Lectin Binding Pattern of Gastric Mucosa of Pacific White-Sided Dolphin, Lagenorhynchus obliquidens

Using affinity chromatography on HPA-, PNA-, Con A, and WGA-agarose columns only a part (10-30%) of the high molecular weight mucous glycoproteins could be isolated from the Triton X-100 solubilized components of normal as well as carcinomatous gastric mucosa. The main part of the mucus was not bound by the lectins, which corresponds to our earlier lectin histochemical observations on paraffin-embedded tissue sections. The lectin-bound mucous glycoproteins had a relatively lower molecular weight, ranging from about 250-1,000 kilodaltons, as indicated by polyacrylamide gradient gel electrophoresis and by gel filtration on Biogel A 1.5 m column. In gas chromatographic analysis the molar ratio of aminohexoses to galactose was found to be much higher (3:1) in the lectin-bound mucous substances than in the whole high molecular weight mucus (1:1). This finding indicates that lectins have a higher affinity to the hexosamine rich components of mucus, which may be special forms of mucous glycoprotein molecules or the incompletely glycosylated core and backbone regions of the oligosaccharide chains of mucus. Extremely high hexosamine values (10:1) were found in the PNA isolated mucus of gastric adenocarcinoma. Since it is known that PNA binds to the terminal disaccharide, beta-galactose-(1-3)-N-acetylgalactosamine, which is localized at the reducing end of the oligosaccharide chains of mucus, it is highly probable that the elongation of the oligosaccharide side chains is disturbed in gastric cancer cells.

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Changes in lectin-binding pattern in the digestive tract ofXenopus laevis during metamorphosis. I. Gastric region

Journal of Morphology ◽

10.1002/jmor.1052050102 ◽

1990 ◽

Vol 205 (1) ◽

pp. 1-8 ◽

Cited By ~ 5

Author(s):

Atsuko Ishizuya-Oka ◽

Atsumi Shimozawa

Keyword(s):

Digestive Tract ◽

Lectin Binding ◽

Binding Pattern

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Lectin-binding pattern as tool to identify and enrich specific primary testis cells of the tilapia (Oreochromis niloticus) and medaka (Oryzias latipes)

Journal of Experimental Zoology Part B Molecular and Developmental Evolution ◽

10.1002/jez.b.21117 ◽

2007 ◽

Vol 308B (2) ◽

pp. 127-138 ◽

Cited By ~ 6

Author(s):

Sergey V. Tokalov ◽

Herwig O. Gutzeit

Keyword(s):

Oreochromis Niloticus ◽

Lectin Binding ◽

Oryzias Latipes ◽

Binding Pattern

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Lectin-Binding Pattern in Ovarian Structures of Rats with Experimental Polycystic Ovaries

Reproduction in Domestic Animals ◽

10.1111/rda.12174 ◽

2013 ◽

Vol 48 (5) ◽

pp. 850-857 ◽

Cited By ~ 3

Author(s):

CG Barbeito ◽

HH Ortega ◽

V Matiller ◽

EJ Gimeno ◽

NR Salvetti

Keyword(s):

Lectin Binding ◽

Binding Pattern ◽

Polycystic Ovaries

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Lectin-binding pattern of the senegalese sole Solea senegalensis oogenesis

Microscopy Research and Technique ◽

10.1002/jemt.22040 ◽

2012 ◽

Vol 75 (8) ◽

pp. 1124-1135 ◽

Cited By ~ 4

Author(s):

Gianluca Accogli ◽

Sara Zizza ◽

Angel García-lópez ◽

Carmen Sarasquete ◽

Salvatore Desantis

Keyword(s):

Lectin Binding ◽

Solea Senegalensis ◽

Senegalese Sole ◽

Binding Pattern

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Immunogold study on lectin binding in the porcine zona pellucida and granulosa cells

European Journal of Histochemistry ◽

10.4081/846 ◽

2009 ◽

Vol 47 (4) ◽

pp. 353 ◽

Cited By ~ 9

Author(s):

