A tryptophan-substituted member of the AKH/RPCH family isolated from a stick insect corpus cardiacum

GÄde, Gerd; Kellner, Roland; Rinehart, Kenneth L.; Proefke, Mark L.

doi:10.1016/0006-291x(92)90215-7

Cited by 54 publications

(36 citation statements)

References 18 publications

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“…The site of attachment was not established, but it was thought likely to be the indolic N atom (Gade et al, 1992). From our results it is clear that in RNase Us the hexose is linked to the C2 position, and it will be of interest to establish whether the same is true for the insect neuropeptide.…”

Section: Discussionmentioning

confidence: 77%

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

Hofsteenge¹,

Müller²,

Beer³

et al. 1994

Biochemistry

270

234

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We report a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue. An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us. Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan. The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety. 'H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole. This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N-or 0-glycosidic bonds.

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Section: Discussionmentioning

confidence: 77%

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

Hofsteenge¹,

Müller²,

Beer³

et al. 1994

Biochemistry

270

234

View full text Add to dashboard Cite

show abstract

“…In addition, it seems probable also that a neuropeptide from Carausius morosus is C-glycosylated (29).…”

Section: Resultsmentioning

confidence: 99%

“…Urokinase-type plasminogen activator is mitogenic for a number of cells in culture, and this activity depends on its EGF-like domain that carries a fucosyl residue on Thr 18 . The defucosylated domain binds as tightly to cells as the fucosy- b Gäde et al (29) hypothesize that the unknown hexose is attached to N1 of the indole.…”

Section: Discussionmentioning

confidence: 99%

C-Mannosylation and O-Fucosylation of Thrombospondin Type 1 Repeats

Peredo

Klein

Maček

et al. 2002

Molecular & Cellular Proteomics

110

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The final chemical structure of a newly synthesized protein is often only attained after further covalent modification. Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods. Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation. Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin. Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated. O-Fucosylation sites were determined by a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach. Four of five TSRs carry the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites. In analogy to thrombospondin-1, we assume this to be Glc-Fuc-O-Ser/Thr. Our current knowledge of these glycosylations will be discussed.

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“…C6, C7, C8␣, C8␤, C9, and properdin, are C-mannosylated on multiple Trp residues (21,22). This form of protein glycosylation appears to be widespread in biology, since the C-mannosyltransferase activity has been found in mammals, birds, amphibians, and fish (23,24), and tryptophan hexosylation has been found in insect cells (25).…”

Section: Thrombospondin (Tsp)mentioning

confidence: 99%

C-Mannosylation and O-Fucosylation of the Thrombospondin Type 1 Module

Hofsteenge

Huwiler

Maček

et al. 2001

Journal of Biological Chemistry

233

228

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Thrombospondin-1 (TSP-1) is a multidomain protein that has been implicated in cell adhesion, motility, and growth. Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of ϳ60 amino acids in length with conserved Cys and Trp residues. The Trp residues occur in WXXW patterns, which are the recognition motifs for protein C-mannosylation. This modification involves the attachment of an ␣-mannosyl residue to the C-2 atom of the first tryptophan. Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated. Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction. In the course of these studies it was appreciated that the TSRs in TSP-1 undergo a second form of unusual glycosylation. By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr. This is the first protein in which such a disaccharide has been identified, although protein O-fucosylation is well described in epidermal growth factor-like modules. Both C-and O-glycosylations take place on residues that have been implicated in the interaction of TSP-1 with glycosaminoglycans or other cellular receptors.

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A tryptophan-substituted member of the AKH/RPCH family isolated from a stick insect corpus cardiacum

Cited by 54 publications

References 18 publications

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us

C-Mannosylation and O-Fucosylation of Thrombospondin Type 1 Repeats

C-Mannosylation and O-Fucosylation of the Thrombospondin Type 1 Module

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