The cell surface proteoglycan from mouse mammary epithelial cells bears chondroitin sulfate and heparan sulfate glycosaminoglycans.

Rapraeger, Alan C.; Jalkanen, Markku; Endo, Eiko; Koda, Joy E.; Bernfield, Merton

doi:10.1016/s0021-9258(17)39146-9

Cited by 263 publications

(38 citation statements)

References 35 publications

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“…As the outermost layer of the cell, the glycocalyx is a highly versatile network consisting mainly of proteoglycans [5] and glycoproteins covering the membrane. The glycocalyx exhibits different important functions, e.g., from being a physical barrier regulating endocytotic processes [6][7][8], mediating immunogenicity [9][10][11][12], cell adhesion [13][14][15] and signaling [16], to the transduction of shear stress toward the cytoskeleton [17][18][19].…”

Section: Introductionmentioning

confidence: 99%

Metabolic Glycoengineering in hMSC-TERT as a Model for Skeletal Precursors by Using Modified Azide/Alkyne Monosaccharides

Altmann

Mut

Wolf

et al. 2021

IJMS

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Metabolic glycoengineering enables a directed modification of cell surfaces by introducing target molecules to surface proteins displaying new features. Biochemical pathways involving glycans differ in dependence on the cell type; therefore, this technique should be tailored for the best results. We characterized metabolic glycoengineering in telomerase-immortalized human mesenchymal stromal cells (hMSC‑TERT) as a model for primary hMSC, to investigate its applicability in TERT-modified cell lines. The metabolic incorporation of N‑azidoacetylmannosamine (Ac4ManNAz) and N‑alkyneacetylmannosamine (Ac4ManNAl) into the glycocalyx as a first step in the glycoengineering process revealed no adverse effects on cell viability or gene expression, and the in vitro multipotency (osteogenic and adipogenic differentiation potential) was maintained under these adapted culture conditions. In the second step, glycoengineered cells were modified with fluorescent dyes using Cu-mediated click chemistry. In these analyses, the two mannose derivatives showed superior incorporation efficiencies compared to glucose and galactose isomers. In time-dependent experiments, the incorporation of Ac4ManNAz was detectable for up to six days while Ac4ManNAl-derived metabolites were absent after two days. Taken together, these findings demonstrate the successful metabolic glycoengineering of immortalized hMSC resulting in transient cell surface modifications, and thus present a useful model to address different scientific questions regarding glycosylation processes in skeletal precursors.

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Section: Introductionmentioning

confidence: 99%

Metabolic Glycoengineering in hMSC-TERT as a Model for Skeletal Precursors by Using Modified Azide/Alkyne Monosaccharides

Altmann

Mut

Wolf

et al. 2021

IJMS

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Section: Syndecan-1 and Its Gag Chainsmentioning

confidence: 99%

“…Syndecan-1, a membrane PG originally isolated from mouse mammary epithelial cells (Rapraeger and Bernfield 1983), is the first hybrid-type PG described bearing both heparan sulfate (HS) and chondroitin sulfate (CS) chains; the latter are shorter at least in mouse mammary epithelial cells (Rapraeger et al 1985). The notion that GAG chains, particularly the HS chains, would anchor the cells to the extracellular matrix (Rapraeger et al 1985) was raised in the "early days" of syndecan. A comparison of syndecan-1 from simple and stratified epithelia showed that molecular heterogeneity between the two samples depends largely on the fact that the same core protein is substituted with more and longer GAG chains in the simple epithelium, which may account for differences in how these two tissue types are organized (Sanderson and Bernfield 1988).…”

Section: Syndecan-1 and Its Gag Chainsmentioning

confidence: 99%

The Mutual Impact of Syndecan-1 and Its Glycosaminoglycan Chains—A Multivariable Puzzle

Eriksson

Spillmann

2012

J Histochem Cytochem.

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Proteoglycans, with their core proteins and attached glycosaminoglycan chains, are recognized as important partners in many biological processes, yet often experimental analysis of their molecular action is considered for only part of these molecules: either the protein or the carbohydrate unit. In this article, we have tried to summarize, with an example of the syndecan family in general and more specifically with syndecan-1, what is known considering the mutual influence of these different components, and we follow whether the nature of the glycosaminoglycan chains matters for these effects.

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“…Wherever it has been analyzed, syndecan-1 bears heparan sulfate chains, but in some epithelia, there are additional chondroitin or dermatan sulfate chains. This was noted particularly in non-stratifying epithelial cell types, including the NMuMg line [7,8]. It is proposed that the chondroitin/dermatan sulfate chains are located more membrane-proximally, while the heparan sulfate chains are located distally [8].…”

Section: Introductionmentioning

confidence: 99%

Syndecan-1 (CD138), Carcinomas and EMT

Couchman

2021

IJMS

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Cell surface proteoglycans are known to be important regulators of many aspects of cell behavior. The principle family of transmembrane proteoglycans is the syndecans, of which there are four in mammals. Syndecan-1 is mostly restricted to epithelia, and bears heparan sulfate chains that are capable of interacting with a large array of polypeptides, including extracellular matrix components and potent mediators of proliferation, adhesion and migration. For this reason, it has been studied extensively with respect to carcinomas and tumor progression. Frequently, but not always, syndecan-1 levels decrease as tumor grade, stage and invasiveness and dedifferentiation increase. This parallels experiments that show depletion of syndecan-1 can be accompanied by loss of cadherin-mediated adhesion. However, in some tumors, levels of syndecan-1 increase, but the characterization of its distribution is relevant. There can be loss of membrane staining, but acquisition of cytoplasmic and/or nuclear staining that is abnormal. Moreover, the appearance of syndecan-1 in the tumor stroma, either associated with its cellular component or the collagenous matrix, is nearly always a sign of poor prognosis. Given its relevance to myeloma progression, syndecan-1-directed antibody—toxin conjugates are being tested in clinical and preclinical trials, and may have future relevance to some carcinomas.

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The cell surface proteoglycan from mouse mammary epithelial cells bears chondroitin sulfate and heparan sulfate glycosaminoglycans.

Cited by 263 publications

References 35 publications

Metabolic Glycoengineering in hMSC-TERT as a Model for Skeletal Precursors by Using Modified Azide/Alkyne Monosaccharides

Metabolic Glycoengineering in hMSC-TERT as a Model for Skeletal Precursors by Using Modified Azide/Alkyne Monosaccharides

The Mutual Impact of Syndecan-1 and Its Glycosaminoglycan Chains—A Multivariable Puzzle

Syndecan-1 (CD138), Carcinomas and EMT

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