Crovidisin, a Collagen-Binding Protein Isolated from Snake Venom ofCrotalus viridis,Prevents Platelet–Collagen Interaction

Liu, Chao-Zong; Huang, Tur-Fu

doi:10.1006/abbi.1996.9787

Cited by 45 publications

(22 citation statements)

References 12 publications

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“…The venom metalloproteinases, such as jararhagin [21,127], catrocollastatin [128,129] and crovidisin [130] have been reported to specifically inhibit the adhesion of collagen to platelets and subsequent platelet aggregation. Jararhagin has been referred to as a collagen receptor (GPIa/IIa) antagonist, while the mechanism of action of catrocollastatin and crovidisin is attributed to their collagen-binding activity rather than binding of GPIa/IIa [129][130][131][132]. Not only platelet aggregation but also the release reaction, thromboxane formation and increase of intracellular Ca 2+ level of platelets in response to collagen were completely abolished by crovidisin [130].…”

Section: Venom Metalloproteasesmentioning

confidence: 99%

“…Jararhagin has been referred to as a collagen receptor (GPIa/IIa) antagonist, while the mechanism of action of catrocollastatin and crovidisin is attributed to their collagen-binding activity rather than binding of GPIa/IIa [129][130][131][132]. Not only platelet aggregation but also the release reaction, thromboxane formation and increase of intracellular Ca 2+ level of platelets in response to collagen were completely abolished by crovidisin [130]. [133,134].…”

Section: Venom Metalloproteasesmentioning

confidence: 99%

“…GPIIa) with loss of the integrin structure necessary for the binding of macromolecular ligands [132]. However, both the action of crovidisin and catrocollastatin were independent of the proteolytic activity (or metalloproteinase domain), and they do not bind to integrin h 2 i 1 [129,130]. A cyclic oligopeptide corresponding to the conserved fragment containing SECD, but not the linear SECD fragment, in the disintegrin-like domain of catrocollastatin (table 1) was shown to inhibit collagen-induced platelet aggregation and to bind to collagen [129].…”

Section: Membrane-anchored Adamsmentioning

confidence: 99%

See 2 more Smart Citations

What have snakes taught us about integrins?

Huang¹

1998

Cellular and Molecular Life Sciences (CMLS)

102

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Snake venoms contain unique components that affect cell-matrix interactions. Disintegrins represent a class of low molecular weight, Arg-Gly-Asp (RGD)-containing, cysteine-rich peptides purified from the venom of various snakes among the Viperidae and Crotalidae. They bind with various degrees of specificity to integrins alpha IIb beta 3, alpha 5 beta 1 and alpha V beta 3 expressed on cells. Snake venom metalloproteases (high molecular mass haemorrhagins) also contain disintegrin-like domains, in addition to zinc-chelating sequences. Membrane-anchored ADAMs (A Disintegrin And Metalloprotease domain), multidomain molecules consisting of metalloprotease, disintegrin-like, cysteine-rich, and epidermal growth factor domains, a transmembrane domain and a cytoplasmic tail, are a new family of proteins. In the light of the large number and wide distribution of ADAMs, they may participate in cell-cell fusion events, including sperm-egg binding and fusion, myoblast fusion and other cell-cell and cell-matrix interactions. The structure-function relationship of these molecules is discussed.

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Section: Venom Metalloproteasesmentioning

confidence: 99%

Section: Venom Metalloproteasesmentioning

confidence: 99%

Section: Membrane-anchored Adamsmentioning

confidence: 99%

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What have snakes taught us about integrins?

Huang¹

1998

Cellular and Molecular Life Sciences (CMLS)

102

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“…The more amazing is the finding, that several venom proteinases, such as the PIII-SVMPs, Crovidisin from Crotalus viridis, Catrocollastatin from Crotalus atrox, and jararhagin from B. jararaca (Liu and Hang, 1997;Tanjoni et al, 2003Tanjoni et al, , 2010, in addition firmly bind to triple-helical collagen molecules. Also, the von Willebrand factor (vWF) A-domain, which is present in several ECM proteins, such as vWF, matrilins and certain collagen types, but also in integrin receptors, is bound by the non-catalytic cysteine-rich domain of the PIII SVMP jararhagin (Pinto et al, 2007;Serrano et al, 2006).…”

Section: Fibrinogen and Beyond: Other Extracellular Matrix Molecules mentioning

confidence: 96%

Matrix biology meets toxinology

Eble

2010

Matrix Biology

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“…Snake venom components have been characterised that affect collagen-platelet interactions by binding to collagen or platelet-collagen receptors. These include crovidisin [30] Fig. 3.…”

Section: Natural Inhibitorsmentioning

confidence: 99%

Platelet Collagen Receptors: A New Target for Inhibition?

Clemetson

1999

Pathophysiol Haemos Thromb

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Collagen is a major component of extracellular matrix and a wide variety of types exist. Cells recognise collagen in different ways depending on sequence and structure. They can recognise predominantly primary sequence, they may require triple-helical structure or they can require fibrillar structures. Since collagens are major constituents of the subendothelium that determine the thrombogenicity of the injured or pathological vessel wall, a major role is induction of platelet activation and aggregation as the start of repair processes. Platelets have at least two direct and one indirect (via von Willebrand factor) receptors for collagen, and collagen has specific recognition motifs for these receptors. These receptors and recognition motifs are under intensive investigation in the search for possible methods to control platelet activation in vivo. A wide range of proteins has been identified and, in part, characterised from both haematophageous insects and invertebrates but also from snake venoms that inhibit platelet activation by collagen or induce platelet activation via collagen receptors on platelets. These will provide model systems to test the effect of inhibition of specific collagen-platelet receptor interactions for both effectiveness as well as for side effects and should provide assay systems for the development of small molecule inhibitors. Since platelet inhibitors for long-term prophylaxis of cardiovascular diseases are still in clinical trials there are many unanswered questions about long-term effects both positive and negative. The major problem which still has to be definitively solved about these alternative approaches to inhibition of platelet activation is whether they will show advantages in terms of dose-response curves while offering decreased risks of bleeding problems. Preliminary studies would seem to suggest that this is indeed the case.

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Crovidisin, a Collagen-Binding Protein Isolated from Snake Venom ofCrotalus viridis,Prevents Platelet–Collagen Interaction

Cited by 45 publications

References 12 publications

What have snakes taught us about integrins?

What have snakes taught us about integrins?

Matrix biology meets toxinology

Platelet Collagen Receptors: A New Target for Inhibition?

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