Publication: Histochemical demonstration and analysis of poly-N-acetyllactosamine structures in normal and malignant human tissues
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Date
1996
Authors
Ito, N. ; yokota, M. ; Nagaike, C. ; Morimura, Y. ; Hatake, K. ; Matsunaga, T.
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Publisher
Murcia : F. Hernández
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DOI
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info:eu-repo/semantics/article
Description
Abstract
Poly-N-acetyllactosaminyl structures carry a
variety of physiologically and pathologically important
carbohydrate antigens and are presumed to have
essential roles in the process of cellular recognition,
differentiation, malignant transformation and cancer
metastasis. Monoclonal antibodies, lectins and endo-Bgalactosidase
are useful histochemical tools for detecting
and analyzing poly-N-acetyllactosamines in tissue
sections. 1 (branched structure) and i (linear structure)
antigens recognized by monoclonal antibodies have been
shown to be differentiation antigens in mouse embryo
and mouse and human teratocarcinoma cells as well as
in human erythrocytes. They are also oncofoetal antigens
and are expressed in carcinoma cells in severa1 tissues
and organs. Immobilized lectins specific to po1y-Nacetyllactosamine
structures have been successfully
applied for fractioning glycoproteins with po1y-Nacetyllactosamine,
but histochemical use of these lectins
has been restricted to some animal tissues. Arnong them,
pokeweed mitogen agglutinin was used to detect
branched poly-N-acetyllactosamine in normal and
malignant human colon, demonstrating that it has a
highly selective affinity for colorectal carcinomas.
Griffonia simplicifolia agglutinin-11 staining following
endo-B-galactosidase digestion procedure revealed the
presence of poly-N-acetyllactosamine structures with or without blood group-specificities in severa1 normal
human tissues. By using this procedure, it was
demonstrated that the blood group-related antigens
oncofoetally expressed in thyroid carcinoma cells are
carried by poly-N-acetyllactosamines containing a
domain susceptible to the enzyme digestion. Staining
with lectins specific to poly-N-acetyllactosamine in
combination with endo-B-galactosidase digestion
demonstrated that poly-N-acetyllactosaminyl structures
ubiquitously and consistently produced in thyroid
papillary carcinomas are highly heterogeneous in their
chain length and branching status and quite different from those produced in other thyroid neoplasms.
Staining with monoclonal antibodies or lectins combined
with endo-B-galactosidase digestion procedures have
been proven to be powerful tools for localizing and
analyzing different types of poly-N-acetyllactosamine
structures in normal and malignant tissues.
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