Genetic differences in the histochemically defined structure of oligosaccharides in mice.

A wide range of tissues from three interfertile species of mice and an interspecific hybrid was examined with lectins conjugated to peroxidase to localize specifically glycoconjugates containing terminal alpha-N-acetylgalactosamine, alpha-galactose, and alpha-fucose, and the terminal disaccharide galactose-(beta 1----3)-N-acetylgalactosamine. This battery of lectins disclosed marked heterogeneity of glycoconjugates in different histological sites in a given animal and even between cells in a presumably homogeneous cell population within an organ. No variation with any lectin was observed between individuals of two closely related inbred strains of Mus domesticus at any specific histological or cytological site. In contrast, littermates of an outbred strain of Mus castaneus differed in binding of certain lectins at various sites, attesting to a genetic basis for individual variation. Hybrids between castaneus and domesticus mice also showed individual variation. Moreover, extensive differences between the mouse species were demonstrable with every lectin in glycoconjugates of stored secretions, Golgi cisternae, and apical or basolateral plasmalemma in many cell types. Totaling the differences in tabulated staining intensities for each possible species pair gave a measure of the overall extent of difference at 53 histological sites. According to this measure, the three species are about equally divergent from one another. Some differences between species appeared to depend on histological rather than histochemical variation, as, for example, a greater abundance of granular duct cells in the sublingual and submandibular glands in Mus hortulanus. Other differences were apparently derived from pathological change, as exemplified by casts and lymphoid infiltrates in kidney and structurally atypical submandibular gland lobules in Mus castaneus, and possibly by infiltrating cells in intestinal lamina propria and epithelium in Mus castaneus and hortulanus.

[1]  S. Spicer,et al.  Heterogeneous distribution of glycoconjugates in human kidney tubules , 1985, The Anatomical record.

[2]  S. Spicer,et al.  Histochemical evaluation of secretory glycoproteins in human salivary glands with lectin-horseradish peroxidase conjugates. , 1984, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[3]  S. Spicer,et al.  Histochemical evaluation of mouse and rat kidneys with lectin-horseradish peroxidase conjugates. , 1983, The American journal of anatomy.

[4]  A. Wilson,et al.  Mitochondrial DNA evolution in mice. , 1983, Genetics.

[5]  H. Holthofer Lectin binding sites in kidney. A comparative study of 14 animal species. , 1983 .

[6]  B. Ponder,et al.  Organ-related differences in binding of Dolichos biflorus agglutinin to vascular endothelium. , 1983, Developmental biology.

[7]  S. Spicer,et al.  Light microscopic histochemical detection of sugar residues in secretory glycoproteins of rodent and human tracheal glands with lectin-horseradish peroxidase conjugates and the galactose oxidase-Schiff sequence. , 1983, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[8]  R. Parmley,et al.  Cytochemistry of complex carbohydrates by light and electron microscopy: available methods and their application. , 1983, Monographs in pathology.

[9]  S. Spicer,et al.  Alterations in the proximal nephron of beige mice with the Chédiak-Higashi syndrome. , 1982, The American journal of pathology.

[10]  G. Strecker,et al.  Specificity of Twelve Lectins Towards Oligosaccharides and Glycopeptides Related to N‐Glycosylproteins , 2005 .

[11]  T. Muramatsu,et al.  Discrete Distribution of binding sites for Dolichos biflorus agglutinin (DBA) and for peanut agglutinin (PNA) in mouse organ tissues. , 1981, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[12]  S. Spicer,et al.  Histochemical reactivity of peanut lectin-horseradish peroxidase conjugate. , 1980, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[13]  N. Kochibe,et al.  Purification and properties of a novel fucose-specific hemagglutinin of Aleuria aurantia. , 1980, Biochemistry.

[14]  D. Fiete,et al.  Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides. , 1979, The Journal of biological chemistry.

[15]  L. A. Murphy,et al.  Carbohydrate binding specificity of four N-acetyl-D-galactosamine- "specific" lectins: Helix pomatia A hemagglutinin, soy bean agglutinin, lima bean lectin, and Dolichos biflorus lectin. , 1977, Biochemistry.

[16]  R. Lotan,et al.  The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). , 1975, The Journal of biological chemistry.

[17]  I. Goldstein,et al.  An alpha-D-galactosyl-binding lectin from Bandeiraea simplicifolia seeds. Isolation by affinity chromatography and characterization. , 1974, The Journal of biological chemistry.

[18]  N. Sharon,et al.  Lectins: cell-agglutinating and sugar-specific proteins. , 1972, Science.

[19]  L. Orgel,et al.  Biochemical Evolution , 1971, Nature.

[20]  E. Kabat,et al.  Purification and characterization of a lectin (plant hemagglutinin) with blood group A specificity from Dolichos biflorus. , 1970, Biochemistry.

[21]  S. Avrameas,et al.  Coupling of enzymes to proteins with glutaraldehyde. Use of the conjugates for the detection of antigens and antibodies. , 1969, Immunochemistry.

[22]  E. Holborow,et al.  The distribution of the blood group. A antigen in human tissues. , 1960, British journal of experimental pathology.

[23]  V. Joysey The relation between animal and human blood groups. , 1959, British medical bulletin.