Cell-based adhesion assays for isolation of snake venom’s integrin antagonists

Philip Lazarovici; Cezary Marcinkiewicz; Peter I. Lelkes

doi:10.1007/978-1-4939-9845-6_11

Cell-based adhesion assays for isolation of snake venom’s integrin antagonists

Philip Lazarovici
, Cezary Marcinkiewicz
, Peter I. Lelkes

Cancer Signaling and Microenvironment (CSM)

Hebrew University of Jerusalem
Temple University

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

7 Scopus citations

Abstract

Snake venoms could lead to the development of new drugs to treat a range of life-threatening conditions like cardiovascular diseases. Most snake venoms contain a large variety of lethal toxins as well as anti-adhesive proteins such as disintegrins, which have evolved from the harmless compounds ADAMs (proteins with a disintegrin and a metalloprotease domain) and C-type lectin proteins which disturb connective tissue and cell-matrix interaction. These anti-adhesive proteins target and block integrin receptors and disrupt normal biological processes in snakes’ prey such as connective tissue physiology and blood clotting. This chapter provides the experimental details of a practical, cell-based adhesion protocol to help identify and isolate disintegrins and C-type lectin proteins from snake venoms, important tools in integrin research and lead compounds for drug discovery.

Original language	English
Title of host publication	Methods in Molecular Biology
Publisher	Humana Press Inc.
Pages	205-223
Number of pages	19
Volume	2068
DOIs	https://doi.org/10.1007/978-1-4939-9845-6_11
State	Published - 2020

Publication series

Name	Methods in molecular biology (Clifton, N.J.)
Publisher	Humana Press
ISSN (Print)	1064-3745

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Animals
Biological Assay
Blood Coagulation/drug effects
Cell Adhesion/physiology
Disintegrins/antagonists & inhibitors
Humans
Lectins/chemistry
Snake Venoms/analysis

Access to Document

10.1007/978-1-4939-9845-6_11

Cite this

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title = "Cell-based adhesion assays for isolation of snake venom{\textquoteright}s integrin antagonists",

abstract = "Snake venoms could lead to the development of new drugs to treat a range of life-threatening conditions like cardiovascular diseases. Most snake venoms contain a large variety of lethal toxins as well as anti-adhesive proteins such as disintegrins, which have evolved from the harmless compounds ADAMs (proteins with a disintegrin and a metalloprotease domain) and C-type lectin proteins which disturb connective tissue and cell-matrix interaction. These anti-adhesive proteins target and block integrin receptors and disrupt normal biological processes in snakes{\textquoteright} prey such as connective tissue physiology and blood clotting. This chapter provides the experimental details of a practical, cell-based adhesion protocol to help identify and isolate disintegrins and C-type lectin proteins from snake venoms, important tools in integrin research and lead compounds for drug discovery.",

keywords = "Animals, Biological Assay, Blood Coagulation/drug effects, Cell Adhesion/physiology, Disintegrins/antagonists \& inhibitors, Humans, Lectins/chemistry, Snake Venoms/analysis",

author = "Philip Lazarovici and Cezary Marcinkiewicz and Lelkes, \{Peter I.\}",

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doi = "10.1007/978-1-4939-9845-6\_11",

language = "English",

volume = "2068",

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AU - Lazarovici, Philip

AU - Marcinkiewicz, Cezary

AU - Lelkes, Peter I.

N1 - Publisher Copyright: © Springer Science+Business Media, LLC, part of Springer Nature 2020.

PY - 2020

Y1 - 2020

N2 - Snake venoms could lead to the development of new drugs to treat a range of life-threatening conditions like cardiovascular diseases. Most snake venoms contain a large variety of lethal toxins as well as anti-adhesive proteins such as disintegrins, which have evolved from the harmless compounds ADAMs (proteins with a disintegrin and a metalloprotease domain) and C-type lectin proteins which disturb connective tissue and cell-matrix interaction. These anti-adhesive proteins target and block integrin receptors and disrupt normal biological processes in snakes’ prey such as connective tissue physiology and blood clotting. This chapter provides the experimental details of a practical, cell-based adhesion protocol to help identify and isolate disintegrins and C-type lectin proteins from snake venoms, important tools in integrin research and lead compounds for drug discovery.

AB - Snake venoms could lead to the development of new drugs to treat a range of life-threatening conditions like cardiovascular diseases. Most snake venoms contain a large variety of lethal toxins as well as anti-adhesive proteins such as disintegrins, which have evolved from the harmless compounds ADAMs (proteins with a disintegrin and a metalloprotease domain) and C-type lectin proteins which disturb connective tissue and cell-matrix interaction. These anti-adhesive proteins target and block integrin receptors and disrupt normal biological processes in snakes’ prey such as connective tissue physiology and blood clotting. This chapter provides the experimental details of a practical, cell-based adhesion protocol to help identify and isolate disintegrins and C-type lectin proteins from snake venoms, important tools in integrin research and lead compounds for drug discovery.

KW - Animals

KW - Biological Assay

KW - Blood Coagulation/drug effects

KW - Cell Adhesion/physiology

KW - Disintegrins/antagonists & inhibitors

KW - Humans

KW - Lectins/chemistry

KW - Snake Venoms/analysis

UR - https://www.scopus.com/pages/publications/85072847378

U2 - 10.1007/978-1-4939-9845-6_11

DO - 10.1007/978-1-4939-9845-6_11

M3 - Chapter

C2 - 31576530

AN - SCOPUS:85072847378

VL - 2068

T3 - Methods in molecular biology (Clifton, N.J.)

SP - 205

EP - 223

BT - Methods in Molecular Biology

PB - Humana Press Inc.

ER -

Cell-based adhesion assays for isolation of snake venom’s integrin antagonists

Abstract

Publication series

UN SDGs

Keywords

Access to Document

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