Production of hybrid glycoproteins and accumulation of oligosaccharides in the brain of sheep and pigs administered swainsonine or locoweed

Tulsiani, D. R. P.; Broquist, Harry P.; James, Lynn F.; Touster, Oscar

doi:10.1016/0003-9861(88)90327-x

Cited by 58 publications

(32 citation statements)

References 29 publications

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“…Swainsonine is known to induce a storage disease similar to the genetic mannosidosis as well as a potent inhibitor of lysosomal mannosidase and Golgi mannosidase II. Loss of mannosidase activity ultimately leads to cellular vacuolation and cellular death in a variety of organs, including the cerebrum and cerebellum [30, 31]. Similar to other studies, lectin histochemistry demonstrated Con-A positive findings in the cytoplasmic vacuoles of Purkinje cells of the present goats, suggesting accumulation of mannose rich oligosaccharide material in the vacuoles [24].…”

Section: Discussionsupporting

confidence: 80%

Cerebellar Ataxia Suspected to Be Caused by <i>Oxytropis glabra</i> Poisoning in Western Mongolian Goats

Takeda

Tanaka

Shimada

et al. 2014

The Journal of Veterinary Medical Science

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In the last five years in western Mongolia, a neurological disorder and resultant economic loss have developed in goats, sheep, cattle and horses: association of the disease with ingestion of Oxytropis glabra, a toxic plant, was suggested. Affected goats showed neurological signs, including ataxia, incoordination, hind limb paresis, fine head tremor and nystagmus. Three goats, one with moderate clinical signs and the other two with severe clinical signs, were necropsied and examined to describe and characterize the histologic, immunohistochemical and ultrastructural lesions. Although no gross pathological changes were observed in a variety of organs including the central nervous system of these goats, microscopic examination of the cerebellum demonstrated degenerative changes in all these goats, such as vacuolar changes and loss of Purkinje cells, torpedo formation in the granular layer, increased number of spheroids in the cerebellar medulla, and loss of axons and myelin sheaths of Purkinje cells. The chemical analysis of the dried plant detected 0.02–0.05% (dry weight basis) of swainsonine. This is the first report describing the clinical and pathological findings in Mongolian goats suspected to be affected by O. glabra poisoning.

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Section: Discussionsupporting

confidence: 80%

Cerebellar Ataxia Suspected to Be Caused by <i>Oxytropis glabra</i> Poisoning in Western Mongolian Goats

Takeda

Tanaka

Shimada

et al. 2014

The Journal of Veterinary Medical Science

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“…The detection of this compensatory (possibly exemplary) backup mechanism can be interpreted as a sign of the vital importance of maintaining correct processing of N-glycans. This view is corroborated by independent experience with (i) glycosylation inhibitors such as swainsonine from plants of the genus Swainsona, which cause a disease known as locoism [530], or tunicamycin whose deadly effects due to blocking Nglycosylation at the first step of the dolichol cycle, that is the formation of Dol-P-P-GlcNAc, are counterbalanced by gene amplification [531] as well as (ii) with deliberately engineered loss-of-function mutants after altering a glycosyltransferase gene in the mouse genome [463,532,533]. Knockout mice with gene disruption in N-acetylglucosaminyltransferase I, which effectively reduces glycosylation to a 'yeast-or insect-like' status, are invariably subject to embryonic lethality, although mutant cells in vitro suffer no overt consequences [463,532,533].…”

Section: Review Articlementioning

confidence: 60%

Eukaryotic glycosylation: whim of nature or multipurpose tool?

Reuter¹,

Gabius²

1999

Cellular and Molecular Life Sciences (CMLS)

214

141

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Protein and lipid glycosylation is a ubiquitous phenomenon. The task of cataloguing the great structural variety of the glycan part has demanded considerable efforts over decades. This patient endeavor was imperative to discern the inherent rules of glycosylation which cannot affirm assumptions on a purely coincidental nature of this type of protein and lipid modification. These results together with theoretical considerations uncover a salient property of oligosaccharides. In comparison with amino acids and nucleotides, monosaccharides excel in their potential to serve as units of hardware for storing biological information. Thus, the view that glycan chains exclusively affect physiochemical properties of the conjugates is indubitably flawed. This original concept has been decisively jolted by the discovery of endogenous receptors (lectins) for distinct glycan epitopes which are as characteristic as a fingerprint or a signature for a certain protein (class) or cell type. Recent evidence documents that these binding proteins are even endowed with the capacity to select distinct low-energy conformers of the often rather flexible oligosaccharides, granting entry to a new level of regulation of ligand affinity by shifting conformer equilibria. The assessment of the details of this recognition by X-ray crystallography, nuclear magnetic resonance spectroscopy, microcalorimetry and custom-made derivatives is supposed to justify a guarded optimism in satisfying the need for innovative drug design in antiadhesion therapy, for example against viral or bacterial infections and unwanted inflammation. This review presents a survey of the structural aspects of glycosylation and of evidence to poignantly endorse the notion that carrier-attached glycan chains can partake in biological information transfer at the level of cell compartments, cells and organs.

