Protein Domain Histochemistry (PDH)
| Autor: | Anna-Katharina Kurze, Maximillian Bockhorn, Christoph Wagener, Naghmeh Mortezai, Annegret Debus, Gerrit Wolters-Eisfeld, Axel Niendorf, Peter Nollau, Birgit Klampe |
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| Rok vydání: | 2012 |
| Předmět: |
CLEC10A
Tissue Fixation Histology Glycosylation Protein domain Breast Neoplasms Plasma protein binding Biology law.invention 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Polysaccharides C-type lectin law Humans Lectins C-Type Breast Cloning Molecular 030304 developmental biology 0303 health sciences Paraffin Embedding Histocytochemistry Lectin Articles Recombinant Proteins Protein Structure Tertiary HEK293 Cells Biochemistry chemistry 030220 oncology & carcinogenesis biology.protein Recombinant DNA Immunohistochemistry Female Anatomy Protein Binding |
| Zdroj: | Journal of Histochemistry & Cytochemistry; Vol 61 |
| ISSN: | 1551-5044 0022-1554 |
| Popis: | Specialized protein domains bind to posttranslational modifications (PTMs) of proteins, such as phosphorylation or glycosylation. When such PTM-binding protein domains are used as analytical tools, the functional states of cells and tissues can be determined with high precision. Here, we describe the use of recombinant CLEC10A (CD301), a human glycoreceptor of the C-type lectin family, for the detection of ligands in sections from formalin-fixed, paraffin-embedded normal and cancerous mammary tissues. A construct, in which part of the carbohydrate recognition domain (CRD) was deleted, was used as a negative control. In comparison to normal mammary glands, a pronounced staining of tumor tissues was observed. Because the construct with the truncated CRD did not show any tissue staining, the binding of the wild-type glycoreceptor can be attributed to its carbohydrate recognition domain. To distinguish our novel approach from immunohistochemistry, we propose the designation “protein domain histochemistry” (PDH). |
| Databáze: | OpenAIRE |
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