BACKGROUND/AIMS: The purpose of this study was to investigate the malignant potential of aberrant crypt foci (ACF) by measuring the multiplicity of crypts and lectin expression in the early and late stages of 1,2-dimethylhydrazine (DMH)-induced colon carcinogenesis. METHODS: Six-week-old Wistar rats were injected subcutaneously with DMH for 27 weeks. We classified ACF according to the number of crypts per ACF as a few crypts (< or =3 crypts, FC ACF) or numerous crypts (> or =4 crypts, NC ACF). Immunohistochemistry was used to evaluate lectin expression. RESULTS: In the early stage, FC ACF (590/1,902, 31.0%) occurred more frequently than NC ACF (35/449, 7.8%); whereas in the late stage, NC ACF (176/449, 39.2%) occurred more frequently than FC ACF (324/1,902, 17.0%). The number of ACF peaked at 15 to 20 weeks. The ratio of NC/FC ACF increased gradually during carcinogenesis. The expression of both UEA1 and PNA was higher in NC ACF than FC ACF. Lectin expression increased in the late stage compared with the early stage. CONCLUSIONS: The expression of lectin was higher in NC ACF and ACF in the late stage. Therefore, ACF with higher multiplicities in the late stage may have more malignant potential in DMH-induced colon carcinogenesis.
1,2-Dimethylhydrazine ; Aberrant Crypt Foci ; Animals ; Colon ; Dimenhydrinate ; Immunohistochemistry ; Peanut Agglutinin ; Rats ; Rats, Wistar

5-fluorouracil was combined with peanut agglutinin by a water-soluble carbodiimide to prepare the tumor target conjugate of 5-fluorouracil-peanut agglutinin and the ratio of drug to conjugate was determined by the modified trinitrobenzenesulfonic acid method (TNBS). The ratio of drug to conjugate was 76.33%. The result showed that 5-fluorouracil could link to the peanut agglutinin by EDC/NHS crosslinking with high drug ratio.
Antineoplastic Agents ; chemistry ; Cross-Linking Reagents ; chemistry ; Fluorouracil ; chemistry ; Peanut Agglutinin ; chemistry

Using peanut agglutinin(PNA), neurarninidase, and avidin-biotin peroxidase com plex(ABC) technique, normal skin specimens, nevocellular nevi, and malignant melanomas were studied, and different PNA binding patterns between nevocellular nevi and malignant melanomas were observed. The results were as follows : 1. In normal skin, except the basement membrane, epidermis and hair follicle epithelium showed a cell membrane staining of PNA after neuraminidase pretreat ment. Sebaceous glands revealed membranous and cytoplasmic staining of PNA, but sweat ducts were not stained. 2. In nevocellular nevi, none of the nevus cells were stained with PNA aftet neuraminidase preteatment. 3. In malignant melanomas, all of the melanorna cells were stained along the cell mernbrane with PNA after neuraminidase pretreatment. Therefore, the PNA staining after neuraminidase pretreatment on paraffin embedded sections using ABC technique is considered to be a useful probe for the differentiation between malignant malanoma and nevocellular nevus.
Basement Membrane ; Cell Membrane ; Cytoplasm ; Epidermis ; Epithelium ; Hair Follicle ; Melanoma* ; Neuraminidase ; Nevus* ; Paraffin ; Peanut Agglutinin* ; Peroxidase ; Sebaceous Glands ; Skin ; Sweat

Great difficulty may be encountered in the differentiation of basal cell carcinoma from trichoepithelioma snd, in some cases, it may even be irnpossible. Immunohistochemical methods using peanut agglutinin(PNA) which is glycoprotein of non-immune origin selectively binding to galactose-N-acetyl-galactosa-mine are increasingly used in dermatopathology to improve the diagnosis and differential diagnosis. Using PNA, anti-PNA antibody, and peroxidase antiperoxi-dase(PAP) technique, normal skin specimens, basal cell carcinomas, trichoepitheliiomas, and a variety of different skin tumors were studied, and different PNA Ibinding sites between basal cell carcinomas and trichoepitheliomas were observed. The results were as follows : l. In normal skin, except the basement membrane, epidermis and hair follicle epithelium showed a cell membrane staining of PNA, which stained weakly in the Ibssal cell layer. Sebaceous glands revealed membranous and cytoplasmic staining of PNA, but sweat ducts and duct coi1s were mostly negative. 2. 34 of 36(94.4%) basal cell carcinoma sections demonstrated peritumorous PNA-positive bands, and none of 5 trichoepithelioma sections showed peritumorous PNA-binding. 3. Peritumorous PNA-positive bands were strongly positive in solid and keratotic basal cell carcinomas, but decreased or absent in the vicinity of the ulceration or the dense inflammatory infiltration. 4. None of the other skin tumors(squamous cell carcinoms, keratoscanthoma, Bowens disesse and actinic keratosis} showed a periturnorous PNA-positive band. Therefore, we believe that the PNA staining on paraffin-embedded sections using PAP technique can be a useful probe for the differentiation of basal cell carcinoma from trichoepithelioma.
Actins ; Basement Membrane ; Carcinoma, Basal Cell* ; Cell Membrane ; Cytoplasm ; Diagnosis ; Diagnosis, Differential ; Epidermis ; Epithelium ; Glycoproteins ; Hair Follicle ; Peanut Agglutinin* ; Peroxidase ; Sebaceous Glands ; Skin ; Sweat ; Ulcer

