Identification of a Drosophila Vitamin K-dependent γ-Glutamyl Carboxylase

Li, Tao; Yang, Chao; Jin, Da-Yun; Stafford, Darrel W.

doi:10.1074/jbc.m001790200

Cited by 52 publications

(51 citation statements)

References 21 publications

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“…The organization of the N terminus propeptide is unique to these proteases, composed of a ␥-carboxylation (Gla) domain followed by two EGF or kringle domains. Although Gla, EGF, and SP modules exist in invertebrates such as Drosophila melanogaster, there is no evidence for this unique domain organization (28). Likewise, serine proteases responsible for hemolymph coagulation in Tachypleus tridentatus (Japanese horseshoe crab) and other invertebrates species differ significantly in N terminus domain content and organization from mammalian coagulation proteases (29)(30)(31).…”

Section: Discussionmentioning

confidence: 97%

Demonstration of the extrinsic coagulation pathway in teleostei: Identification of zebrafish coagulation factor VII

Sheehan

Templer

Gregory

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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It is not known whether the mammalian mechanism of coagulation initiation is conserved in fish. Identification of factor VII is critical in providing evidence for such a mechanism. A cDNA was cloned from a zebrafish (teleost) library that predicted a protein with sequence similarity to human factor VII. Factor VII was shown to be present in zebrafish blood and liver by Western blot analysis and immunohistochemistry. Immunodepletion of factor VII from zebrafish plasma selectively inhibited thromboplastin-triggered thrombin generation. Heterologous expression of zebrafish factor VII demonstrated a secreted protein (50 kDa) that reconstituted thromboplastin-triggered thrombin generation in immunodepleted zebrafish plasma. These results suggest conservation of the extrinsic coagulation pathway between zebrafish and humans and add credence to the zebrafish as a model for mammalian hemostasis. The structure of zebrafish factor VIIa predicted by homology modeling was consistent with the overall three-dimensional structure of human factor VIIa. However, amino acid disparities were found in the epidermal growth factor-2͞serine protease regions that are present in the human tissue factor-factor VIIa contact surface, suggesting a structural basis for the species specificity of this interaction. In addition, zebrafish factor VII demonstrates that the Gla-EGF-EGF-SP domain structure, which is common to coagulation factors VII, IX, X, and protein C, was present before the radiation of the teleosts from the tetrapods. Identification of zebrafish factor VII significantly narrows the evolutionary window for development of the vertebrate coagulation cascade and provides insight into the structural basis for species specificity in the tissue factor-factor VIIa interaction.

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Section: Discussionmentioning

confidence: 97%

Demonstration of the extrinsic coagulation pathway in teleostei: Identification of zebrafish coagulation factor VII

Sheehan

Templer

Gregory

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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“…These peptides, however, exhibit no discernible sequence similarity to the Gla domains found in vertebrates. Moreover, sequence paralogs of vertebrate Gla domains do not appear to be present in the Drosophila genome (20). Although Gla-containing polypeptides are thus likely to be ubiquitous among metazoans, the Gla domain, with its canonical fingerprint of Gla residues and characteristic phosphatidylserine-binding properties, has been definitively identified only in vertebrate species.…”

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confidence: 99%

“…Gene and cDNA sequences that encode GGC orthologs have been identified in diverse protostomes, including cone snails of the genus Conus (19) and arthropods, such as Drosophila melanogaster (20). A variety of Gla-containing neuroactive peptides have been isolated from cone snail venom (ref.…”

mentioning

confidence: 99%

Vitamin K-dependent proteins in Ciona intestinalis , a basal chordate lacking a blood coagulation cascade

Kulman

Harris

Nakazawa

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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We have isolated and sequenced several cDNAs derived from the sea squirt Ciona intestinalis that encode vitamin K-dependent proteins. Four of these encode ␥-carboxyglutamic acid (Gla) domain-containing proteins, which we have named Ci-Gla1 through Ci-Gla4. Two additional cDNAs encode the apparent orthologs of ␥-glutamyl carboxylase and vitamin K epoxide reductase. Ci-Gla1 undergoes ␥-glutamyl carboxylation when expressed in CHO cells and is homologous to Gla-RTK, a putative receptor tyrosine kinase previously identified in a related ascidian. The remaining three Gla domain proteins are similar to proteins that participate in fundamental developmental processes, complement regulation, and blood coagulation. These proteins are generally expressed at low levels throughout development and exhibit either relatively constant expression (Ci-Gla1, ␥-glutamyl carboxylase, and vitamin K epoxide reductase) or spatiotemporal regulation (Ci-Gla2, -3, and -4). These results demonstrate the evolutionary emergence of the vitamin K-dependent Gla domain before the divergence of vertebrates and urochordates and suggest novel functions for Gla domain proteins distinct from their roles in vertebrate hemostasis. In addition, these findings highlight the usefulness of C. intestinalis as a model organism for investigating vitamin K-dependent physiological phenomena, which may be conserved among the chordate subphyla.ascidian ͉ ␥-carboxyglutamic acid ͉ urochordate ͉ warfarin

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“…Despite being short, this region contains important MGP-conserved features like the invariant cysteine residues involved in intramolecular disulfide bridge and 3 Glu residues shown to be ␥-carboxylated in vertebrates. A vitamin K-dependent ␥-glutamyl carboxylase has also been described in D. melanogaster (51) suggesting that Glu residues present within the pseudo-Gla domain of Msp-300 could be ␥-carboxylated and play a role in calcium binding. Despite similarities in both sequence and tissue distribution (i.e.…”

Section: Discussionmentioning

confidence: 99%

Evolution of Matrix and Bone γ-Carboxyglutamic Acid Proteins in Vertebrates

Laizé

Martel

Viegas

et al. 2005

Journal of Biological Chemistry

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The evolution of calcified tissues is a defining feature in vertebrate evolution. Investigating the evolution of proteins involved in tissue calcification should help elucidate how calcified tissues have evolved. The purpose of this study was to collect and compare sequences of matrix and bone ␥-carboxyglutamic acid proteins (MGP and BGP, respectively) to identify common features and determine the evolutionary relationship between MGP and BGP. Thirteen cDNAs and genes were cloned using standard methods or reconstructed through the use of comparative genomics and data mining. These sequences were compared with available annotated sequences (a total of 48 complete or nearly complete sequences, 28 BGPs and 20 MGPs) have been identified across 32 different species (representing most classes of vertebrates), and evolutionarily conserved features in both MGP and BGP were analyzed using bioinformatic tools and the Tree-Puzzle software. We propose that: 1) MGP and BGP genes originated from two genome duplications that occurred around 500 and 400 million years ago before jawless and jawed fish evolved, respectively; 2) MGP appeared first concomitantly with the emergence of cartilaginous structures, and BGP appeared thereafter along with bony structures; and 3) BGP derives from MGP. We also propose a highly specific pattern definition for the Gla domain of BGP and MGP.

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Identification of a Drosophila Vitamin K-dependent γ-Glutamyl Carboxylase

Cited by 52 publications

References 21 publications

Demonstration of the extrinsic coagulation pathway in teleostei: Identification of zebrafish coagulation factor VII

Demonstration of the extrinsic coagulation pathway in teleostei: Identification of zebrafish coagulation factor VII

Vitamin K-dependent proteins in Ciona intestinalis , a basal chordate lacking a blood coagulation cascade

Evolution of Matrix and Bone γ-Carboxyglutamic Acid Proteins in Vertebrates

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