epithelial lesions with presently undefined biological implications.
Insights
Calcyclin, a cell cycle-regulated protein, binds to specific molecules in mammalian tissues. Its expression and binding sites are found in normal skin and various skin tumors, suggesting differential regulation in melanomas and lymphomas.
Area of Science:
- Cell Biology
- Dermatology
- Biochemistry
Background:
- Calcyclin is a cell cycle-regulated protein in fibroblasts.
- It functions as a sialic acid-binding protein and binds to specific mammalian proteins, including annexins, in a calcium-dependent manner.
- Calcyclin's binding activity is preserved when labeled, enabling its use as a histochemical tool.
Purpose of the Study:
- To investigate the expression and localization of calcyclin and its accessible binding sites in normal skin and various skin tumors.
- To determine if calcyclin and its ligands are differentially regulated in different types of skin lesions.
- To explore the co-localization of calcyclin with annexins in situ.
Main Methods:
- Histochemical and immunohistochemical techniques were employed.
- Serial sections of normal skin and various skin tumors (benign, pre-cancerous, malignant) were analyzed.
- Specific antibodies against annexins were used to assess co-localization.
Main Results:
- Calcyclin and its ligands were ubiquitously expressed in the cytoplasm and nucleus of normal skin, epithelial tumors, and benign melanocytic tumors.
- Calcyclin and binding sites were present in over 80% of tumor cells in epithelial lesions.
- Heterogeneous expression patterns were observed in melanomas and lymphomas.
- Annexin family members showed some degree of co-localization with calcyclin in situ.
Conclusions:
- Calcyclin and its binding molecules, such as annexins, are widely distributed in normal skin and epithelial tumors.
- Differential regulation of calcyclin and its binding partners may occur in melanomas and lymphomas compared to epithelial lesions.
- Further research is needed to understand the biological implications of these differential regulations.