Hemorrhagic metalloproteinases from snake venoms

Bjarnason, Jón B.; Fox, Jay W.

doi:10.1016/0163-7258(94)90049-3

Cited by 549 publications

(320 citation statements)

References 147 publications

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“…A low-molecular weight hemorrhagic toxin has been isolated from ACL venom, ACL hemorrhagic toxin I, but it is not responsible for all of the hemorrhagic activity as the crude venom demonstrated more activity than the purified hemorrhagic toxin alone (Johnson and Ownby, 1993b). The presence of more high-molecular weight hemorrhagic toxins in the CVV venom may account for the results of the present experiment, as the higher molecular weight hemorrhagic toxins are generally more potent (Bjarnason and Fox, 1994). The results of the hemorrhage assays in this experiment are consistent with Ownby et al (1988), who reported massive hemorrhage as a result of CVV envenomation.…”

Section: Intramuscularsupporting

confidence: 91%

Neutralization of edema, hemorrhage and myonecrosis induced by North American crotalid venoms in simulated first-aid treatments

Evans

Ownby

1999

Toxicon

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Section: Intramuscularsupporting

confidence: 91%

Neutralization of edema, hemorrhage and myonecrosis induced by North American crotalid venoms in simulated first-aid treatments

Evans

Ownby

1999

Toxicon

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“…Viper venoms have now been shown to contain at least four classes of proteins involved in this process. These include C-lectin-like proteins, venom metalloproteinases (reprolysins) that may or may not include a disintegrin domain (28), and monomeric and dimeric disintegrins. Monomeric disintegrins potently inhibit ␤3-containing integrins, including the platelet integrin ␣IIb␤3 (10,11), and by interfering with platelet aggregation, result in extensive tissue hemorrhage at the site of viper bites.…”

Section: Fig 11mentioning

confidence: 99%

Inhibitory Effects of MLDG-containing Heterodimeric Disintegrins Reveal Distinct Structural Requirements for Interaction of the Integrin α9β1 with VCAM-1, Tenascin-C, and Osteopontin

Marcinkiewicz

Taooka

Yokosaki³

et al. 2000

Journal of Biological Chemistry

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The integrin ␣9␤1 is expressed on epithelial cells, smooth muscle cells, skeletal muscle, and neutrophils and recognizes at least three distinct ligands: vascular cell adhesion molecule 1 (VCAM-1), tenascin-C, and osteopontin. The ␣9 subunit is structurally similar to the integrin ␣4 subunit, and ␣9␤1 and ␣4␤1 both recognize VCAM-1 as a ligand. We therefore examined whether the disintegrin EC3, which we have recently shown specifically inhibits the binding of ␣4 integrins to ligands, would also be a functional inhibitor of ␣9␤1. EC3 and a novel heterodimeric disintegrin that we identified, EC6, both were potent inhibitors of ␣9␤1-mediated adhesion to VCAM-1 and of neutrophil migration across tumor necrosis factor-activated endothelial cells. A peptide containing a novel MLDG motif shared by both of these disintegrins also inhibited ␣9␤1-and ␣4␤1-mediated adhesion to VCAM-1. Surprisingly though, concentrations of EC3 that completely inhibited adhesion of ␣9-transfected cells to VCAM-1 had little or no effect on adhesion to either of the other ␣9␤1 ligands, osteopontin and tenascin-C. Furthermore, peptides AEIDGIEL and SV-VYGLR, which we have previously shown inhibit binding of ␣9␤1-expressing cells to tenascin-C and osteopontin, respectively, had no effect on adhesion to VCAM-1. These data suggest that there are structurally distinct requirements for interactions of the ␣9␤1 integrin with VCAM-1 and the extracellular matrix ligands osteopontin and tenascin-C.The integrin ␣9 subunit forms a single known heterodimer, ␣9␤1, that is widely expressed in epithelia and smooth and skeletal muscle and on neutrophils (1, 2). We and others have identified three distinct ligands for ␣9␤1: the extracellular matrix proteins tenascin-C (3) and osteopontin (4 -6) and the inducible endothelial immunoglobulin family member, VCAM-1 1 (1). We have mapped the ligand-binding site in tenascin-C to an exposed peptide loop in the third fibronectin type III repeat containing the sequence AEIDGIEL (7). We have also mapped the ␣9␤1 ligand-binding site in osteopontin (6). Although an initial report suggested that ␣9␤1 might bind to an RGD-containing sequence in osteopontin (5), we were able to demonstrate by extensive mutagenesis that the binding site is within the linear peptide sequence SVVYGLR immediately adjacent to the RGD site (6).Structurally, the ␣9 subunit is closely related to the ␣4 subunit, and on the basis of sequence homology ␣4 and ␣9 appear to be the only known members of a subfamily of integrin ␣ subunits that lack both an insertional domain and an extracellular disulfide-linked cleavage site (2). Furthermore, both subunits are expressed on leukocytes and mediate leukocyte migration (1, 8). Finally, both integrins recognize VCAM-1 as a ligand (1, 9). We have shown that both ␣4␤1 and ␣9␤1 contribute to the chemotactic migration of human neutrophils across endothelial cell monolayers activated by tumor necrosis factor-␣ (TNF␣), an effect that is due at least in part to interaction of these integrins with VCAM-1 induced in resp...

