Journal ArticleDOI
RGD and other recognition sequences for integrins.
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TLDR
As the integrin-mediated cell attachment influences and regulates cell migration, growth, differentiation, and apoptosis, the RGD peptides and mimics can be used to probe integrin functions in various biological systems.Abstract:
Proteins that contain the Arg-Gly-Asp (RGD) attachment site, together with the integrins that serve as receptors for them, constitute a major recognition system for cell adhesion. The RGD sequence is the cell attachment site of a large number of adhesive extracellular matrix, blood, and cell surface proteins, and nearly half of the over 20 known integrins recognize this sequence in their adhesion protein ligands. Some other integrins bind to related sequences in their ligands. The integrin-binding activity of adhesion proteins can be reproduced by short synthetic peptides containing the RGD sequence. Such peptides promote cell adhesion when insolubilized onto a surface, and inhibit it when presented to cells in solution. Reagents that bind selectively to only one or a few of the RGD-directed integrins can be designed by cyclizing peptides with selected sequences around the RGD and by synthesizing RGD mimics. As the integrin-mediated cell attachment influences and regulates cell migration, growth, differentiation, and apoptosis, the RGD peptides and mimics can be used to probe integrin functions in various biological systems. Drug design based on the RGD structure may provide new treatments for diseases such as thrombosis, osteoporosis, and cancer.read more
Citations
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Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering
TL;DR: Although modern synthetic biomaterials represent oversimplified mimics of natural ECMs lacking the essential natural temporal and spatial complexity, a growing symbiosis of materials engineering and cell biology may ultimately result in synthetic materials that contain the necessary signals to recapitulate developmental processes in tissue- and organ-specific differentiation and morphogenesis.
Journal ArticleDOI
Mutations in PCSK9 cause autosomal dominant hypercholesterolemia.
Marianne Abifadel,Mathilde Varret,Jean-Pierre Rabès,Delphine Allard,Khadija Ouguerram,Martine Devillers,Corinne Cruaud,Suzanne Benjannet,Louise Wickham,D. Erlich,Aurélie Derré,Ludovic Villéger,Michel Farnier,Isabel Beucler,Eric Bruckert,Jean Chambaz,Bernard Chanu,Jean-Michel Lecerf,Gérald Luc,Philippe Moulin,Jean Weissenbach,Annick Prat,Michel Krempf,Claudine Junien,Nabil G. Seidah,Catherine Boileau +25 more
TL;DR: Two mutations in the gene PCSK9 (encoding proprotein convertase subtilisin/kexin type 9) that cause ADH are reported, a newly identified human subtilase that is highly expressed in the liver and contributes to cholesterol homeostasis.
Journal ArticleDOI
RGD modified polymers: biomaterials for stimulated cell adhesion and beyond
TL;DR: The impacts of RGD peptide surface density, spatial arrangement as well as integrin affinity and selectivity on cell responses like adhesion and migration are discussed.
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Hydrogels as Extracellular Matrix Mimics for 3D Cell Culture
TL;DR: The use of both synthetic and natural hydrogels as scaffolds for three-dimensional cell culture as well as synthetic hydrogel hybrids that incorporate sophisticated biochemical and mechanical cues as mimics of the native extracellular matrix are discussed.
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Cancer Treatment by Targeted Drug Delivery to Tumor Vasculature in a Mouse Model
TL;DR: In vivo selection of phage display libraries was used to isolate peptides that home specifically to tumor blood vessels that enhanced the efficacy of the anticancer drug doxorubicin and reduced its toxicity.
References
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Journal ArticleDOI
New perspectives in cell adhesion : RGD and integrins
TL;DR: Together, the adhesion proteins and their receptors constitute a versatile recognition system providing cells with anchorage, traction for migration, and signals for polarity, position, differentiation, and possibly growth.
Journal ArticleDOI
Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
TL;DR: The ability of fibronectin to bind cells can be accounted for by the tetrapeptide L-arginyl-glycyl- L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of fibronsectin and present in at least five other proteins.
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Requirement of vascular integrin alpha v beta 3 for angiogenesis
TL;DR: The adhesion receptor integrin alpha v beta 3 was identified as a marker of angiogenic vascular tissue in this paper, and it showed a fourfold increase in expression during angiogenesis on the chick chorioallantoic membrane.
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Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels
Peter C. Brooks,Anthony M.P. Montgomery,Mauricio Rosenfeld,Ralph A. Reisfeld,Tianhua Hu,George Klier,David A. Cheresh +6 more
TL;DR: In this article, a single intravascular injection of a cyclic peptide or monoclonal antibody antagonist of integrin alpha v beta 3 disrupts ongoing angiogenesis on the chick chorioallantoic membrane (CAM).
Journal ArticleDOI
Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor
TL;DR: Affinity chromatography on wheat germ agglutinin-Sepharose showed that the 140 kd protein is a glycoprotein and, in combination with the fibronectin fragment chromatography, gave highly enriched preparations of the 140Kd protein.