In:
Journal of Histochemistry & Cytochemistry, SAGE Publications, Vol. 61, No. 3 ( 2013-03), p. 199-205
Abstract:
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).
Type of Medium:
Online Resource
ISSN:
0022-1554
,
1551-5044
DOI:
10.1369/0022155412474823
Language:
English
Publisher:
SAGE Publications
Publication Date:
2013
detail.hit.zdb_id:
1421306-0
SSG:
12
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