Occurrence of O‐linked Xyl‐GlcNAc and Xyl‐Glc disaccharides in trocarin, a factor Xa homolog from snake venom

  title={Occurrence of O‐linked Xyl‐GlcNAc and Xyl‐Glc disaccharides in trocarin, a factor Xa homolog from snake venom},
  author={J. Joseph and M. Valiyaveettil and D. Gowda and R. Kini},
  journal={Journal of Thrombosis and Haemostasis},
Summary.  Trocarin is a 46515‐Da group D prothrombin‐activating glycoprotein from the venom of the Australian elapid, Tropidechis carinatus. Amino acid sequencing and functional characterization of trocarin demonstrated that it is a structural and functional homolog of mammalian blood coagulation factor (F)Xa. In this study we show that, in contrast to mammalian Xa, which is not glycosylated, trocarin contains an O‐linked carbohydrate moiety in its light chain and an N‐linked carbohydrate… Expand
Glycan structures and intrageneric variations of venom acidic phospholipases A2 from Tropidolaemus pitvipers
This is the first glycan structure of the snake venom PLA2 to be solved, and the enzymatic removal of glycans from both PLA2s did not significantly alter their effects on lipid hydrolysis and platelet aggregation. Expand
Terminal disialylated multiantennary complex-type N-glycans carried on acutobin define the glycosylation characteristics of the Deinagkistrodon acutus venom.
Glycosylation analysis of nonmammalian sources often springs surprises and conjures up intriguing views of evolutionary adaptation. Many of the constituents of snake venoms are known to beExpand
Group D prothrombin activators from snake venom are structural homologues of mammalian blood coagulation factor Xa.
The purification of Group D prothrombin activators from three Australian snake venoms using a single-step method and their N-terminal sequences reveal that hopsarin D is structurally and functionally similar to mammalian coagulation FXa. Expand
Structures of N-Glycans of Bothrops Venoms Revealed as Molecular Signatures that Contribute to Venom Phenotype in Viperid Snakes *
For the first time a comprehensive set of N-glycan structures present in snake venoms are defined and mirror the phylogeny cladograms of South American bothropoid snakes reported in studies on morphological, molecular data and feeding habits, exhibiting distinct molecular signatures for each venom. Expand
Molecular Diversity in Venom from the Australian Brown Snake, Pseudonaja textilis*S
Most of the venom proteins including proteins previously not known to be present in the venom are identified, including procoagulant and plasmin inhibitor, currently in development as human therapeutic agents. Expand
Comparative analysis of prothrombin activators from the venom of Australian elapids.
The molecular phylogenetic analysis described here represents a new approach for distinguishing group C and D snake prothrombin activators and correlates well with previous classifications. Expand
The intriguing world of prothrombin activators from snake venom.
  • R. Kini
  • Biology, Medicine
  • Toxicon : official journal of the International Society on Toxinology
  • 2005
This review provides a detailed description of the current knowledge on all prothrombin activators and highlights several intriguing questions that are yet to be answered. Expand
Identification and comparative analysis of novel factors from the venom gland of the coastal taipan (Oxyuranus scutellatus) and related species
This thesis describes the cloning, characterisation and comparative analysis of a number of unique toxins from the venom gland of the coastal taipan and a total of seven other related Australian snakes, representing the most detailed and comprehensive description to date of the cloning and characterisation of different genes associated with envenomation from Australian snakes. Expand
The structural characteristics and evolution of the venom prothrombin activators and blood coagulation factors from Australian elapids are discussed, which show that these snakes possess two parallel prothROMbin activating systems, one in their venom and the other in their blood. Expand


Glycan‐dependent signaling: O‐linked N‐acetylglucosamine
  • J. Hanover
  • Biology, Medicine
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2001
The addition of O‐linked N‐acetylglucosamine to target proteins may serve as a signaling modification analogous to protein phosphor‐ylation, and the glycan modification is likely to perform similar signaling functions in mammalian cells. Expand
Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and aXyl-GlC-Ser structure in the first epidermal growth factor-like domains of human factors VIII and IX and protein Z in addition to that of bovines protein Z. Expand
The subcellular distribution of terminal N-acetylglucosamine moieties. Localization of a novel protein-saccharide linkage, O-linked GlcNAc.
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  • Medicine, Chemistry
  • The Journal of biological chemistry
  • 1986
The distribution of O-linked GlcNAc in highly enriched rat liver subcellular organelles is reported and evidence that terminal Glc NAc transferases are localized to the Golgi complex suggests that glycosylation with O-linkages to protein is not an exclusive marker for a particular organelle. Expand
Amino acid sequence of trocarin, a prothrombin activator from Tropidechis carinatus venom: its structural similarity to coagulation factor Xa.
Among snake venom procoagulant proteins, group II prothrombin activators are functionally similar to blood coagulation factor Xa, and trocarin is the first true structural homologue of a coagulations factor. Expand
Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X.
It appears that carbohydrate residues in factor X play an important role in the activation of the zymogen. Expand
Influence of the carbohydrate moiety on the stability of glycoproteins.
The hypothesis that the general function of protein glycosylation is to aid in folding of the nascent polypeptide chain and in stabilization of the conformation of the mature glycoprotein is supported. Expand
Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine.
The results indicate that the carbohydrate moiety O-glycosidically linked to serine 52 does not appear to be involved either in the interaction of factor VIIa with tissue factor, or the expression of its proteolytic activity toward factor X or factor IX following complex formation with tissue factors. Expand
A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z.
The presence of the unique trisaccharide structure in factors VII, IX and protein Z leads us to anticipate its biological role in the tissue factor pathway. Expand
Effect of the carbohydrate moiety on the secondary structure of beta 2-glycoprotein. I. Implications for the biosynthesis and folding of glycoproteins.
Findings which are in agreement with earlier reports suggest that the carbohydrate moiety of beta 2I possesses more bi- than tri-antennas, probably three of the former and two of the latter carbohydrate units. Expand
Erythrocytes contain cytoplasmic glycoproteins. O-linked GlcNAc on Band 4.1.
Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces ofExpand