SPARC/SFN interaction, suppresses type I collagen in dermal fibroblasts

Claudia Chavez-Muñoz, Ryan Hartwell, Reza B. Jalili, Seyed Mehdi Jafarnejad, Amy Lai, Layla Nabai, Abdi Ghaffari, Peymon Hojabrpour, Natalia Kanaan, Vincent Duronio, Emma Guns, Artem Cherkasov, Aziz Ghahary

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


We previously suggested that keratinocyte releasable factors might modulate the wound healing process by regulating the expression of key
extracellular matrix components such as collagenase (matrix metalloproteinase-1) and type I collagen in fibroblasts. The first one, we called it
keratinocyte-derived anti-fibrogenic factor (KDAF), identified as stratifin (SFN) also named 14-3-3s, revealing a strong collagenase activity.
However, the second factor, which we named keratinocyte-derived collagen-inhibiting factor(s) (KD-CIF) that has shown to control the
synthesis of type I collagen, was not known. Upon conducting a series of systematic protein purification methods followed by mass
spectroscopy, two proteins: secreted protein acidic rich in cystein (SPARC) and SFN were identified in keratinocyte-conditioned media. Using
co-immunoprecipitation and 3D modeling, we determined that SFN and SPARC form a complex thereby controlling the type I collagen
synthesis and expression in fibroblasts. The levels of these proteins in fibrotic tissues (animal and human) were also evaluated and a
differential expression of these proteins between normal and fibrotic tissue confirmed their potential role in development of fibrotic condition.
In conclusion, this study describes for the first time an interaction between SPARC and SFN that may have implications for the regulation
of matrix deposition and prevention of dermal fibrotic conditions such as hypertrophic scars and keloid
Original languageEnglish
Pages (from-to)2622-2632
Number of pages11
JournalJournal of Cellular Biochemistry
Issue number8
Early online date15 Jun 2012
Publication statusPublished - Aug 2012
Externally publishedYes


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