PMID- 10366422
OWN - NLM
STAT- MEDLINE
DCOM- 19990702
LR  - 20071114
IS  - 0014-4827 (Print)
IS  - 0014-4827 (Linking)
VI  - 249
IP  - 2
DP  - 1999 Jun 15
TI  - Alpha 2 beta 1 integrin mediates dermal fibroblast attachment to type VII
      collagen via a 158-amino-acid segment of the NC1 domain.
PG  - 231-9
AB  - Dermal fibroblasts are in apposition to type VII (anchoring fibril) collagen in
      both unwounded and wounded skin. The NC1 domain of type VII collagen contains
      multiple submodules with homology to known adhesive molecules, including
      fibronectin type III-like repeats and a potential RGD cell attachment site. We
      previously reported the structure and matrix binding properties of authentic and 
      recombinant NC1. In this study, we examined the interaction between dermal
      fibroblasts and the NC1 domain of type VII collagen. We found that both
      recombinant and authentic NC1 vigorously promoted human fibroblast attachment.
      Adhesion of fibroblasts to NC1 was dose dependent, saturable, and abolished by
      both polyclonal and monoclonal antibodies to NC1. Cell adhesion to NC1 was
      divalent cation dependent and specifically inhibited by a monoclonal antibody
      directed against the alpha2 or beta1 integrin subunits, but not by the presence
      of RGD peptides. Furthermore, the cell-binding activity of NC1 was not
      conformation dependent, since heat-denatured NC1 still promoted cell adhesion.
      Using a series of recombinant NC1 deletion mutant proteins, the cell binding site
      of NC1 was mapped to a 158-aa (residues 202-360) subdomain. We conclude that
      human dermal fibroblasts interact with the NC1 domain of type VII collagen and
      this cell-matrix interaction is mediated by the alpha2beta1 integrin and is RGD
      independent.
CI  - Copyright 1999 Academic Press.
FAU - Chen, M
AU  - Chen M
AD  - Departments of Dermatology, Northwestern University Medical School, Chicago,
      Illinois, 60611, USA.
FAU - O'Toole, E A
AU  - O'Toole EA
FAU - Li, Y Y
AU  - Li YY
FAU - Woodley, D T
AU  - Woodley DT
LA  - eng
GR  - P01 AR 41045/AR/NIAMS NIH HHS/United States
GR  - R01 A33625/PHS HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Exp Cell Res
JT  - Experimental cell research
JID - 0373226
RN  - 0 (Integrins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Receptors, Collagen)
RN  - 9007-34-5 (Collagen)
SB  - IM
SB  - S
MH  - Binding Sites
MH  - Cell Adhesion/physiology
MH  - Cells, Cultured
MH  - Collagen/chemistry/*metabolism/physiology
MH  - Extracellular Matrix/physiology
MH  - Fibroblasts/*metabolism/physiology
MH  - Humans
MH  - Integrins/antagonists & inhibitors/*physiology
MH  - Peptide Fragments/metabolism/*physiology
MH  - Receptors, Collagen
MH  - Skin/*cytology/metabolism
EDAT- 1999/06/15 00:00
MHDA- 1999/06/15 00:01
CRDT- 1999/06/15 00:00
PHST- 1999/06/15 00:00 [pubmed]
PHST- 1999/06/15 00:01 [medline]
PHST- 1999/06/15 00:00 [entrez]
AID - 10.1006/excr.1999.4473 [doi]
AID - S0014-4827(99)94473-7 [pii]
PST - ppublish
SO  - Exp Cell Res. 1999 Jun 15;249(2):231-9. doi: 10.1006/excr.1999.4473.