Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus

J. B. Smith; R.David G. Theakston; A. L. J. Coelho; C. Barja-Fidalgo; J. J. Calvete; C. Marcinkiewicz

doi:10.1016/s0014-5793(02)02233-0

Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus

J. B. Smith, R.David G. Theakston, A. L. J. Coelho, C. Barja-Fidalgo, J. J. Calvete, C. Marcinkiewicz

Tropical Disease Biology

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Abstract

Ocellatusin is a new RGD-containing short monomeric disintegrin. It is a better inhibitor of alpha(5)beta(1) integrin and a more potent inducer of the expression of a ligand-induced binding site epitope on beta(1) integrin subunit than echistatin. In further contrast to echistatin, ocellatusin has a direct chemotactic stimulus on human neutrophils in vitro. The distinct effects of these two close evolutionarily related disintegrins might be explained by the presence of methionine-22 and histidine-29 in the RGD loop of ocellatusin, which are arginine and aspartic acid, respectively, in echistatin. These mutations may modulate the conformation and/or recognition properties of the integrin-binding loop of ocellatusin.

Original language	English
Pages (from-to)	111-115
Number of pages	5
Journal	FEBS Letters
Volume	512
Issue number	1-3
DOIs	https://doi.org/10.1016/s0014-5793(02)02233-0
Publication status	Published - 13 Feb 2002

Keywords

Cell adhesion
Disintegrin
Integrin antagonist
Platelet aggregation
RGD peptide

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10.1016/s0014-5793(02)02233-0

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title = "Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus",

abstract = "Ocellatusin is a new RGD-containing short monomeric disintegrin. It is a better inhibitor of alpha(5)beta(1) integrin and a more potent inducer of the expression of a ligand-induced binding site epitope on beta(1) integrin subunit than echistatin. In further contrast to echistatin, ocellatusin has a direct chemotactic stimulus on human neutrophils in vitro. The distinct effects of these two close evolutionarily related disintegrins might be explained by the presence of methionine-22 and histidine-29 in the RGD loop of ocellatusin, which are arginine and aspartic acid, respectively, in echistatin. These mutations may modulate the conformation and/or recognition properties of the integrin-binding loop of ocellatusin.",

keywords = "Cell adhesion, Disintegrin, Integrin antagonist, Platelet aggregation, RGD peptide",

author = "Smith, \{J. B.\} and Theakston, \{R.David G.\} and Coelho, \{A. L. J.\} and C. Barja-Fidalgo and Calvete, \{J. J.\} and C. Marcinkiewicz",

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T1 - Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus

AU - Smith, J. B.

AU - Theakston, R.David G.

AU - Coelho, A. L. J.

AU - Barja-Fidalgo, C.

AU - Calvete, J. J.

AU - Marcinkiewicz, C.

PY - 2002/2/13

Y1 - 2002/2/13

N2 - Ocellatusin is a new RGD-containing short monomeric disintegrin. It is a better inhibitor of alpha(5)beta(1) integrin and a more potent inducer of the expression of a ligand-induced binding site epitope on beta(1) integrin subunit than echistatin. In further contrast to echistatin, ocellatusin has a direct chemotactic stimulus on human neutrophils in vitro. The distinct effects of these two close evolutionarily related disintegrins might be explained by the presence of methionine-22 and histidine-29 in the RGD loop of ocellatusin, which are arginine and aspartic acid, respectively, in echistatin. These mutations may modulate the conformation and/or recognition properties of the integrin-binding loop of ocellatusin.

AB - Ocellatusin is a new RGD-containing short monomeric disintegrin. It is a better inhibitor of alpha(5)beta(1) integrin and a more potent inducer of the expression of a ligand-induced binding site epitope on beta(1) integrin subunit than echistatin. In further contrast to echistatin, ocellatusin has a direct chemotactic stimulus on human neutrophils in vitro. The distinct effects of these two close evolutionarily related disintegrins might be explained by the presence of methionine-22 and histidine-29 in the RGD loop of ocellatusin, which are arginine and aspartic acid, respectively, in echistatin. These mutations may modulate the conformation and/or recognition properties of the integrin-binding loop of ocellatusin.

KW - Cell adhesion

KW - Disintegrin

KW - Integrin antagonist

KW - Platelet aggregation

KW - RGD peptide

U2 - 10.1016/s0014-5793(02)02233-0

DO - 10.1016/s0014-5793(02)02233-0

M3 - Article

SN - 0014-5793

VL - 512

SP - 111

EP - 115

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

Characterization of a monomeric disintegrin, ocellatusin, present in the venom of the Nigerian carpet viper, Echis ocellatus

Abstract

Keywords

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