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Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues.

Standard

Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues. / Nollau, Peter; Wolters-Eisfeld, Gerrit; Seyed Mortezai, Naghmeh; Kurze, Anna-Katharina; Klampe, Birgit; Debus, Annegret; Bockhorn, Maximilian; Niendorf, Axel; Wagener, Christoph.

In: J HISTOCHEM CYTOCHEM, Vol. 61, No. 3, 3, 03.2013, p. 199-205.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Nollau, P, Wolters-Eisfeld, G, Seyed Mortezai, N, Kurze, A-K, Klampe, B, Debus, A, Bockhorn, M, Niendorf, A & Wagener, C 2013, 'Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues.', J HISTOCHEM CYTOCHEM, vol. 61, no. 3, 3, pp. 199-205. https://doi.org/10.1369/0022155412474823

APA

Nollau, P., Wolters-Eisfeld, G., Seyed Mortezai, N., Kurze, A-K., Klampe, B., Debus, A., Bockhorn, M., Niendorf, A., & Wagener, C. (2013). Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues. J HISTOCHEM CYTOCHEM, 61(3), 199-205. [3]. https://doi.org/10.1369/0022155412474823

Vancouver

Nollau P, Wolters-Eisfeld G, Seyed Mortezai N, Kurze A-K, Klampe B, Debus A et al. Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues. J HISTOCHEM CYTOCHEM. 2013 Mar;61(3):199-205. 3. https://doi.org/10.1369/0022155412474823

Bibtex

@article{6ac6cb9457eb41298bf996a766af2cc9,
title = "Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues.",
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).",
keywords = "Humans, Female, Protein Structure, Tertiary, Protein Binding, Cloning, Molecular, HEK293 Cells, Breast/*pathology, Breast Neoplasms/diagnosis/*pathology, Histocytochemistry/*methods, Lectins, C-Type/*analysis/*metabolism, Paraffin Embedding/methods, Polysaccharides/metabolism, Recombinant Proteins/analysis/metabolism, Tissue Fixation/methods, Humans, Female, Protein Structure, Tertiary, Protein Binding, Cloning, Molecular, HEK293 Cells, Breast/*pathology, Breast Neoplasms/diagnosis/*pathology, Histocytochemistry/*methods, Lectins, C-Type/*analysis/*metabolism, Paraffin Embedding/methods, Polysaccharides/metabolism, Recombinant Proteins/analysis/metabolism, Tissue Fixation/methods",
author = "Peter Nollau and Gerrit Wolters-Eisfeld and {Seyed Mortezai}, Naghmeh and Anna-Katharina Kurze and Birgit Klampe and Annegret Debus and Maximilian Bockhorn and Axel Niendorf and Christoph Wagener",
year = "2013",
month = mar,
doi = "10.1369/0022155412474823",
language = "English",
volume = "61",
pages = "199--205",
journal = "J HISTOCHEM CYTOCHEM",
issn = "0022-1554",
publisher = "Histochemical Society Inc.",
number = "3",

}

RIS

TY - JOUR

T1 - Protein domain histochemistry (PDH): binding of the carbohydrate recognition domain (CRD) of recombinant human glycoreceptor CLEC10A (CD301) to formalin-fixed, paraffin-embedded breast cancer tissues.

AU - Nollau, Peter

AU - Wolters-Eisfeld, Gerrit

AU - Seyed Mortezai, Naghmeh

AU - Kurze, Anna-Katharina

AU - Klampe, Birgit

AU - Debus, Annegret

AU - Bockhorn, Maximilian

AU - Niendorf, Axel

AU - Wagener, Christoph

PY - 2013/3

Y1 - 2013/3

N2 - 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).

AB - 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).

KW - Humans

KW - Female

KW - Protein Structure, Tertiary

KW - Protein Binding

KW - Cloning, Molecular

KW - HEK293 Cells

KW - Breast/pathology

KW - Breast Neoplasms/diagnosis/pathology

KW - Histocytochemistry/methods

KW - Lectins, C-Type/analysis/metabolism

KW - Paraffin Embedding/methods

KW - Polysaccharides/metabolism

KW - Recombinant Proteins/analysis/metabolism

KW - Tissue Fixation/methods

KW - Humans

KW - Female

KW - Protein Structure, Tertiary

KW - Protein Binding

KW - Cloning, Molecular

KW - HEK293 Cells

KW - Breast/pathology

KW - Breast Neoplasms/diagnosis/pathology

KW - Histocytochemistry/methods

KW - Lectins, C-Type/analysis/metabolism

KW - Paraffin Embedding/methods

KW - Polysaccharides/metabolism

KW - Recombinant Proteins/analysis/metabolism

KW - Tissue Fixation/methods

U2 - 10.1369/0022155412474823

DO - 10.1369/0022155412474823

M3 - SCORING: Journal article

C2 - 23275449

VL - 61

SP - 199

EP - 205

JO - J HISTOCHEM CYTOCHEM

JF - J HISTOCHEM CYTOCHEM

SN - 0022-1554

IS - 3

M1 - 3

ER -