scholarly journals Binding of aberrant glycoproteins recognizable by Helix pomatia agglutinin in adrenal cancers

BJS Open ◽  
2018 ◽  
Vol 2 (5) ◽  
pp. 353-359 ◽  
Author(s):  
R. Parameswaran ◽  
W. B. Tan ◽  
M. E. Nga ◽  
G. S. T. Soon ◽  
K. Y. Ngiam ◽  
...  
Keyword(s):  
Helix Pomatia ◽  
Helix Pomatia Agglutinin

Crystallization of Helix pomatia agglutinin (HPA), a protein from the edible snail

1999 ◽  
Vol 55 (11) ◽  
pp. 1903-1905 ◽  
Author(s):  
John N. Lisgarten ◽  
James E. Pitts ◽  
Rex A. Palmer ◽  
Colin D. Reynolds ◽  
Minh Hoa Dao-Thi ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Diffraction Pattern ◽  
Helix Pomatia ◽  
Unit Cell ◽  
Hanging Drop ◽  
Helix Pomatia Agglutinin ◽  
Cell Dimensions ◽  
Protein Molecules ◽  
Unit Cell Dimensions ◽  
Drop Technique

Crystals of Helix pomatia agglutinin (HPA) have been grown by the hanging-drop technique using polyethylene glycol as the precipitant at 293 K. Over a period of one to two weeks the crystals grew to maximum dimensions of 0.10 × 0.05 × 0.02 mm. The crystals belong to space group P6322, with unit-cell dimensions a = b = 63.3, c = 105.2 Å and Z = 12 identical monomers of Mr = 13 kDa, aggregating into two 78 kDa hexameric protein molecules per unit cell, each with symmetry 32 (D 3). The diffraction pattern extends to 3.6 Å at 293 K.

scholarly journals Lectin-binding properties of human breast cancer cell lines and human milk with particular reference to Helix pomatia agglutinin.

1995 ◽  
Vol 43 (3) ◽  
pp. 275-281 ◽  
Author(s):  
U Schumacher ◽  
E Adam ◽  
S A Brooks ◽  
A J Leathem
Keyword(s):  
Breast Cancer ◽  
Cell Lines ◽  
Binding Sites ◽  
Lectin Binding ◽  
Helix Pomatia ◽  
Breast Cancer Cell Lines ◽  
Human Breast ◽  
Membrane Glycoproteins ◽  
Tissue Sections ◽  
Helix Pomatia Agglutinin

Several studies have shown binding of a variety of lectins to breast cancer cells in tissue sections. In particular, binding of the lectin from the Roman snail, Helix pomatia agglutinin (HPA), to breast cancer cells is linked with a poor prognosis. The molecular basis for lectin binding to metastatic breast cancers is not known. To elucidate this in a model system, lectin-binding patterns of seven human breast cancer cell lines were investigated, their cell membranes were isolated, and HPA binding was assessed. In addition, the influence of fixation and processing on lectin-binding sites was also investigated. Binding of lectins to the tumor cells was very heterogeneous between and within the different cell lines and was influenced by fixation and processing. However, some cell lines showed HPA-binding sites both in vivo and in tissue sections. Analysis of the isolated cell membrane glycoproteins from these cell lines on Western blots revealed that HPA can bind to several membrane glycoproteins. In contrast, human milk shows only one major milk glycoprotein that is HPA-positive. Therefore, a switch in glycosylation appears to be taking place during the transformation to a metastatic phenotype.

Prognostic value of the histochemical expression of Helix pomatia agglutinin in advanced colorectal cancer

1994 ◽  
Vol 37 (2) ◽  
pp. 181-184 ◽  
Author(s):  
Yoichi Ikeda ◽  
Masaki Mori ◽  
Yosuke Adachi ◽  
Tetsuya Matsushima ◽  
Keizo Sugimachi
Keyword(s):  
Colorectal Cancer ◽  
Prognostic Value ◽  
Advanced Colorectal Cancer ◽  
Helix Pomatia ◽  
Helix Pomatia Agglutinin

Proteome analysis of metastatic colorectal cancer cells recognized by the lectin Helix pomatia agglutinin (HPA)

PROTEOMICS ◽  
2007 ◽  
Vol 7 (22) ◽  
pp. 4082-4089 ◽  
Author(s):  
Julien Saint-Guirons ◽  
Elton Zeqiraj ◽  
Udo Schumacher ◽  
Pamela Greenwell ◽  
Miriam Dwek
Keyword(s):  
Colorectal Cancer ◽  
Metastatic Colorectal Cancer ◽  
Cancer Cells ◽  
Helix Pomatia ◽  
Proteome Analysis ◽  
Helix Pomatia Agglutinin ◽  
Colorectal Cancer Cells

scholarly journals Lectinhistochemical staining of granuloma induced by bacillus Calmette-Guerin in Piaractus mesopotamicus

2013 ◽  
pp. 3753-3758
Author(s):  
Wilson G. Manrique ◽  
Gustavo S. Claudiano ◽  
Mayra AP. Figueiredo ◽  
Thalita R. Petrillo ◽  
Paulo F. Marcusso ◽  
...  
Keyword(s):  
Wheat Germ ◽  
Close Contact ◽  
Lectin Binding ◽  
Helix Pomatia ◽  
Control Group ◽  
Bacillus Calmette Guerin ◽  
Epithelioid Cells ◽  
Dolichos Biflorus ◽  
Piaractus Mesopotamicus ◽  
Helix Pomatia Agglutinin

ABSTRACTObjetive. This study was conducted to evaluate, by means of lectinhistochemistry (LHC), the expression of carbohydrates in granulomas induced by the bacillus Calmette-Guerin (BCG) in muscle tissue of Piaractus mesopotamicus after 33 days. Material and methods. Histological sections with 3 μm thick were incubated with the following lectins :WGA (Wheat germ agglutinin), DBA (Dolichos biflorus agglutinin) and HPA (Helix pomatia agglutinin), and the results were evaluated by light microscopy. Results. Acid fast bacilli were stained by Ziehl Neelsen (ZN) and strong labeled by WGA in the cytoplasm of macrophages. Labeling with DBA was intense in fibroblasts and weak in macrophages. On the other hand, HPA binding was stronger in macrophages, especially in those that were in close contact with epithelioid cells, without evidence of binding to fibroblasts. The epithelioid cells were not labeled by the used lectins, but they were identified by Hematoxilin-Eosin (HE). The lectins labeled specific type saccharides in glycoproteins, as N-acetylglucosamine present in bacilli and macrophages, as well as N-acetyl-galactosamine in macrophages. The control group showed no inflammation or lectin binding. Conclusions. This technique may be useful in identifying receptors for WGA, DBA and the HPA lectins in epithelioid granuloma induced by BCG in P. mesopotamicus

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