cDNA Sequences for Four Snake Venom Metalloproteinases: Structure, Classification, and Their Relationship to Mammalian Reproductive Proteins

Hite, L A; Jia, Li-Guo; Bjarnason, Jón B.; Fox, Jay W.

doi:10.1006/abbi.1994.1026

Cited by 226 publications

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“…To date over a hundreds SVMPs have been reported, and classified into the following four classes according to the domain structure/molecular size: P-I, composed of only metalloproteinase domain/20-30 kDa; P-II, containing metalloproteinase and disintegrin domains/30-50 kDa; P-III, consisting of metalloproteinase, disintegrin-like and Cys-rich/50-80 kDa; and P-IV, containing an additional C-type lectin sequence at the C-terminal of P-III/80-100 kDa (Hite et al, 1994;Kini and Evans, 1992). All the metalloproteinases have zinc-binding sites (HExGHxxGxxH), and cysteine residue in prodomain chelates to zinc in the latent form.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

et al. 2006

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-During the characterization of hemorrhagic factor in venom of Rhabdophis tigrinus tigrinus, so-called Yamakagashi in Japan, one of the Colubridae family, a novel metalloproteinase with molecular weight of 38 kDa in the Duvernoy's gland of Yamakagashi was identified by gelatin zymography and by monitoring its proteolytic activity using a fluorescence peptide substrate, MOCAc-PLGLA 2 pr(Dnp)AR-NH 2 , which was developed for measuring the well-known matrix metalloproteinase (MMP) activity.After purification by gel filtration HPLC and/or column switch HPLC system consisting of an affinity column, which was immobilized with a synthetic BS-10 peptide (MQKPRCGVPD) originating from propeptide domain of MMP-7 and a reversed-phase column, the N-terminal amino acid sequence of the 38 kDa metalloproteinase was identified as FNTFPGDLK which shared a high homology to Xenopus MMP-9.The 38 kDa metalloproteinase required Zn 2+ and Ca 2+ ions for its proteolytic activity. In addition, the proteolytic activity was almost completely inhibited by BS-10, a MMP inhibitor, but not by the serine proteinase inhibitors, cysteine proteinase inhibitors and aspartic proteinase inhibitors.Together these results demonstrated that the 38 kDa proteinase is a novel snake verom metalloproteinase (SVMP) containing HExGHxxGxxH motif which possesses high affinity to the BS-10 peptide, into its molecule, and the enzymatic properties are closed to that of MMPs.Based on the results obtained in the present study, we concluded that the 38 kDa metalloproteinase is a novel metalloproteinase whose activity may be regulated by the cysteine switch mechanism, and could be classified as one of the matrix metalloproteinases rather than snake venom metalloproteinases.

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Section: Introductionmentioning

confidence: 99%

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

et al. 2006

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“…In their venom glands, snakes of the family Crotalidae (adders) produce extremely aggressive proteolytic enzymes, which can cause hemorrhage and tissue necrosis (see reviews by Bjarnason Takeya et al, 1990;Hite et al, 1992Hite et al, , 1994Kini & Evans, 1992). These toxins have been named adamalysins after adamalysin 11, an enzyme from the rattlesnake Crotalus adamanteus (Gomis-Ruth et al, 1993a.…”

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confidence: 99%

The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

et al. 1995

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The three-dimensional structures of the zinc endopeptidases human neutrophil collagenase, adamalysin I1 from rattle snake venom, alkaline proteinase from Pseudomonas aeruginosa, and astacin from crayfish are topologically similar, with respect to a five-stranded 0-sheet and three a-helices arranged in typical sequential order. The four proteins exhibit the characteristic consensus motif HEXXHXXGXXH, whose three histidine residues are involved in binding of the catalytically essential zinc ion. Moreover, they all share a conserved methionine residue beneath the active site metal as part of a superimposable "Met-turn.'' This structural relationship is supported by a sequence alignment performed on the basis of topological equivalence showing faint but distinct sequential similarity. The alkaline proteinase is about equally distant (26% sequence identity) to both human neutrophil collagenase and astacin and a little further away from adamalysin I1 (17% identity). The pairs astacin/adamalysin 11, astacidhuman neutrophil collagenase, and adamalysin Whuman neutrophil collagenase exhibit sequence identities of 16%, 14%, and 13%, respectively. Therefore, the corresponding four distinct families of zinc peptidases, the astacins, the matrix metalloproteinases (matrixins, collagenases), the adamalysins/reprolysins (snake venom proteinases/reproductive tract proteins), and the serralysins (large bacterial proteases from Serratia, Erwinia, and Pseudomonas) appear to have originated by divergent evolution from a common ancestor and form a superfamily of proteolytic enzymes for which the designation "metzincins" has been proposed. There is also a faint but significant structural relationship of the metzincins to the thermolysin-like enzymes, which share the truncated zincbinding motif HEXXH and, moreover, similar topologies in their N-terminal domains.Keywords: crystal structure; metalloproteinase; molecular evolution; protein family; sequence alignment; topology is involved in metal binding (McKerrow, 1987;

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“…In turn, SVMP are part of the "metzincin" family of zinc-dependent metalloproteinases, together with matrix metalloproteinases (MMP), astacins, and serralysins, all of them exhibiting an identical zinc-dependent motif, with the sequence HEXXHXXGXXH and the presence of a methionine turn . SVMP can be divided into four classes depending on their domain organization (Hite et al 1994): P-I, comprising only the metalloproteinase domain; P-II, having a metalloproteinase domain followed by a disintegrin-like domain; P-III, comprising metalloproteinase, disintegrin-like and cysteine-rich domains, and P-IV, containing additionally a lectin-like domain linked by disulfide bonds. The disintegrin-like domain shows high sequence identity with venom disintegrins (Markland 1998), which are proteolytically released from P-II precursors.…”

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“…The disintegrin-like domain shows high sequence identity with venom disintegrins (Markland 1998), which are proteolytically released from P-II precursors. However, the disintegrin-like domain does not contain the typical RGD sequence found in disintegrins, showing different sequences in this region (Paine et al 1992, Hite et al 1994. All these metalloproteinases are synthesized as zymogens, and are proteolytically processed to yield the active enzyme .…”

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confidence: 99%

“…The role of the others domains in the toxicity of high molecular weight enzymes is not clear, although it has been shown that large hemorrhagic metalloproteinases having disintegrinlike and high-cysteine domains, are more active at inducing hemorrhage than enzymes comprising only the metalloproteinase domain , Hite et al 1994. Interestingly, there are metalloproteinases in snake venoms which are devoid of hemorrhagic activity (Willis & Tu 1988, Markland 1998.…”

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Inflammatory effects of snake venom metalloproteinases

Teixeira

Fernandes

Zuliani

et al. 2005

Mem. Inst. Oswaldo Cruz

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cDNA Sequences for Four Snake Venom Metalloproteinases: Structure, Classification, and Their Relationship to Mammalian Reproductive Proteins

Cited by 226 publications

References 0 publications

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

Inflammatory effects of snake venom metalloproteinases

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