Genetic and Sex-related Differences in the Structure of Submandibular Glycoconjugates

Schulte, Bradley A.

doi:10.1177/00220345870660021001

Cited by 23 publications

(20 citation statements)

References 48 publications

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“…The nine lectins used here were selected for their ability to distinguish the different types of cells present histochemically in the rat submandibular gland. The staining with UEA-I, LFA, PNA, LCA, DBA, and SBA (see Table 1) corresponded to previous studies (Schulte, 1987; Schulte and Spicer, 1984). Our ble to fine discrepancies in their preferred sugars with regard to both penultimate sugar and anomeric configuration (Spicer and Schulte, 1992;Watanabe et al, 1981;Lotan and Nicolson, 1979;Lis and Sharon, 1973;Sharon and Lis, 1972).…”

Section: Discussionsupporting

confidence: 88%

“…The application of labeled lectins in situ has provided information about the identity and distribution of specific glycoconjugates in secretory granules of various cell populations in different salivary glands (see Accili et al, 1992;Hosaka et al, 1986;Schulte, 1987;Schulte and Spicer, 1983Yamada and Shimizu, 1979). These studies have revealed a considerable heterogeneity in the secretory glycoconjugates present in salivary parenchymal cells.…”

Section: Introductionmentioning

confidence: 99%

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Use of lectin probes on tissues and sympathetic saliva to study the glycoproteins secreted by rat submandibular glands.

Zhang¹,

Proctor²,

Garrett³

et al. 1994

J Histochem Cytochem.

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We used a panel of nine lectins to detect the glycosylation patterns of rat submandibular glycoproteins. Binding of lectins was assessed on tissue sections and on Western blots of electrophoretically separated glycoproteins from glandular extracts or sympathetic saliva. Histochemical staining of tissue sections showed that two lectins (DBA and SBA) with affinity for terminal GalNAc residues were localized specifically to acinar cells. In contrast, LTA and UEA-I (alpha Fuc-directed) and LFA (NeuAc-directed) bound exclusively to granular tubule cells. PNA and MPA (beta Gal-directed), LCA (alpha Man- and alpha Glc-directed), WGA (beta GlcNAc- and NeuAc-directed), and sWGA (beta GlcNAc-directed) bound to both acinar and granular tubule cells. On electroblot preparations, LFA, PNA, WGA, DBA, and SBA reacted with high molecular weight acinar mucin components both in glandular extracts and in saliva. LTA, UEA-I, LFA, PNA, MPA, LCA, WGA, sWGA, and DBA bound to lower molecular weight bands on blots known to contain granular tubular proteinases. Lectin binding to acini and granular tubules was reduced in sections and in most bands from glandular extracts after sympathetic nerve stimulation. Our results show that (a) secretory glycoproteins from rat submandibular acinar cells are non-fucosylated and contain abundant alpha GalNAc and NeuAc and a small proportion of beta Gal in their oligosaccharide side chains, and (b) alpha Fuc, NeuAc, beta Gal, and alpha GalNAc form the major carbohydrate moieties of the secretory glycoproteins from granular tubules. The results confirm the considerable potential of lectin probes for studying glycoproteins in secretions and in their cells of origin.

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Section: Discussionsupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Use of lectin probes on tissues and sympathetic saliva to study the glycoproteins secreted by rat submandibular glands.

Zhang¹,

Proctor²,

Garrett³

et al. 1994

J Histochem Cytochem.

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“…These tendencies have been noted previously in salivary glands from other species by Schulte [9], who commented, "In some species, heterogeneity in glycoprotein structure was observed among morphologically similar cells within a gland". More recently Menghi et al [8] have noted differences in lectin binds between adjacent convoluted granular tubule cells in rats.…”

Section: Discussionsupporting

confidence: 80%

Lectin Histochemistry to Study Nerve-induced Exocytosis from Rabbit Submandibular Glands.

