Leberagin-C, A disintegrin-like/cysteine-rich protein from Macrovipera lebetina transmediterranea venom, inhibits alphavbeta3 integrin-mediated cell adhesion

Limam, Inès; Bazaa, Amine; Srairi-Abid, Najet; Taboubi, Salma; Jebali, Jed; Zouari-Kessentini, Raoudha; Kallech-Ziri, Olfa; Mejdoub, Hafedh; Hammami, Asma; Ayeb, Mohamed El; Luis, José; Marrakchi, Naziha

doi:10.1016/j.matbio.2009.09.009

Cited by 40 publications

(31 citation statements)

References 63 publications

(106 reference statements)

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“…Similarly, native and recombinant DC domains of alternagin, catrocollastatin and atrolysin A inhibit collagen-induced platelet aggregation [100,103,116]. In contrast, leberagin-C, DC domain containing protein from Macrovipera labetina transmediterranea venom inhibits platelet aggregation induced by thrombin and arachidonic acid with IC 50 of 40 and 50 nM, respectively [117]. It inhibits the adhesion of melanoma tumor cells on fibrinogen and fibronectin, by interfering with the function of α v β 3 and, to a lesser extent, with α v β 6 and α v β 1 integrins.…”

Section: Role Of Non-enzymatic Domains and Subunitsmentioning

confidence: 99%

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Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites

Kini

Koh

2016

Toxins

144

129

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Snake venom metalloproteases, in addition to their contribution to the digestion of the prey, affect various physiological functions by cleaving specific proteins. They exhibit their activities through activation of zymogens of coagulation factors, and precursors of integrins or receptors. Based on their structure–function relationships and mechanism of action, we have defined classification and nomenclature of functional sites of proteases. These metalloproteases are useful as research tools and in diagnosis and treatment of various thrombotic and hemostatic conditions. They also contribute to our understanding of molecular details in the activation of specific factors involved in coagulation, platelet aggregation and matrix biology. This review provides a ready reference for metalloproteases that interfere in blood coagulation, fibrinolysis and platelet aggregation.

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Section: Role Of Non-enzymatic Domains and Subunitsmentioning

confidence: 99%

“…Alternagin-C binds to collagen receptor, α 2 β 1 integrin through its RSECD sequence located in the D domain [102]. Leberagin-C binds to α v β 3 integrin [117]. However, specific integrin-binding motif was not evaluated.…”

Section: Svmps As Research Tools and Diagnostic And Therapeutic mentioning

confidence: 99%

Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites

Kini

Koh

2016

Toxins

144

129

View full text Add to dashboard Cite

show abstract

“…Leberagin-C may interact with αvβ3 and, to a lesser extent, with αvβ6 and α5β1 integrins. This disintegrin is able to prevent platelet aggregation induced by thrombin and arachidonic acid, the adhesion of melanoma tumor cells on fibrinogen and fibronectin [122]. …”

Section: Introductionmentioning

confidence: 99%

Disintegrins from Snake Venoms and their Applications in Cancer Research and Therapy

Macêdo¹,

Fox

Castro³

2015

CPPS

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Integrins regulate diverse functions in cancer pathology and in tumor cell development and contribute to important processes such as cell shape, survival, proliferation, transcription, angiogenesis, migration, and invasion. A number of snake venom proteins have the ability to interact with integrins. Among these are the disintegrins, a family of small, non-enzymatic, and cysteine-rich proteins found in the venom of numerous snake families. The venom proteins may have a potential role in terms of novel therapeutic leads for cancer treatment. Disintegrin can target specific integrins and as such it is conceivable that they could interfere in important processes involved in carcinogenesis, tumor growth, invasion and migration. Herein we present a survey of studies involving the use of snake venom disintegrins for cancer detection and treatment. The aim of this review is to highlight the relationship of integrins with cancer and to present examples as to how certain disintegrins can detect and affect biological processes related to cancer. This in turn will illustrate the great potential of these molecules for cancer research. Furthermore, we also outline several new approaches being created to address problems commonly associated with the clinical application of peptide-based drugs such as instability, immunogenicity, and availability.

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“…Collagen receptor, α2β1 integrin was reported as a target for alternagin C and the sequence, RSECD, located in the disintegrin-like domain was identified as an active site for this interaction (Souza et al, 2000). More recent studies with leberagin-C showed that it inhibits typical RGD-dependent integrin, αvβ3 (Limam et al, 2010). However, specific integrin-binding motif was not evaluated.…”

Section: Snake Venom Disintegrinsmentioning

confidence: 99%

Applications of snake venom components to modulate integrin activities in cell–matrix interactions

Marcinkiewicz

2013

The International Journal of Biochemistry & Cell Biology

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Snake venom proteins are broadly investigated in the different areas of life science. Direct interaction of these compounds with cells may involve a variety of mechanisms that result in diverse cellular responses leading to the activation or blocking of physiological functions of the cell. In this review, the snake venom components interacting with integrins will be characterized in context of their effect on cellular response. Currently, two major families of snake venom proteins are considered as integrin-binding molecules. The most attention has been devoted to the disintegrin family, which binds certain types of integrins through specific motifs recognized as a tri-peptide structurally localized on an integrin-binding loop. Other snake venom integrin-binding proteins belong to the C-type lectin family. Snake venom molecules bind to the cellular integrins resulting in a modulation of cell signaling and in consequence, the regulation of cell proliferation, migration and apoptosis. Therefore, snake venom research on the integrin-binding molecules may have significance in biomedicine and basic cell biology.

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Leberagin-C, A disintegrin-like/cysteine-rich protein from Macrovipera lebetina transmediterranea venom, inhibits alphavbeta3 integrin-mediated cell adhesion

Cited by 40 publications

References 63 publications

Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites

Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites

Disintegrins from Snake Venoms and their Applications in Cancer Research and Therapy

Applications of snake venom components to modulate integrin activities in cell–matrix interactions

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