PMID- 23637968
OWN - NLM
STAT- MEDLINE
DCOM- 20131226
LR  - 20220310
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 8
IP  - 4
DP  - 2013
TI  - Tenascin C promiscuously binds growth factors via its fifth fibronectin type 
      III-like domain.
PG  - e62076
LID - 10.1371/journal.pone.0062076 [doi]
LID - e62076
AB  - Tenascin C (TNC) is an extracellular matrix protein that is upregulated during 
      development as well as tissue remodeling. TNC is comprised of multiple 
      independent folding domains, including 15 fibronectin type III-like (TNCIII) 
      domains. The fifth TNCIII domain (TNCIII5) has previously been shown to bind 
      heparin. Our group has shown that the heparin-binding fibronectin type III 
      domains of fibronectin (FNIII), specifically FNIII12-14, possess affinity towards 
      a large number of growth factors. Here, we show that TNCIII5 binds growth factors 
      promiscuously and with high affinity. We produced recombinant fragments of TNC 
      representing the first five TNCIII repeats (TNCIII1-5), as well as subdomains, 
      including TNCIII5, to study interactions with various growth factors. Multiple 
      growth factors of the platelet-derived growth factor (PDGF) family, the 
      fibroblast growth factor (FGF) family, the transforming growth factor beta 
      (TGF-beta) superfamily, the insulin-like growth factor binding proteins (IGF-BPs), 
      and neurotrophins were found to bind with high affinity to this region of TNC, 
      specifically to TNCIII5. Surface plasmon resonance was performed to analyze the 
      kinetics of binding of TNCIII1-5 with TGF-beta1, PDGF-BB, NT-3, and FGF-2. The 
      promiscuous yet high affinity of TNC for a wide array of growth factors, mediated 
      mainly by TNCIII5, may play a role in multiple physiological and pathological 
      processes involving TNC.
FAU - De Laporte, Laura
AU  - De Laporte L
AD  - Institute of Bioengineering, School of Life Sciences and School of Engineering, 
      Ecole Polytechnique Federale de Lausanne, Lausanne, Switzerland.
FAU - Rice, Jeffrey J
AU  - Rice JJ
FAU - Tortelli, Federico
AU  - Tortelli F
FAU - Hubbell, Jeffrey A
AU  - Hubbell JA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130418
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
RN  - 0 (Insulin-Like Growth Factor Binding Proteins)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 0 (Neurotrophin 3)
RN  - 0 (Peptide Fragments)
RN  - 0 (Proto-Oncogene Proteins c-sis)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tenascin)
RN  - 0 (Transforming Growth Factor beta1)
RN  - 0 (VEGFA protein, human)
RN  - 0 (Vascular Endothelial Growth Factor A)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
RN  - 1B56C968OA (Becaplermin)
SB  - IM
MH  - Becaplermin
MH  - Fibroblast Growth Factor 2/metabolism
MH  - HEK293 Cells
MH  - Humans
MH  - Insulin-Like Growth Factor Binding Proteins/metabolism
MH  - Intercellular Signaling Peptides and Proteins/*metabolism
MH  - Neurotrophin 3/metabolism
MH  - Peptide Fragments/metabolism
MH  - Protein Structure, Tertiary
MH  - Proto-Oncogene Proteins c-sis/*metabolism
MH  - Recombinant Proteins/metabolism
MH  - Surface Plasmon Resonance
MH  - Tenascin/*metabolism
MH  - Transforming Growth Factor beta1/metabolism
MH  - Vascular Endothelial Growth Factor A/metabolism
PMC - PMC3630135
COIS- Competing Interests: The authors have declared that no competing interests exist.
EDAT- 2013/05/03 06:00
MHDA- 2013/12/27 06:00
PMCR- 2013/04/18
CRDT- 2013/05/03 06:00
PHST- 2012/10/26 00:00 [received]
PHST- 2013/03/16 00:00 [accepted]
PHST- 2013/05/03 06:00 [entrez]
PHST- 2013/05/03 06:00 [pubmed]
PHST- 2013/12/27 06:00 [medline]
PHST- 2013/04/18 00:00 [pmc-release]
AID - PONE-D-12-33038 [pii]
AID - 10.1371/journal.pone.0062076 [doi]
PST - epublish
SO  - PLoS One. 2013 Apr 18;8(4):e62076. doi: 10.1371/journal.pone.0062076. Print 2013.