The effect of peptide surface density on mineralization of a matrix deposited by osteogenic cells
2000; Wiley; Volume: 52; Issue: 4 Linguagem: Inglês
10.1002/1097-4636(20001215)52
ISSN1097-4636
AutoresAlireza Rezania, Kevin E. Healy,
Tópico(s)Polymer Surface Interaction Studies
ResumoJournal of Biomedical Materials ResearchVolume 52, Issue 4 p. 595-600 The effect of peptide surface density on mineralization of a matrix deposited by osteogenic cells Alireza Rezania, Alireza Rezania Division of Biological Materials, Northwestern University, 311 E. Chicago Avenue, Chicago, Illinois 60611-3008 Department of Biomedical Engineering, Robert R. McCormick School of Engineering and Applied Science, Northwestern University, Evanston, Illinois 60201Search for more papers by this authorKevin E. Healy, Corresponding Author Kevin E. Healy [email protected] Division of Biological Materials, Northwestern University, 311 E. Chicago Avenue, Chicago, Illinois 60611-3008 Department of Biomedical Engineering, Robert R. McCormick School of Engineering and Applied Science, Northwestern University, Evanston, Illinois 60201Division of Biological Materials, Northwestern University, 311 E. Chicago Avenue, Chicago, Illinois 60611-3008Search for more papers by this author Alireza Rezania, Alireza Rezania Division of Biological Materials, Northwestern University, 311 E. Chicago Avenue, Chicago, Illinois 60611-3008 Department of Biomedical Engineering, Robert R. McCormick School of Engineering and Applied Science, Northwestern University, Evanston, Illinois 60201Search for more papers by this authorKevin E. Healy, Corresponding Author Kevin E. Healy [email protected] Division of Biological Materials, Northwestern University, 311 E. Chicago Avenue, Chicago, Illinois 60611-3008 Department of Biomedical Engineering, Robert R. McCormick School of Engineering and Applied Science, Northwestern University, Evanston, Illinois 60201Division of Biological Materials, Northwestern University, 311 E. Chicago Avenue, Chicago, Illinois 60611-3008Search for more papers by this author First published: 03 October 2000 https://doi.org/10.1002/1097-4636(20001215)52:4 3.0.CO;2-3Citations: 147AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract The density of Arg-Gly-Asp-containing peptides covalently grafted to solid materials has been shown to affect adhesion, spreading, and focal contact formation. The objective of this study was to examine the effect of ligand density on mineralization of the extracellular matrix deposited by osteoblasts. In particular, RGD-modified quartz surfaces with ligand densities varying over two orders (0.01–3.6 pmol/cm2) of magnitude were prepared to assess the long-term function of osteoblasts on peptide-derivatized surfaces. After 3 weeks in culture, surfaces modified with a 15 amino acid peptide (Ac-Cys-Gly-Gly-Asn-Gly-Glu-Pro-Arg-Gly-Asp-Thr-Tyr-Arg-Ala-Tyr-NH2) at a density ≥0.62 pmol/cm2 significantly (p < 0.05) enhanced mineralization compared with a RGD surface density of 0.01 pmol/cm2, RGE surfaces, or clean surfaces adsorbed with serum proteins. These results suggest that regulation of the surface density of adhesive ligands on biomaterial surfaces is a critical determinant in a strategy to alter the degree of extracellular matrix maturation in contact with solid surfaces (e.g., implants). Further studies are required to elucidate the intracellular signal transduction pathways that mediate long-term matrix mineralization through the initial engagement of these adhesive ligands. © 2000 John Wiley & Sons, Inc. J Biomed Mater Res, 52, 595–600, 2000. References 1Massia SP, Hubbell JA. An RGD spacing of 440 nm is sufficient for integrin α5β3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation. J Cell Biol 1991; 114: 1089–1100. 