PMID- 15174104
OWN - NLM
STAT- MEDLINE
DCOM- 20041222
LR  - 20151119
IS  - 1549-3296 (Print)
IS  - 1549-3296 (Linking)
VI  - 70
IP  - 1
DP  - 2004 Jul 1
TI  - Enhancing the biological activity of immobilized osteopontin using a type-1 
      collagen affinity coating.
PG  - 10-9
AB  - The covalent attachment of biomolecules onto surfaces represents a step toward 
      the improvement of biomaterial properties by providing relevant biological 
      signals of interest to the cell culture or tissue environment. The chemistries 
      involved, however, often attach proteins to the surface in a random fashion, 
      rather than the conformation or orientation most easily recognized by cells and 
      other proteins both in vitro and in vivo. An alternative approach is to take 
      advantage of natural interactions to both bind and orient a biomolecule 
      "naturally," thereby enhancing its biological activity. Type 1 collagen has been 
      shown to bind to osteopontin (OPN), a protein implicated in processes such as 
      wound healing, endothelial cell survival, and angiogenesis. This study seeks to 
      characterize, quantify, and exploit this interaction in order to present a more 
      naturally recognized form of OPN to the environment surrounding a biomaterial. 
      Binding of OPN to type 1 collagen was confirmed using Surface Plasmon Resonance 
      (SPR). Radio-iodination of OPN showed that binding to collagen was dose-dependent 
      and maximal in basic conditions. Principal component analysis of Time-of-Flight 
      Secondary Ion Mass Spectrometry (ToF-SIMS) data identified differences in OPN 
      immobilized via different techniques. Adhesion of bovine aortic endothelial cells 
      on OPN immobilized using the affinity coating was also significantly enhanced 
      compared to controls. Investigation into the in vivo relevance of this 
      immobilization method is currently underway.
CI  - Copyright 2004 Wiley Periodicals, Inc.
FAU - Martin, Stephanie M
AU  - Martin SM
AD  - Department of Bioengineering, University of Washington, Seattle, Washington 
      98195, USA.
FAU - Schwartz, Jeffrey L
AU  - Schwartz JL
FAU - Giachelli, Cecilia M
AU  - Giachelli CM
FAU - Ratner, Buddy D
AU  - Ratner BD
LA  - eng
GR  - RR01296/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biomed Mater Res A
JT  - Journal of biomedical materials research. Part A
JID - 101234237
RN  - 0 (Bicarbonates)
RN  - 0 (Coated Materials, Biocompatible)
RN  - 0 (Collagen Type I)
RN  - 0 (Excipients)
RN  - 0 (Imidazoles)
RN  - 0 (Iodine Radioisotopes)
RN  - 0 (Sialoglycoproteins)
RN  - 106441-73-0 (Osteopontin)
RN  - 25249-16-5 (Polyhydroxyethyl Methacrylate)
RN  - 63A10X1FSP (N,N-carbonyldiimidazole)
SB  - IM
MH  - Animals
MH  - Bicarbonates/chemistry
MH  - Cattle
MH  - Cell Adhesion
MH  - Cells, Cultured
MH  - Coated Materials, Biocompatible/*chemistry
MH  - Collagen Type I/*chemistry
MH  - Endothelial Cells/metabolism
MH  - Excipients
MH  - Imidazoles
MH  - Iodine Radioisotopes
MH  - Isotope Labeling
MH  - Mass Spectrometry
MH  - Osteopontin
MH  - Polyhydroxyethyl Methacrylate
MH  - Principal Component Analysis
MH  - Sialoglycoproteins/administration & dosage/analysis/*pharmacology
MH  - Surface Plasmon Resonance
EDAT- 2004/06/03 05:00
MHDA- 2004/12/23 09:00
CRDT- 2004/06/03 05:00
PHST- 2004/06/03 05:00 [pubmed]
PHST- 2004/12/23 09:00 [medline]
PHST- 2004/06/03 05:00 [entrez]
AID - 10.1002/jbm.a.30052 [doi]
PST - ppublish
SO  - J Biomed Mater Res A. 2004 Jul 1;70(1):10-9. doi: 10.1002/jbm.a.30052.