Arg-Gly-Asp: A versatile cell recognition signal

Ruoslahti, Erkki; Pierschbacher, Michael D.

doi:10.1016/0092-8674(86)90259-x

Cited by 1,358 publications

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“…These results are in full agreement with those reported by Bond et al [6] for the protein isolated from bovine serum and confirm that bovine angiogenin has the same enzymatic activities as human angiogenin, A major difference between bovine angiogenin and the three other related proteins is the presence in position 67 of an Arg-Gly-Asp sequence. This tripeptidic sequence represents a recognition site in fibronectin and other adhesive proteins from ArgGly-Asp directed adhesion receptor localized in endothelial cells [11]. Our preliminary results, which show that bovine angiogenin induces the proliferation of bovine brain capillary endothelial cells at concentrations ranging from 10 to 100 ng, suggest that this tripeptide could be involved in the interaction of bovine angiogenin with the endothelial cells (Chamoux, M. et aI., unpublished).…”

Section: Characteristics Of the Sequencementioning

confidence: 72%

The complete amino acid sequence of bovine milk angiogenin

et al. 1988

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The amino acid sequence of angiogenin isolated from bovine milk was deduced by gas-phase sequencing of the protein and its fragments. The protein contains 125 residues and has a calculated molecular mass of 14577 Da. The sequence is highly homologous (65% identity) to the sequence of human angiogenin, most of the differences being the result of conservative replacements. Like human angiogenin, the bovine protein is also homologous to bovine pancreatic RNase A (34% identity) and the three major active site residues known to be involved in the catalytic process, His-14, Lys-41 and His-115, are conserved. When tested against conventional substrates for RNase A activity, bovine angiogenin displays the same selective ribonucleolytic activity as human angiogenin. The sequence of bovine angiogenin contains the cell recognition tripeptide Arg-Gly-Asp which is not present in the human protein.

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Section: Characteristics Of the Sequencementioning

confidence: 72%

The complete amino acid sequence of bovine milk angiogenin

et al. 1988

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“…25 The matrices that will be presented in this work consist of proteins grafted with PEG diacrylate by reaction of the terminal PEG-acrylates with protein-thiols. The reaction is rapid at physiological conditions.…”

Section: Asparagine (N) Aspartic Acid (D) Cysteine (C) Glutamic Acmentioning

confidence: 99%

Biologically Engineered Protein-graft-Poly(ethylene glycol) Hydrogels: A Cell Adhesive and Plasmin-Degradable Biosynthetic Material for Tissue Repair

et al. 2002

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To address the need for bioactive materials toward clinical applications in wound healing and tissue regeneration, an artificial protein was created by recombinant DNA methods and modified by grafting of poly(ethylene glycol) diacrylate. Subsequent photopolymerization of the acrylate-containing precursors yielded protein-graft-poly(ethylene glycol) hydrogels. The artificial protein contained repeating amino acid sequences based on fibrinogen and anti-thrombin III, comprising an RGD integrin-binding motif, two plasmin degradation sites, and a heparin-binding site. Two-dimensional adhesion studies showed that the artificial protein had specific integrin-binding capability based on the RGD motif contained in its fibrinogen-based sequence. Furthermore, heparin bound strongly to the protein's anti-thrombin III-based region. Protein-graft-poly(ethylene glycol) hydrogels were plasmin degradable, had Young's moduli up to 3.5 kPa, and supported three-dimensional outgrowth of human fibroblasts. Cell attachment in three dimensions resulted from specific cell-surface integrin binding to the material's RGD sequence. Hydrogel penetration by cells involved serine-protease mediated matrix degradation in temporal and spatial synchrony with cellular outgrowth. Protein-graft-poly(ethylene glycol) hydrogels represent a new and versatile class of biomimetic hybrid materials that hold clinical promise in serving as implants to promote wound healing and tissue regeneration.

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“…6c), indicating that their function as cell attachment sequence or Nglycosylation site, respectively, is not hindered. The RGD motif was first identified in the animal cellsubstratum adhesion proteins fibronectin, fibrinogen, vitronectin and the von Willebrand coagulation factor (Ruoslathi and Pierschbacher, 1986), and was found to be crucial for the interaction with their cell surface receptors, the so-called integrins (D'Souza et al, 1988;Hynes, 1987). These specific ligand-receptor interactions mediate adhesion of cells to the extracellular matrix and are essential for normal development of animal cells.…”

Section: (G) Analysis Of Ipi-o Aa Sequencesmentioning

confidence: 99%

Structure and genomic organization of the ipiB and ipiO gene clusters of Phytophthora infestans

Pieterse

West

Verbakel

et al. 1994

Gene

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SUMMARYTwo in p/anta-induced (ipi) genes, designated ipiB and ipiO, of the potato late blight fungus, Phytophthora infestans (Mont.) de Bary, were isolated from a genomic library by a differential hybridization procedure [Pieterse et al., Physiol. Mol. Plant Pathol. (1993a) in press]. Both genes are expressed at high levels in the early phases of the pathogenic interaction of P. infestans with its host plant potato, suggesting that their gene products have a function in the early stages of the infection process. Here, we describe the nucleotide (nt) sequence and genomic organization of ipiB and ipi0. The ipiB gene belongs to a small gene family consisting of at least three genes, designated ipiBl, ipiB2 and ipiB3, which are clustered in a head-to-tail arrangement. The three ipiB genes are highly homologous throughout the coding regions and 5' and 3' flanking regions. The P. infestans genome contains two very similar ipi0 genes, ipi01 and ipi02, which are closely linked and arranged in an inverted orientation. The ipiB genes encode three novel, highly similar Glyrich proteins of 301, 343 and 347 amino acids (aa), respectively. The Gly-rich domains of the IPI-B proteins are predominantly composed of two repeats with the core sequences,

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Arg-Gly-Asp: A versatile cell recognition signal

Cited by 1,358 publications

References 0 publications

The complete amino acid sequence of bovine milk angiogenin

The complete amino acid sequence of bovine milk angiogenin

Biologically Engineered Protein-graft-Poly(ethylene glycol) Hydrogels: A Cell Adhesive and Plasmin-Degradable Biosynthetic Material for Tissue Repair

Structure and genomic organization of the ipiB and ipiO gene clusters of Phytophthora infestans

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