F Parillo ◽

C Dallâ€™Aglio ◽

A Verini Supplizi ◽

P Ceccarelli ◽

AM Gargiulo

Keyword(s):

Sialic Acid ◽

Horseradish Peroxidase ◽

Granulosa Cells ◽

Zona Pellucida ◽

Lectin Binding ◽

Protein A ◽

Ultrastructural Localization ◽

Binding Pattern ◽

Con A ◽

Lectin Receptors

An ultrastructural localization of lectin receptors on the zona pellucida (ZP) of porcine antral oocytes and on the granulosa cells was performed using a panel of horseradish peroxidase- labelled lectins in conjunction with antiperoxidase antibody and protein A-gold. In some cases, lectin incubation was preceded by sialidase digestion. WGA-, Con-A-, UEA-I-, RCA-I-, PNA- and SBA-reactive sites were distributed differently in the porcine ZP. Sialidase digestion increased the positivity obtained with RCA-I and it was necessary to promote PNA and SBA reactivity. These results indicated that the ZP contained N-acetylglucosamine, a-mannose, a- fucose, b-Gal-(1-4)GlcNAc, b-Gal- (1-3)GalNAc, b-GalNAc and sialic acid residues. We also observed the presence of vesicles in both the ooplasm and granulosa cells, showing a similar lectin binding pattern to that of the ZP, thus suggesting that the oocyte and granulosa cells are the site of synthesis of ZP glucidic determinants.

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Lectin binding patterns in normal, metaplastic, and neoplastic gastric mucosa.

Journal of Histochemistry & Cytochemistry ◽

10.1177/40.5.1573249 ◽

1992 ◽

Vol 40 (5) ◽

pp. 681-687 ◽

Cited By ~ 9

Author(s):

T Narita ◽

H Numao

Keyword(s):

Gastric Mucosa ◽

Lectin Binding ◽

Type A ◽

Blood Groups ◽

Blood Type ◽

Luminal Surface ◽

Diffuse Type ◽

Normal Gastric Mucosa ◽

Significant Difference ◽

Tissue Specimens

We investigated lectin binding patterns on tissue specimens of normal and metaplastic gastric surface mucosae, gastric adenomas, and intestinal and diffuse-type gastric carcinomas. Compared with normal gastric mucosa, metaplastic mucosa exhibited an increase of ConA binding and decreases of WGA, PNA, UEA-1, and DBA binding in the cytoplasm, and decreases of ConA, PNA, and UEA-1 binding at the luminal surface. Intestinal carcinomas were similar to metaplastic gastric surface mucosa in ConA, WGA, and UEA-1 binding in the cytoplasm, while diffuse-type carcinomas were similar to normal gastric mucosa in WGA and UEA-1 binding in the cytoplasm. Adenomas were similar to intestinal carcinomas in ConA and UEA-1 binding in the cytoplasm, but were different from intestinal carcinomas in Con A and UEA-1 binding at the luminal surface. For UEA-1, normal and metaplastic gastric surface mucosae did not show a significant difference between the blood type A, AB, B group and the O group. Intestinal and diffuse carcinomas and adenomas also did not show such a difference between the blood groups. For DBA, normal gastric surface mucosa showed a significant difference between the blood type B, O group and the A, AB group. Normal gastric mucosa of the blood type A, AB group was frequently positive for DBA binding in the cytoplasm and at the luminal surface. Metaplastic mucosa did not show a significant difference between the blood groups. Intestinal and diffuse-type carcinomas and adenomas also did not show a difference between the blood groups. DBA binding in the cytoplasm of intestinal carcinomas and adenomas was more frequently positive than that of normal and metaplastic mucosae, except for normal gastric mucosa of the blood type A, AB group. Compared with diffuse-type carcinomas, intestinal carcinomas were accompanied by a significant increase of ConA binding and decreases of WGA and PNA binding in the cytoplasm.

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