10.1083/jcb.114.5.1089 CASPubMedWeb of Science®Google Scholar 2Massia SP, Hubbell JA. Covalent surface immobilization of Arg-Gly-Asp- and Tyr-Ile-Gly-Ser-Arg-containing peptides to obtain well-defined cell-adhesive substrates. Anal Biochem 1990; 187: 292–301. 10.1016/0003-2697(90)90459-M CASPubMedWeb of Science®Google Scholar 3Brandley BK, Schnaar RL. Covalent attachment of an Arg-Gly-Asp sequence peptide to derivatizable polyacrylamide surfaces: Support of fibroblast adhesion and long-term growth. Anal Biochem 1988; 172: 270–278. 10.1016/0003-2697(88)90442-3 CASPubMedWeb of Science®Google Scholar 4Danilov YN, Juliano RL. (Arg-Gly-Asp)n-albumin conjugates as a model substratum for integrin-mediated cell adhesion. Exp Cell Res 1989; 182: 186–196. 10.1016/0014-4827(89)90290-5 CASPubMedWeb of Science®Google Scholar 5Ward MD, Dembo M, Hammer DA. Kinetics of cell detachment: Effect of ligand density. Ann Biomed Eng 1995; 23: 322–331. 10.1007/BF02584432 PubMedWeb of Science®Google Scholar 6Ward MD, Dembo M, Hammer DA. Kinetics of cell detachment: Peeling of discrete receptor clusters. Biophys J 1994; 67: 2522–2534. 10.1016/S0006-3495(94)80742-8 CASPubMedWeb of Science®Google Scholar 7Kuo SC, Lauffenberger DA. Relationship between receptor/ligand binding affinity and adhesion strength. Biophys J 1993; 65: 2191–2200. 10.1016/S0006-3495(93)81277-3 CASPubMedWeb of Science®Google Scholar 8Di Milla PA, Stone JA, Albelda SM, Lauffenburger DA, Quinn JA. Measurement of cell adhesion and migration on protein-coated surfaces. Mater Res Soc Symp Proc 1992; 252: 205–212. 10.1557/PROC-252-205 CASGoogle Scholar 9DiMilla PA, Stone JA, Quinn JA, Albelda SM, Lauffenburger DA. Maximal migration of human smooth muscle cells on fibronectin and type IV collagen occurs at an intermediate attachment strength. J Cell Biol 1993; 122: 729–737. 10.1083/jcb.122.3.729 CASPubMedWeb of Science®Google Scholar 10Palecek SP, Loftus JC, Ginsberg MH, Lauffenburger DA, Horwitz AF. Integrin–ligand binding properties govern cell migration speed through cell–substratum adhesiveness. Nature 1997; 385: 537–540. 10.1038/385537a0 CASPubMedWeb of Science®Google Scholar 11Somerman MJ, Fisher LW, Foster RA, Sauk JJ. Human bone sialoprotein I and II enhance fibroblast attachment in vitro. Calcif Tissue Int 1988; 43: 50–53. 10.1007/BF02555169 CASPubMedWeb of Science®Google Scholar 12Mintz KP, Grzesik WJ, Midura RJ, Robey PG, Termine JD, Fisher LW. Purification and fragmentation of nondenatured bone sialoprotein: Evidence for a cryptic, RGD-resistant cell attachment domain. J Bone Min Res 1993; 8: 985–995. 10.1002/jbmr.5650080812 CASPubMedWeb of Science®Google Scholar 13Rezania A, Healy KE. Biomimetic peptide surfaces that regulate adhesion, spreading, cytoskeletal organization, and mineralization of matrix deposited by osteoblast-like cells. Biotech Progress 1999; 15: 19–32. 10.1021/bp980083b CASPubMedWeb of Science®Google Scholar 14Rezania A, Johnson R, Lefkow AR, Healy KE. Bioactivation of metal oxide surfaces. I. Surface characterization and cell response. Langmuir 1999; 15: 6931–6939. 10.1021/la990024n CASWeb of Science®Google Scholar 15Whitson SW, Ehitson MA, Bowers DE, Falk MC. Factors influencing synthesis and mineralization of bone matrix from fetal bovine cells grown in vitro. J Bone Miner Res 1992; 7: 727–741. 10.1002/jbmr.5650070703 CASPubMedWeb of Science®Google Scholar 16Healy KE, Thomas CH, Rezania A, Kim JE, McKeown PJ, Lom B, Hockberger PE. Kinetics of bone cell organization and mineralization on materials with patterned surface chemistry. Biomaterials 1996; 16: 195–208. 