Garrett

Zhang

Proctor

et al. 1997

Acta Histochem. Cytochem

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“…The many locations containing Galfi1,3GalNAc penultimate to sialic acid are recognized as those gaining PNA affinity after sialidase digestion (120,173,(175)(176)(177)180,183,184,219). Sites such as acini of hamster and ovine submandibular glands gain DBA reactivity after sialidase and therefore contain aGalNAc penultimate to sialic acid (178,184).…”

Section: Gzffoniz Szmpfk$olia Isoagglutinin I1 Exemplifies Another Lementioning

confidence: 99%

“…The application of a battery of lectins with varying specificities has revealed striking differences between GCs in the various cell types, in particular those of the gastrointestinal, genitourinary, respiratory, and nervous systems (9,30,31,36,56, 63,76,87,122,169,173,[175][176][177][178][179][180][181][182][183][184][185]201,212,213,219,221,235) which have been most thoroughly examined in this laboratory. These ddferences presumably can be attributed in some cases to differing glycopeptide content between cells and in other instances to cell-specific glycosylation of a given polypeptide (148,228) common to more than one cell type.…”

Section: Gcs D I -E R Among Cell Q P E S In An Individualmentioning

confidence: 99%

Diversity of cell glycoconjugates shown histochemically: a perspective.

Spicer

Schulte²

1992

J Histochem Cytochem.

380

297

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IntroductionThe earliest histochemical methods for demonstrating carbohydratecontaining macromolecules served mainly to &rentiate these substances, as a general class, from the other macromolecular constituents in tissue sections: the proteins, nucleic acids, and lipids (93,137). A later stage in the development of this field aimed at distinguishing by histochemistry subclasses of carbohydratecontaining components, e.g., neutral and acidic constituents and subgroups of the acidic substances. The capacity to characterize complex carbohydrates in situ in tissue sections progressed subsequently with the use of carbohydrate-degrading enzymes to locate moieties possessing a specific carbohydrate linkage labile to the enzyme and of immunostaining to identlfy specific epitopes. An added dimension for analysis of glycoconjugate (GC) structure in situ followed the advent of labeled lectins which allow histochemical demonstration of terminal or internal sugars or of sugar sequences.This review attempts to put in perspective the status of carbohydrate histochemistry before and after introduction of the lectin approach. Progress in the development and application of non-lectin methods for light and electron microscopic localization has been reviewed (126,137,153,172,175,205,210,213,234) and will be covered here in summary form. A voluminous literature on lectin histochemistry and its use in a wide range of adult and embryonic tissues and pathological lesions at the light and electron microscopic level has also been reviewed extensively tinctive chemical structure in diverse sites of highly specialized biologica1 activity. Such an association implies relevance of the chemical nature of the GC to the function where it occurs. A number of examples of such concurrence will be described that point to possible participation of a specific GC in a particular biological function at a precise histological or cytological site. Pre-lectin Histochemistry of Complex CarbohydratesA large class of macromolecules in mammalian tissues differs from the other classes in possessing sugar residues. These carbohydratecontaining components are referred to in general as complex carbohydrates, a term that includes both polysaccharides, such as glycogen, and glycoconjugates (GCs), in which sugars are linked to non-carbohydrate moieties. Histochemical methods specific for visualizing GCs and differentiating them from proteins, nucleic acids, and lipids depended initially on their content of sugars with vicinal hydroxyls and of distinctive acidic moieties (26) (Figure 1; Eble 1). Thus, GCs which alone among the classes of macromolecules contain hexoses with vicinal hydroxyls were visualized selectively with the periodic acid-Schiff (PAS) procedure (93, 109). In addition, highly acidic sulfate esters and less acidic carboxyls of sialic acids and uronic acids in G C s were found to bind a variety of cationic dyes that did not react with less acidic dicarboxylic amino acids in proteins or with nucleic acids. Basic reagents commonly used included alcian bl...

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Genetic and Sex-related Differences in the Structure of Submandibular Glycoconjugates

Cited by 23 publications

References 48 publications

Use of lectin probes on tissues and sympathetic saliva to study the glycoproteins secreted by rat submandibular glands.

Use of lectin probes on tissues and sympathetic saliva to study the glycoproteins secreted by rat submandibular glands.

Lectin Histochemistry to Study Nerve-induced Exocytosis from Rabbit Submandibular Glands.

Diversity of cell glycoconjugates shown histochemically: a perspective.

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