Histochemical and Cytochemical Localization of Blood Group Antigens

摘要: The oligosaccharide structures of blood group antigens are not the primary gene products; they constructed in a stepwise manner by adding particular sugar to precursor oligosaccharides via several glycosyltransferases coded for different genes (Watkins 1966, 1978, 1980). Consequently, final profiles expressed each cell type influenced many factors such as intrinsic composition glycosyltransferase species which defined genotype individuals, relative activity or amount these enzymes (repression, derepression induction enzymes), competition between with overlapping substrate specificity, organization membranes, utilizability precursors and specific sugars, level degradating enzymes. Changes antigen during maturation, differentiation malignant transformation thought be intimately related variability factors. Although great importance attaches histo- cytochemical information on distribution levels messenger RNA corresponding relevant enzyme, detailed precise localization their variants is base line analyzing complex On basis individual histochemical findings about interrelationship cells cellular components producing antigenic (cellular subcellular mosaicism), we can deduce well status activation its product, glycosyltransferases. Thus, prerequisite further analysis at molecular genetic level. As emphasized this article, lectin staining immunostaining methods MAbs combined glycosidase digestion procedures powerful tools situ carbohydrate systems. some cases valuable results have been obtained applying technique, our knowledge concerning still far from satisfactory. Along lectins, key developing successful introduction glycosidases, particular, endoglycosidases since reagents indispensable inner core glycoconjugate antigens. Application techniques ultrastructural an alluring possibility, even though difficulties must overcome. functional roles yet determined, diverse array macromolecules known decorated group-related antigens.(ABSTRACT TRUNCATED AT 400 WORDS)