Preparation and functional evaluation of RGD-modified proteins as αvβ3 integrin directed therapeutics

Bioconjugate Chemistry

Volumn 13, Issue 1, 2002, Pages 128-135

  Kok, Robbert J ^a   Schraa, Astrid J ^b   Bos, Erwin J ^a   Moorlag, Henk E ^b   Ásgeirsdóttir, Sigridur A ^a   Everts, Maaike ^a   Meijer, Dirk K F ^a   Molema, Grietje ^c  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b Tumor Immunology Laboratory   (Netherlands)

^c Laboratory Medicine   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD VESSELS; CELL ADHESION; ENDOTHELIAL CELLS; LIGANDS; PEPTIDES;

ANTIANGIOGENIC; COVALENT ATTACHMENT; ENDOTHELIAL-CELLS; FUNCTIONAL EVALUATION; INTEGRINS; MODIFIED PROTEINS; NATURAL LIGANDS; PEPTIDE LIGAND; PROTEIN CONJUGATES; RGD PEPTIDE;

GLYCOPROTEINS;

ANGIOGENESIS INHIBITOR; ARGINYL-GLYCYL-ASPARTIC ACID; ARGINYLGLYCYLASPARTIC ACID; IMMUNOGLOBULIN G; OLIGOPEPTIDE; PEPTIDE; PROTEIN; VITRONECTIN RECEPTOR;

ARTICLE; CELL ADHESION; CHEMISTRY; DRUG EFFECT; GEL CHROMATOGRAPHY; HUMAN; METABOLISM; POLYACRYLAMIDE GEL ELECTROPHORESIS; SYNTHESIS; VASCULAR ENDOTHELIUM;

ANGIOGENESIS INHIBITORS; CELL ADHESION; CHROMATOGRAPHY, GEL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENDOTHELIUM, VASCULAR; HUMANS; IMMUNOGLOBULIN G; OLIGOPEPTIDES; PEPTIDES; PROTEINS; RECEPTORS, VITRONECTIN;

EID: 0036007606     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc015561+     Document Type: Article

References (24)

1. Angiogenesis: Potentials for pharmacologic intervention in the treatment of cancer, cardiovascular diseases, and chronic inflammation
2. An address system in the vasculature of normal tissues and tumors
3. Phage libraries displaying cyclic peptides with different ring sizes: Ligand specificities of the RGD-directed integrins
4. Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model
5. Solution structures and integrin binding activities of an RGD peptide with two isomers
6. Structural and functional aspects of RGD-containing cyclic pentapeptides as highly potent and selective integrin alpha-v-beta-3 antagonists
7. Carbohydrate Derivatives for Use in Drug Design: Cyclic alpha(v)-Selective RGD Peptides
8. Radiolabeled alpha(v)beta3 integrin antagonists: A new class of tracers for tumor targeting
9. Mechanisms for the hepatic clearance of oligopeptides and proteins. Implications for rate of elimination, bioavailability and cell-specific drug delivery to the liver
10. Protein measurement with the Folin Phenol reagent
11. Basal tissue factor expression in endothelial cell cultures is caused by contaminating smooth muscle cells. Reduction by using chymotrypsin instead of collagenase
12. Evidence for the involvement of endothelial cell integrin alphaVbeta3 in the disruption of the tumor vasculature induced by TNF and IFN-gamma
13. Preparation of iodine-131 labeled human growth hormone of high specific activity
14. Superactivation of integrin alphavbeta3 by low antagonist concentrations
15. Selective RGD-mediated adhesion of osteoblasts at surfaces of implants
16. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid
17. Successful targeting of albumin to rat hepatic stellate cells using albumin modified with cyclic peptides that recognize the collagen type VI receptor
18. N-Methylated cyclic RGD peptides as highly active and selective alpha(V)beta(3) integrin antagonists
19. Tumor infarction in mice by antibody-directed targeting of tissue factor to tumor vasculature
20. Enhancement of tumor necrosis factor alpha antitumor immunotherapeutic properties by targeted delivery to aminopeptidase N (CD13)
21. Synergy between an antiangiogenic integrin alphav antagonist and an antibody-cytokine fusion protein eradicates spontaneous tumor metastases
22. Immunotargeting of glucose oxidase to endothelium in vivo causes oxidative vascular injury in the lungs
23. Development of proteinaceous drug targeting constructs using chemical and recombinant DNA approaches
24. Selective adhesion of endothelial cells to artificial membranes with a synthetic RGD-lipopeptide