Histochemical demonstration of different types of poly-N-acetyllactosamine structures in human thyroid neoplasms using lectins and endo-beta-galactosidase digestion.
Blood-group-related antigens expressed in papillary carcinomas and other types of neoplasm of the human thyroid glands have been shown to be carried by poly-N-acetyllactosamines containing a linear domain susceptible to endo-beta-galactosidase digestion. To make clear more precisely the backbone poly-N-acetyllactosamine structures, labelled lectins specific to different types of these structures and specific to core structures with beta 1-6GlcNAc branching of N- and O-linked glycoproteins were employed in conjunction with prior endo-beta-galactosidase digestion on formalin-fixed, paraffin-embedded neoplasms of the human thyroid glands. In papillary carcinomas, Datura stramonium agglutinin (DSA) and succinyl wheat germ agglutinin (Suc-WGA) reacted most consistently and frequently with papillary carcinomas from all the individuals examined. Pokeweed mitogen (PWM) likewise stained the cells of papillary carcinomas from all the individuals examined, but in some individuals the number of lectin-reactive cells were very small. Lycoperscion esculentum aggultinin (LEA), Solanum tuberosum agglutinin (STA), Phaseolus vulgaris agglutinin L (PHA-L) and Artocarpus integrifolia agglutinin (jacalin) similarly bound to the cancer cells from most of the individuals, and in these cases the number of reactive cells was usually much more restricted than was the case with DSA or PWM. In adenoma and other types of carcinoma, such as follicular carcinomas, these lectins specific to poly-N-acetyllactosamine exhibited slight or no reactivity with the cells, whereas PHA-L and jacalin similarly bound to the cells of adenomas and carcinomas from most of the individuals examined. Prior digestion with endo-beta-galactosidase completely eliminated or markedly reduced the reactivity with PWM and LEA in papillary carcinomas. Reactivity with DSA, Suc-WGA, STA, PHA-L and jacalin was slightly reduced or not at all affected by enzyme digestion. These results confirmed that poly-N-acetyllactosamine species found in papillary carcinomas are quite different from those in other types of thyroid neoplasm, suggesting that at least three different types of poly-N-acetyllactosamine, that is, linear unbranched short and long sequences and highly branched ones are produced in these cells.
Ito
N
N
Department of Legal Medicine, Nara Medical University, Japan.
Yokota
M
M
Kawahara
S
S
Nagaike
C
C
Morimura
Y
Y
Hirota
T
T
Matsunaga
T
T
D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005260:Female; D006023:Glycoproteins / Q000032:analysis; D006026:Glycoside Hydrolases; D006651:Histocytochemistry; D006801:Humans; D037102:Lectins; D008297:Male; D008875:Middle Aged; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000032:analysis*; D012680:Sensitivity and Specificity; D013964:Thyroid Neoplasms / Q000737:chemistry* / Q000473:pathology; D001616:beta-Galactosidase / Q000378:metabolism*
D006023:Glycoproteins; D037102:Lectins; D011134:Polysaccharides; C037199:poly-N-acetyllactosamine; D006026:Glycoside Hydrolases; C026093:keratan-sulfate endo-1,4-beta-galactosidase; D001616:beta-Galactosidase