scholarly journals Proteolytic Processing of Connective Tissue Growth Factor in Normal Ocular Tissues and during Corneal Wound Healing

2012 ◽  
Vol 53 (13) ◽  
pp. 8093 ◽  
Author(s):  
Paulette M. Robinson ◽  
Tyler S. Smith ◽  
Dilan Patel ◽  
Meera Dave ◽  
Alfred S. Lewin ◽  
...  
Keyword(s):  
Wound Healing ◽  
Growth Factor ◽  
Connective Tissue ◽  
Connective Tissue Growth Factor ◽  
Tissue Growth ◽  
Proteolytic Processing ◽  
Ocular Tissues ◽  
Corneal Wound Healing ◽  
Corneal Wound

164 The expression of connective tissue growth factor during wound healing

1997 ◽  
Vol 15 (2) ◽  
pp. 130
Author(s):  
N. Hayashi ◽  
T. Kakinuma ◽  
S. Kawara ◽  
K. Takehara ◽  
K. Tamaki ◽  
...  
Keyword(s):  
Wound Healing ◽  
Growth Factor ◽  
Connective Tissue ◽  
Connective Tissue Growth Factor ◽  
Tissue Growth

scholarly journals Connective tissue growth factor (CCN2) is a matricellular preproprotein controlled by proteolytic activation

2018 ◽  
Vol 293 (46) ◽  
pp. 17953-17970 ◽  
Author(s):  
Ole Jørgen Kaasbøll ◽  
Ashish K. Gadicherla ◽  
Jian-Hua Wang ◽  
Vivi Talstad Monsen ◽  
Else Marie Valbjørn Hagelin ◽  
...  
Keyword(s):  
Growth Factor ◽  
Connective Tissue ◽  
Connective Tissue Growth Factor ◽  
Osteoclast Differentiation ◽  
Tissue Growth ◽  
Proteolytic Processing ◽  
Biologically Active ◽  
Proteolytic Fragment ◽  
Proteolytic Activation ◽  
Fibroblast Migration

Connective tissue growth factor (CTGF; now often referred to as CCN2) is a secreted protein predominantly expressed during development, in various pathological conditions that involve enhanced fibrogenesis and tissue fibrosis, and in several cancers and is currently an emerging target in several early-phase clinical trials. Tissues containing high CCN2 activities often display smaller degradation products of full-length CCN2 (FL-CCN2). Interpretation of these observations is complicated by the fact that a uniform protein structure that defines biologically active CCN2 has not yet been resolved. Here, using DG44 CHO cells engineered to produce and secrete FL-CCN2 and cell signaling and cell physiological activity assays, we demonstrate that FL-CCN2 is itself an inactive precursor and that a proteolytic fragment comprising domains III (thrombospondin type 1 repeat) and IV (cystine knot) appears to convey all biologically relevant activities of CCN2. In congruence with these findings, purified FL-CCN2 could be cleaved and activated following incubation with matrix metalloproteinase activities. Furthermore, the C-terminal fragment of CCN2 (domains III and IV) also formed homodimers that were ∼20-fold more potent than the monomeric form in activating intracellular phosphokinase cascades. The homodimer elicited activation of fibroblast migration, stimulated assembly of focal adhesion complexes, enhanced RANKL-induced osteoclast differentiation of RAW264.7 cells, and promoted mammosphere formation of MCF-7 mammary cancer cells. In conclusion, CCN2 is synthesized and secreted as a preproprotein that is autoinhibited by its two N-terminal domains and requires proteolytic processing and homodimerization to become fully biologically active.

scholarly journals A novel primate model of delayed wound healing in diabetes: dysregulation of connective tissue growth factor

Diabetologia ◽  
2009 ◽  
Vol 53 (3) ◽  
pp. 572-583 ◽  
Author(s):  
S. E. Thomson ◽  
S. V. McLennan ◽  
A. Hennessy ◽  
P. Boughton ◽  
J. Bonner ◽  
...  
Keyword(s):  
Wound Healing ◽  
Growth Factor ◽  
Connective Tissue ◽  
Connective Tissue Growth Factor ◽  
Tissue Growth ◽  
Primate Model ◽  
Delayed Wound Healing
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