Effects of tunicamycin upon glycoprotein synthesis and development of early mouse embryos

Atienza-Samols, Sui Bi; Pine, Perla Razon; Sherman, Michael I.

doi:10.1016/0012-1606(80)90070-6

Cited by 70 publications

(20 citation statements)

References 24 publications

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“…These experiments showed that preincubation of lymphocytes with either tunicamycin, an inhibitor of N-glycosylation of proteins [42] or 4-methylumbelliferyl-~-D-xyloside, a partial modifier of glycosaminoglycan synthesis [43], had no effect on lymphocyte migration. Similarly, treatment of lymphocytes with hyaluronidase and chondroitinase ABC did not modify the migration of lymphocytes.…”

Section: Discussionmentioning

confidence: 94%

Modification of lymphocyte migration by sulfated polysaccharides

Brenan

Parish

1986

Eur J Immunol

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The role of sulfated polysaccharides in lymphocyte migration has been analyzed in vivo using lymphocytes labeled with an intracellular DNA-binding fluorochrome Hoechst 33342. The influence of a panel of sulfated polysaccharides on entry (by injecting the sulfated polysaccharide prior to the labeled cells) and displacement from lymphoid organs (by injecting the sulfated polysaccharide after the labeled cells have localized) indicated that different sulfated polysaccharides have selective effects on entry and displacement, and furthermore positioning of subpopulations within organs. Additional experiments suggested that receptors for sulfated polysaccharides on high endothelial venules may interact with complementary structures on lymphocytes. The data supporting this conclusion were: (a) the normal localization behavior of lymphocytes preincubated with sulfated polysaccharides; (b) an inverse relationship between the expression of lymphocyte surface receptors for sulfated polysaccharides and the ability of the lymphocytes to enter lymphoid organs and (c) the selective binding of sulfated polysaccharide-coupled fluoresceinated beads to high endothelial venules. In this case only the beads coupled with the sulfated polysaccharides that inhibited entry bound to the high endothelial venules. These findings are discussed in terms of a fundamental cellular recognition system utilizing sulfated polysaccharides.

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Section: Discussionmentioning

confidence: 94%

Modification of lymphocyte migration by sulfated polysaccharides

Brenan

Parish

1986

Eur J Immunol

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“…In addition, cell adhesion molecules and other membrane glycoproteins required for compaction and preimplantation development, such as E-cadherin, carry N-glycans (49,65). N-glycan synthesis is increased at the blastocyst stage (2), and treatment of preimplantation mouse embryos with tunicamycin, an inhibitor of N-glycan synthesis, prevents blastocyst development (3,58). However, tunicamycin removes all N-glycans, resulting in empty glycosylation sites with severe structural consequences.…”

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confidence: 99%

Inactivation of the Mgat1 Gene in Oocytes Impairs Oogenesis, but Embryos Lacking Complex and Hybrid N-Glycans Develop and Implant

Shi

Williams

Seppo

et al. 2004

Molecular and Cellular Biology

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Complex and hybrid N-glycans contain sugar residues that have been implicated in fertilization, compaction of the embryo, and implantation. Inactivation of the Mgat1 gene responsible for their synthesis is embryonic lethal, but homozygous mutant blastocysts are phenotypically normal due to the presence of maternal Mgat1 gene transcripts. To identify roles for complex and hybrid N-glycans in oogenesis and preimplantation development, the Mgat1 gene in oocytes was deleted by using a ZP3Cre recombinase transgene. All mutant oocytes had an altered zona pellucida (ZP) that was thinner than the control ZP, and they did not possess complex N-glycans but contained ZP1, ZP2, and ZP3 glycoproteins. Mutant eggs were fertilized, all embryos implanted, and heterozygotes developed to birth. However, mutant females had decreased fertility, yielded fewer eggs after stimulation with gonadotropins, and produced a reduced number of preimplantation embryos and less progeny than controls. About 25% of embryonic day 3.5 (E3.5) embryos derived from mutant eggs were severely retarded in development, even when they were heterozygous and expressed complex N-glycans. Thus, a proportion of Mgat1 ؊/؊ oocytes were developmentally compromised. Surprisingly, mutant eggs also gave rise to Mgat1 ؊/؊ embryos that developed normally, implanted, and progressed to E9.5. Therefore, complex or hybrid N-glycans are required at some stage of oogenesis for the generation of a developmentally competent oocyte, but fertilization, blastogenesis, and implantation may proceed in their absence.

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“…That carbohydrate residues may be important during embryogenesis was first inferred from their rapid and permanent modulation at various stages of development (Richa and Solter, 1986). Indeed, carbohydrates have now been directly implicated in the processes of fertilisation (Wassarman, 1987;Bleil and Wasserman, 1988) and of compaction in the early mouse embryo (Surani, 1979;Atienza-Samols et al, 1980;Rastan et al, 1985). Sur-0 1995 WILEY-LISS, INC.…”

Section: Introductionmentioning

confidence: 99%

Galectin‐3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo

Fowlis

Colnot

Ripoche

et al. 1995

Developmental Dynamics

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The galectins are a family of low molecular weight, calcium-independent mammalian carbohydrate binding proteins that exhibit specificity for beta-galactoside derivatives. We have examined the expression pattern of galectin-3 in the developing mouse embryo by in situ hybridisation and immunohistochemistry. In the embryo proper, galectin-3 message and protein are first detected in notochord, starting from 8.5 days post coitum (dpc), and persist until this structure disappears. Galectin-3 is later found in cartilage primordia and in developing skin from 13.5 dpc. This very restricted and dynamic pattern suggests that galectin-3 may participate in the establishment and/or maintenance of notochord as well as the formation of cartilage and differentiation of skin. Finally, we find that galectin-3, which is identical to the macrophage marker Mac-2, is also expressed in embryonic macrophages. 0 1995 Wiley-Liss, Inc.

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Effects of tunicamycin upon glycoprotein synthesis and development of early mouse embryos

Cited by 70 publications

References 24 publications

Modification of lymphocyte migration by sulfated polysaccharides

Modification of lymphocyte migration by sulfated polysaccharides

Inactivation of the Mgat1 Gene in Oocytes Impairs Oogenesis, but Embryos Lacking Complex and Hybrid N-Glycans Develop and Implant

Galectin‐3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo

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