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“…Metallo-collagenases, first discovered in tadpole tissue explants (Gross and Lapiere, 1962), are zinc-containing enzymes that also generally require calcium for their optimum activity and stability, and cleave the collagen helix at a specific locus under physiological conditions (Gawston and Murphy, 1981;Harris and Vater, 1982;Sellers and Murphy, 1981;Stricklin et al, 1977). These enzymes have been widely studied from various mammalian tissues (Harris and Vater, 1982;Sellers and Murphy, 1981) as well as from bacteria, such as Bacillus cereus (Makinen and Makinen, 1987), Clostridium histolyticum (Bond and Van Wart, 1984a, b;Peterkofsky, 1982), Achromobacter (Nguyen et al, 1988), Vibrio alginolyticus (Takeuchi et al, 1992) and Clostridium perfringens (Matsuhita et al, 1994), and snake venom (Bjarnason and Fox, 1994). These metallo-collagenases, extracellular enzymes, are involved in remodeling the extracellular matrix.…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of a Collagenolytic Protease from the Filefish, Novoden modestrus

Kim¹,

Park²,

Kim³

et al. 2002

BMB Reports

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A serine collagenolytic protease was purified from the internal organs of filefish, Novoden modestrus, by ammonium sulfate, ion-exchange chromatography on a DEAE-Sephadex A-50, ion-exchange rechromatography on a DEAE-Sephadex A-50, and gel filtration on a Sephadex G-150 column. The molecular mass of the filefish serine collagenase was estimated to be 27.0 kDa by gel filtration and SDS-PAGE. The purified collagenase was optimally active at pH 7.0-8.0 and 55 o C. The purified enzyme was rich in Ala, Ser, Leu, and Ile, but poor in Trp, Pro, Tyr, and Met. In addition, the purified collagenolytic enzyme was strongly inhibited by N-P-toluenesulfonyl-L-lysine chloromethyl ketone (TLCK), diisopropylfluorophosphate (DFP), and soybean trypsin inhibitor.

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Hemorrhagic metalloproteinases from snake venoms

Cited by 549 publications

References 147 publications

Neutralization of edema, hemorrhage and myonecrosis induced by North American crotalid venoms in simulated first-aid treatments

Neutralization of edema, hemorrhage and myonecrosis induced by North American crotalid venoms in simulated first-aid treatments

Inhibitory Effects of MLDG-containing Heterodimeric Disintegrins Reveal Distinct Structural Requirements for Interaction of the Integrin α9β1 with VCAM-1, Tenascin-C, and Osteopontin

Purification and Characterization of a Collagenolytic Protease from the Filefish, Novoden modestrus

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