Analysis of sulfatide from rat cerebellum and multiple sclerosis white matter by negative ion electrospray mass spectrometry

Marbois, Beth N.; Faull, Kym F.; Fluharty, Arvan L.; Raval-Fernandes, Sujna; Rome, Leonard H.

doi:10.1016/s1388-1981(99)00201-2

Cited by 61 publications

(72 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, as Table 1 shows, there is one more possible molecular species in m/z 1572 of GM1; whether m/z 1572 originates from d20:1/18:0 or d18:1/20:0 could not be determined merely by mass spectra. While m/z 1572 in this case is already known to be d20:1/18:0 from the previous reports [57,58], molecular identification of the corresponding mass spectra in unknown samples would require more detailed MS/MS and MS/MS/MS analyses in practice.…”

Section: The Detection Of Gm1 By Tlc-blot-maldi-qit-tof Msmentioning

confidence: 85%

“…Many studies have shown the complexity of the ceramide moiety of GSLs. A previous report showed that bovine brain GM1 contains equal amounts of two major bases, sphingenine (d18:1) and eicosasphingenine (d20:1), and other bases at less than 5% [57,58]. Carbohydrate sequences of bovine brain GM1 and its major ceramide molecular species are shown in Fig.…”

Section: The Detection Of Gm1 By Tlc-blot-maldi-qit-tof Msmentioning

confidence: 99%

See 1 more Smart Citation

High-sensitivity analysis of glycosphingolipids by matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight imaging mass spectrometry on transfer membranes

Goto‐Inoue

Hayasaka

Sugiura

et al. 2008

Journal of Chromatography B

View full text Add to dashboard Cite

Glycosphingolipids are ubiquitous constituents of cells. Yet there is still room for improvement in the techniques for analyzing glycosphingolipids. Here we report our highly sensitive and convenient analytical technology with imaging mass spectrometry for detailed structural analysis of glycosphingolipids. We were able to determine detailed ceramide structures; i.e. both the sphingosine base and fatty acid, by MS/MS/MS analysis on a PVDF membrane with 10 pmol of GM1, with which only faint bands were visible by primuline staining. The limit of detection was approximately 1 pmol of GM1, which is lower than the value in the conventional reports. (10 pmol)

show abstract

Section: The Detection Of Gm1 By Tlc-blot-maldi-qit-tof Msmentioning

confidence: 85%

Section: The Detection Of Gm1 By Tlc-blot-maldi-qit-tof Msmentioning

confidence: 99%

High-sensitivity analysis of glycosphingolipids by matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight imaging mass spectrometry on transfer membranes

Goto‐Inoue

Hayasaka

Sugiura

et al. 2008

Journal of Chromatography B

View full text Add to dashboard Cite

show abstract

“…5D). The binding sites on CTX A3 for the SGC headgroup and for heparin partially overlap, and Lys 35 is responsible for interacting with the sulfate moiety in both SGC (Fig. 10A) and heparin (40).…”

Section: Discussionmentioning

confidence: 99%

“…11C) (22), the SGC can function as a glue to effect tighter binding between monomers in the CTX A3 dimeric complex. For instance, in the presence of SGC, the dimer gains a pair of intermolecular hydrogen bonds from the side chain nitrogen of Lys 35 and the backbone oxygen of Lys 44 ( Fig. 10B), which is not observed in the CTX A3⅐SDS complex.…”

Section: Sgc-facilitated Ctx Internalization Occurs After Ctx Pore Fomentioning

confidence: 98%

See 1 more Smart Citation

Glycosphingolipid-facilitated Membrane Insertion and Internalization of Cobra Cardiotoxin

Wang

Liu

Lee

et al. 2006

Journal of Biological Chemistry

View full text Add to dashboard Cite

Cobra cardiotoxins, a family of basic polypeptides having lipidand heparin-binding capacities similar to the cell-penetrating peptides, induce severe tissue necrosis and systolic heart arrest in snakebite victims. Whereas cardiotoxins are specifically retained on the cell surface via heparan sulfate-mediated processes, their lipid binding ability appears to be responsible, at least in part, for cardiotoxin-induced membrane leakage and cell death. Although the exact role of lipids involved in toxin-mediated cytotoxicity remains largely unknown, monoclonal anti-sulfatide antibody O4 has recently been shown to inhibit the action of CTX A3, the major cardiotoxin from Taiwan cobra venom, on cardiomyocytes by preventing cardiotoxin-induced membrane leakage and CTX A3 internalization into mitochondria. Here, we show that anti-sulfatide acts by blocking the binding of CTX A3 to the sulfatides in the plasma membrane to prevent sulfatide-dependent CTX A3 membrane pore formation and internalization. We also describe the crystal structure of a CTX A3-sulfatide complex in a membrane-like environment at 2.3 Å resolution. The unexpected orientation of the sulfatide fatty chains in the structure allows prediction of the mode of toxin insertion into the plasma membrane. CTX A3 recognizes both the headgroup and the ceramide interfacial region of sulfatide to induce a lipid conformational change that may play a key role in CTX A3 oligomerization and cellular internalization. This proposed lipid-mediated toxin translocation mechanism may also shed light on the cellular uptake mechanism of the amphiphilic cell-penetrating peptides known to involve multiple internalization pathways.Glycosphingolipids in eukaryotic cells have important biological functions in membrane trafficking and cell signaling (1, 2). The number of disease-related proteins found to interact specifically with glycosphingolipids is also increasing (3-5). For instance, recent studies have shown that natural killer cells can be activated by glycosylceramides from the cell surface of Gram-negative bacteria that do not contain lipopolysaccharide (6, 7). There is also evidence indicating that, in response to tumor necrosis factor-␣, trafficking of ganglioside GD3 from the plasma membrane to mitochondria can trigger several cell death signaling responses (3,8,9). Although the molecular mechanisms accounting for the observed glycosphingolipid transport and glycolipidtriggered cell responses remain elusive, recent progress in determining the three-dimensional structure of protein⅐glycosphingolipid complexes has shed some light on the process (10 -13). These glycosphingolipid-binding proteins function by either extracting lipids from the membrane and forming a water-soluble protein⅐lipid complex, as in the cases of glycosphingolipid transfer protein, saposin B, and lipid-presenting CD1a (10 -12), or by localizing to a glycosphingolipid domain of the plasma membrane and eventually being internalized via the endocytic pathway, as seen for cholera and Shiga toxins (13,14). Aft...

show abstract

Cerebroside sulfate activator protein (Saposin B): chromatographic and electrospray mass spectrometric properties

Faull¹,

Whitelegge²,

Higginson³

et al. 1999

J. Mass Spectrom.

Self Cite

View full text Add to dashboard Cite

Analysis of sulfatide from rat cerebellum and multiple sclerosis white matter by negative ion electrospray mass spectrometry

Cited by 61 publications

References 25 publications

High-sensitivity analysis of glycosphingolipids by matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight imaging mass spectrometry on transfer membranes

High-sensitivity analysis of glycosphingolipids by matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight imaging mass spectrometry on transfer membranes

Glycosphingolipid-facilitated Membrane Insertion and Internalization of Cobra Cardiotoxin

Cerebroside sulfate activator protein (Saposin B): chromatographic and electrospray mass spectrometric properties

Contact Info

Product

Resources

About