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“…Sialylated hybrid oligosaccharide was prepared after endo-N-acetyl-~-D-glucosaminidase treatment of [3H]mannose-labeled glycopeptides prepared from the rat epididymal epithelial cells cultured in the presence of swainsonine (10 #g/ml of the culture medium) as described previously (38). This oligosaccharide (NANAGalGIcNAcMansGIcNAc) was treated with sialidase and fl-D-galactosidase as described (38), and the resulting oligosaccharide (GIcNAcMansGIcNAc) was purified by high resolution gel filtration on a column of Bio-Gel P-4 (42). Swainsoninc isolated from Rhizoctonia leguminicola (32) was provided by Dr. H. P. Broquist of this university, l-Deoxymannojirimycin was from Boehringer Mannheim Diagnostics, Inc., Houston, TX.…”

Section: Methodsmentioning

confidence: 99%

Novel alpha-D-mannosidase of rat sperm plasma membranes: characterization and potential role in sperm-egg interactions.

Tulsiani

Skudlarek

Orgebin‐Crist

1989

The Journal of Cell Biology

130

100

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Abstract. During the course of a study of glycoprotein processing mannosidases in the rat epididymis, we have made an intriguing discovery regarding the presence of a novel ot-o-mannosidase on the rat sperm plasma membranes. Unlike the sperm acrosomal "acid" mannosidase which has a pH optimum of 4.4, the newly discovered Ot-D-mannosidase has a pH optimum of 6.2, and 6.5 when assayed in sperm plasma membranes and intact spermatozoa, respectively. In addition, the two enzymes show different substrate specificity. The acrosomal Ot-D-mannosidase is active mainly towards synthetic substrate, p-nitrophenyl a-Dmannopyranoside, whereas the sperm plasma membrane O~-D-mannosidase shows activity mainly towards mannose-containing oligosaccharides. Evidence is presented which suggest that the sperm plasma membrane Ot-D-mannosidase is different from several processing mannosidases previously characterized from the rat liver.The newly discovered a-D-mannosidase appears to be an intrinsic plasma membrane component, since washing of the purified membranes with buffered 0.4 M NaCI did not release the enzyme in soluble form. The enzyme requires nonionic detergent (Triton X-100) for complete solubilization. The enzyme is activated by Co 2+ and Mn 2÷. However, Cu 2÷ and Zn 2÷ are potent inhibitors of the sperm plasma membrane Ot-D-mannosidase. At a concentration of 0.1 mM, these divalent cations caused nearly complete inactivation of the sperm enzyme. In addition methyl-c~-D-mannoside, methyl-ot-D-glucoside, mannose, 2-deoxy-D-glucose, and D-mannosamine are inhibitors of the sperm surface a-D-mannosidase. The physiological role of the newly discovered enzyme is not yet known. Several published reports in three species, including the rat, suggest that the sperm surface c~-o-mannosidase may have a role in binding to mannose-containing saccharides presumably present on the zona pellucida.I X is generally accepted that one step in the fertilization process requires interaction between complementary molecules present on the surface of the spermatozoon and the zona pellucida. The chemical nature of these complementary recognition sites is poorly understood, although there is growing evidence that carbohydrate moieties on surface membrane glycoconjugates are involved in these interactions (1, 34).In mammals, several sperm proteins have been suggested to bind to zona pellucida (28). Some of these macromolecules have enzymatic activity and are thought to form a stable enzyme-substrate complex by binding to the oligosaccharide units present on the zona pellucida glycoproteins. In mice, galactosyltransferase present on the head region of the spermatozoa mediates sperm-egg binding by interacting with its substrate on the zona pellucida (23). There is also evidence that trypsin-like protease present on spermatozoa of mouse (4, 31) initiates sperm-egg binding. Mouse spermatozoa also contain sialyltransferase (13) and fucosyltransferase (30). The latter enzyme has been suggested to be involved in some aspect of sperm-egg recognition (Apter, E M., ...

show abstract

Production of hybrid glycoproteins and accumulation of oligosaccharides in the brain of sheep and pigs administered swainsonine or locoweed

Cited by 58 publications

References 29 publications

Cerebellar Ataxia Suspected to Be Caused by <i>Oxytropis glabra</i> Poisoning in Western Mongolian Goats

Cerebellar Ataxia Suspected to Be Caused by <i>Oxytropis glabra</i> Poisoning in Western Mongolian Goats

Eukaryotic glycosylation: whim of nature or multipurpose tool?

Novel alpha-D-mannosidase of rat sperm plasma membranes: characterization and potential role in sperm-egg interactions.

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