Red blood cells that agglutinate with most normal adult sera but never with own sera are termed polyagglutinable and can be separated by patterns of lectin reactivity into various types. Among these polyagglutination, activation of the T cryptantigen occurs when carbohydrate structures on glycophorins A and B lose sialic acid and express the disaccharide Gal beta-l-3 GalNac which reacts with the peanut agglutinin, a lectin from Arachis hypogaea. T activation is a temporary condition due to exposure of the membrane antigen to the action of microbial neuraminidase. In T activated red cells, the following hazards, which are theoretically possible, are spontaneous polyagglutination of red cells in vitro, in vivo and severe blood transfusion reactions. We experienced a case of T activation in 6 month old girl with bacterial meningitis caused by Streptococcus pneumoniae. The reactivity to lectins indicated the patient's red cells were T activated. We report a case of T activation in an infant with the review of literature.
Adult ; Arachis ; Blood Transfusion ; Erythrocytes ; Female ; Glycophorin ; Humans ; Infant ; Lectins ; Membranes ; Meningitis, Bacterial ; N-Acetylneuraminic Acid ; Neuraminidase ; Peanut Agglutinin ; Streptococcus pneumoniae

This study was conducted in order to observe ultrastructural changes in the expression of sialoglycoconjugates in maxillary sinus mucosa after inoculation of influenza A virus utilizing four different gold-labeled lectins : ckia amurensis (MAA), wheat germ agglutinin (WGA), sambucus nigra (SNA), and peanut agglutinin (PNA). A comparison of the affinities of these gold-labeled lectins demonstrated the varying distributions of sialoglycoconjugates in the ciliary layer and the granules in goblet cells. Examination of normal sinus mucosa labeled with four gold-labeled lectins showed the distribution of sialoglycoconjugates to be mainly in the ciliary layer and the granules in goblet cells and restricted to the surface of the cilia, microvilli and the secretory light granules. The application of an influenza A virus infection decreased the labeling intensity of gold-labeled MAA in the cilia and the secretory granules but not of WGA. SNA gold did not label the surface of the cilia and granules in either case. PNA gold particles, however, labeled the cilia and the secretory granules very weakly in normal sinus mucosa, but labeled moderately in cases of influenza A virus infection. These results suggest that the sugar residues of sialoglycoconjugates consist of Neu5Ac(alpha2, 3)Gal, GlcNAc, Neu5Ac. They also suggest that the sugar residues serve as a protecting factor or modulator against influenza A virus infection.
Cilia ; Goblet Cells ; Influenza A virus* ; Influenza, Human* ; Lectins ; Maxillary Sinus ; Microvilli ; Mucous Membrane* ; Peanut Agglutinin ; Rabbits* ; Sambucus nigra ; Secretory Vesicles ; Triticum

Lectins are glycoproteins that specifically bind carbohydrate structures and may participate in the biodefense mechanisms of fish. In this study, the binding of three lectins, Dolichos biflorus agglutinin (DBA), soybean agglutinin (SBA), Bandeiraea simplicifolia BS-1 (isolectin B4), Triticum vulgaris (WGA), Arachis hypogaea (PNA) and Ulex europaeus (UEA-I) were studied in the gill, liver, intestine, kidney, heart, and spleen of the flat fish Paralichthys olivaceus. DBA was detected in intestinal mucous cells, as well as in gill epithelial and mucous cells. It was weakly detected in renal tubule epithelial cells and in bile duct epithelial cells. The strong SBA staining was seen in the intestinal club cells, in bile duct epithelial cells and renal tubule epithelial cells. There were intense positive reactions for isolectin B4 in gill epithelial and mucous cells, and the strong isolectin B4 staining was seen in epithelial cells of the bile duct and intestine. The strong WGA staining was seen in the gill mucosal cells, sinusoid, renal tubule epithelial cells and mucosal cells of the intestine. UEA-I was detected in the gill epithelial and mucosal cells, bile duct epithelial cells and renal tubular epithelial cells. These results suggest that the six lectins examined were localized in the covering epithelia of the various organs of the flat fish and they may participate in the biodefense mechanism of the intra body surface in which is exposed to various antigens.
Animals ; Epithelial Cells/metabolism ; Flatfishes/*metabolism ; Histocytochemistry/veterinary ; Lectins/*metabolism ; Mucus/metabolism ; Peanut Agglutinin/metabolism ; Plant Lectins/metabolism ; Soybean Proteins/metabolism ; Wheat Germ Agglutinins/metabolism