PMID- 9933510
OWN - NLM
STAT- MEDLINE
DCOM- 19990312
LR  - 20161124
IS  - 8756-7938 (Print)
IS  - 1520-6033 (Linking)
VI  - 15
IP  - 1
DP  - 1999 Jan-Feb
TI  - Biomimetic peptide surfaces that regulate adhesion, spreading, cytoskeletal 
      organization, and mineralization of the matrix deposited by osteoblast-like 
      cells.
PG  - 19-32
AB  - In an effort to regulate mammalian cell behavior in contact with solid material 
      surfaces, we have functionalized surfaces with different ratios of both the 
      putative cell binding (-Arg-Gly-Asp-) domain and a consensus heparan-binding 
      domain. The peptide sequences -Arg-Gly-Asp- (-RGD-) and 
      -Phe-His-Arg-Arg-Ile-Lys-Ala- (-FHRRIKA-) or mixtures of the two in the ratios of 
      75:25 (mimetic peptide surface I), 25:75 (mimetic peptide surface II), and 50:50 
      (mimetic peptide surface III) were immobilized on model surfaces using a 
      heterobifunctional cross-linker to link the peptide(s) to amine-functionalized 
      quartz surfaces. Contact angle measurements, spectroscopic ellipsometry, and 
      X-ray photoelectron spectroscopy were used to confirm the chemistry, thickness of 
      the overlayers, and surface density of immobilized peptides ( approximately 4-6 
      pmol/cm2). The degree of rat calvaria osteoblast-like cell spreading, focal 
      contact formation, cytoskeletal organization, proliferation, and mineralization 
      of the extracellular matrix (ECM) on model biomaterial surfaces was examined. 
      Mimetic peptide surface II (MPS II) and MPS III supported the highest degree of 
      cell spreading (p < 0.05), following 4 h of incubation, compared to MPS I, 
      homogeneous -RGD-, and homogeneous -FHRRIKA- grafted surfaces. Furthermore, MPS 
      I, MPS II, MPS III, and homogeneous -RGD- surfaces promoted the formation of 
      focal contacts and stress fibers by attached bone cells. The strength of bone 
      cell detachment following 30 min of incubation was significantly higher (p < 
      0.05) on MPS II surfaces compared to homogeneous -RGD- and -FHRRIKA-. However, 
      the degree of cell proliferation on the peptide surfaces were not significantly 
      different from each other (p > 0.1). Following 24 d in culture, the areas of 
      mineralized ECM formed on MPS II and MPS III surfaces were significantly (p < 
      0.05) larger than those of other surfaces. These results demonstrate that 
      utilizing peptide sequences incorporating both cell- and heparin-adhesive motifs 
      can enhance the degree of cell surface interactions and influence the long-term 
      formation of mineralized ECM in vitro.
FAU - Rezania, A
AU  - Rezania A
AD  - Division of Biological Materials, Northwestern University Dental School, 311 East 
      Chicago Avenue, Chicago, Illinois 60611-3008, USA.
FAU - Healy, K E
AU  - Healy KE
LA  - eng
GR  - R01AR43187/AR/NIAMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biotechnol Prog
JT  - Biotechnology progress
JID - 8506292
RN  - 0 (Ibsp protein, rat)
RN  - 0 (Integrin-Binding Sialoprotein)
RN  - 0 (Oligopeptides)
RN  - 0 (Sialoglycoproteins)
RN  - 78VO7F77PN (arginyl-glycyl-aspartic acid)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Bone Matrix/*physiology
MH  - *Calcification, Physiologic
MH  - Cell Adhesion
MH  - Cell Count
MH  - Cells, Cultured
MH  - Cytoskeleton/*chemistry
MH  - Integrin-Binding Sialoprotein
MH  - Molecular Sequence Data
MH  - Oligopeptides/*physiology
MH  - Osteoblasts/chemistry/*physiology
MH  - Rats
MH  - Sialoglycoproteins/*physiology
EDAT- 1999/02/06 00:00
MHDA- 1999/02/06 00:01
CRDT- 1999/02/06 00:00
PHST- 1999/02/06 00:00 [pubmed]
PHST- 1999/02/06 00:01 [medline]
PHST- 1999/02/06 00:00 [entrez]
AID - bp980083b [pii]
AID - 10.1021/bp980083b [doi]
PST - ppublish
SO  - Biotechnol Prog. 1999 Jan-Feb;15(1):19-32. doi: 10.1021/bp980083b.