10.1016/0142-9612(96)85764-4 CASWeb of Science®Google Scholar 17Thomas CH, McFarland CD, Jenkins ML, Rezania A, Steele JG, Healy KE. The role of vitronectin in the attachment and spatial distribution of bone-derived cells on materials with patterned surface chemistry. J Biomed Mater Res 1997; 37: 81–90. 10.1002/(SICI)1097-4636(199710)37:1 3.0.CO;2-T CASPubMedWeb of Science®Google Scholar 18Steele JG, Dalton BA, Johnson G, Underwood PA. Polystyrene chemistry affects vitronectin activity: An explanation for cell attachment to tissue culture polystyrene but not to unmodified polystyrene. J Biomed Mater Res 1993; 27: 927–940. 10.1002/jbm.820270712 CASPubMedWeb of Science®Google Scholar 19Howlett CR, Evans MD, Walsh WR, Johnson G, Steele JG. Mechanism of initial attachment of cells derived from human bone to commonly used prosthetic materials during cell culture. Biomaterials 1994; 15(3): 213–222. 10.1016/0142-9612(94)90070-1 CASPubMedWeb of Science®Google Scholar 20Cooper LF, Yliheikkila PK, Felton DA, Whitson SW. Spatiotemporal assessment of fetal bovine osteoblast culture differentiation indicates a role for BSP in promoting differentiation. J Bone Miner Res 1998; 13: 620–632. 10.1359/jbmr.1998.13.4.620 CASPubMedWeb of Science®Google Scholar 21Nefussi JR, Brami G, Modrowski D, Oboeuf M, Forest N. Sequential expression of bone matrix proteins during rat calvaria osteoblast differentiation and bone nodule formation in vitro. J Histochem Cytochem 1997; 45: 493–503. 10.1177/002215549704500402 CASPubMedWeb of Science®Google Scholar 22Shapiro HS, Chen J, Wrana JL, Zhang Q, Blum M, Sodek J. Characterization of porcine bone sialoprotein: Primary structure and cellular expression. Matrix 1993; 13: 431–440. 10.1016/S0934-8832(11)80109-5 CASPubMedWeb of Science®Google Scholar 23Bianco P, Fisher LW, Young MF, Termine JD, Robey PG. Expression of bone sialoprotein (BSP) in developing human tissue. Calcif Tissue Int 1991; 49: 421–426. 10.1007/BF02555854 CASPubMedWeb of Science®Google Scholar 24Hunter GK, Goldberg HA. Nucleation of hydroxyapatite by bone sialoprotein. Proc Natl Acad Sci 1993; 90: 8562–8565. 10.1073/pnas.90.18.8562 CASPubMedWeb of Science®Google Scholar 25Gronowicz GA, Derome ME. Synthetic peptide containing Arg-Gly-Asp inhibits bone formation and resorption in a mineralizing organ culture system of fetal rat parietal bones. J Bone Miner Res 1994; 9: 193–201. 10.1002/jbmr.5650090208 CASPubMedWeb of Science®Google Scholar 26Rezania A, Healy KE. Integrin subunits responsible for adhesion of human osteoblast-like cells to RGD-containing surfaces. J Orthop Res 1999; 17: 615–623. 10.1002/jor.1100170423 CASPubMedWeb of Science®Google Scholar 27Zhou HY, Takita H, Fujisawa R, Mizuno M, Kuboki Y. Stimulation of bone sialoprotein of calcification is in osteoblast-like MC2T2-E1 cells. Calcif Tissue Int 1995; 56: 403–407. 10.1007/BF00301610 CASPubMedWeb of Science®Google Scholar 28Ward MD, Hammer DA. A theoretical analysis for the effect of focal contact formation on cell–substrate attachment strength. Biophys J 1993; 64: 936–959. 10.1016/S0006-3495(93)81456-5 CASPubMedWeb of Science®Google Scholar 29Olivier LA, Truskey GA. A numerical analysis of forces exerted by laminar flow on spreading cells in a parallel plate flow chamber assay. Biotech Bioeng 1993; 42: 963–973. 10.1002/bit.260420807 CASPubMedWeb of Science®Google Scholar 30Mooney DJ, Langer R, Ingber DE. Cytoskeletal filament assembly and the control of cell spreading and function by extracellular matrix. J Cell Sci 1995; 108: 2311–2320. CASPubMedWeb of Science®Google Scholar 31Saterbak A, Lauffenburger DA. Adhesion mediated by bonds in series. Biotechnol Prog 1996; 12: 682–699. 10.1021/bp960061u CASPubMedWeb of Science®Google Scholar Citing Literature Volume52, Issue415 December 2000Pages 595-600 ReferencesRelatedInformation
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