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Table 1 Differentially expressed proteins (p < 0.05) in seDSC and seASC with described roles on skin wound healing

From: Evaluation of secretomes derived from human dermal and adipose tissue mesenchymal stem/stromal cells for skin wound healing: not as effective as cells

Protein

seDSC

seASC

Function

A2M

–

++

Anti-protease. Inhibits fibrinolysis and coagulation processes

ABI3BP

++

+++

Inhibits proliferation and induces MSC differentiation

ANGPT1

++

–

Development, maturation, vascular stability, and angiogenesis

CCBE1

++

–

Angiogenesis and lymphoangiogenesis

CFL1

↑++

++

Cell polarity and migration

CHI3L1

+++

↑+++

Inflammation and tissue remodeling

COL15A1

++

↑++

Structural protein that stabilizes microvessels

COL5A1

+++

↑+++

Regulates the diameter of collagen fibrils

COMP

+++

↑+++

Increased in fibrotic scars; potential role in vascular remodeling

DDX42

++

–

Involved in cell viability

ECM2

–

++

Facilitates matrix organization and cellular adhesion

EIF3D

++

–

Regulates proliferation, differentiation, and apoptosis

FERMT2

++

↑++

Mediates focal adhesion. Participates in the connection between extracellular matrix and cytoskeleton, and modulates cellular morphology

GREM1/2

↑+

+

BMP antagonist. Stimulates viability, proliferation, and osteogenic and chondrogenic differentiation

HSPG2

++

+++

Regulates vascular response after injury. Anti-angiogenic action

IGFBP2

++

–

Inhibits IGF-dependent cell proliferation

IGFBP5

–

++

Controls cell survival, differentiation, and apoptosis

IL-6

++

+++

Can act as a pro- or anti-inflammatory cytokine. Immunomodulatory, angiogenic, and anti-apoptotic effects

IQGAP2

++

–

Interacts with the cytoskeleton, adhesion molecules, and signaling pathways to regulate cellular morphology and motility

LAMA1

–

++

Mediates cell adhesion, migration, and tissue organization

MMP9

++

+++

Degrades collagen IV and V, along with other extracellular proteins

NOV

++

↑++

Modulates proliferation, adhesion, migration, differentiation, and cell survival. Induces angiogenesis and acts as a receptor ligand for integrins. Stimulates fibroblast adhesion and chemotaxis and decreases the adherence of inflammatory monocytes. Suppresses MMP9 expression

PARP1

++

–

Modulates the expression of inflammatory genes and is involved in DNA repair, genomic stability, and apoptosis

PCDH7

++

–

Induces platelet degranulation, cell–cell recognition, and adhesion

PLAU

++

↑++

Functions as a protease in tissue remodeling and cell migration

PTGIS

–

++

Synthesizes prostaglandin I2, induces vasodilation, and inhibits platelet aggregation

RARRES2

–

++

Modulates inflammation, acts as a chemotactic agent for leukocytes, and exhibits antimicrobial effects on the skin. Induces adipogenesis and angiogenesis and regulates lipid and glucose metabolism

SBSN

–

++

Controls epidermal differentiation

SEMA7A

++

+++

Regulates cell migration and immune responses. Stimulates focal adhesion and the production of inflammatory cytokines

SERPINE1

+++

↑+++

Protease inhibitor

SERPINE2

↑+++

+++

Protease inhibitor

SLIT2

++

↑++

Inhibits migration, proliferation, chemotaxis, and angiogenesis

SPARC

+++

↑+++

Cell–matrix interactions. Stimulates MMP, angiogenesis, proliferation, and migration

TGFB1

+

++

Controls cell proliferation and differentiation

THBS2

+++

↑+++

Modulates adhesion and migration of mesenchymal cells

TIMP1

+++

↑+++

Inhibits MMP and apoptosis and promotes proliferation

VCAN

++

+++

Regulates cell motility, proliferation, and differentiation. May participate in intercellular signaling

VCL

↑+++

+++

Enhances cell adhesion

  1. Scores are based on peak intensity label-free quantification
  2. For proteins with similar scores but statistically different, arrows (↑) indicate in which secretome the expression was higher
  3. The functions of the proteins were obtained through searches on the online platforms http://www.uniprot.org and http://www.ncbi.nlm.nih.gov/gene
  4. LFQ: Label-free quantification; A2M: Alpha-2-macroglobulin; ABI3BP: ABI family member 3-binding protein; ANGPT1: Angiopoietin-1; BMP: Bone morphogenetic protein; CCBE1: Collagen and calcium-binding EGF domain-containing protein 1; CFL1: Cofilin-1; CHI3L1: Chitinase-3-like protein 1; COL15A1: Collagen alpha-1 (XV) chain – Restin 1,2,3,4; COL5A1: Collagen alpha-1 (V) chain; COMP: Cartilage oligomeric matrix protein; DDX42: ATP-dependent RNA helicase; ECM2: Extracellular matrix protein 2; EIF3D: Eukaryotic translation initiation factor 3 subunit D; FERMT2: Fermitin family homolog 2; GREM1/2: Gremlin 1/2; HSPG2: Heparin sulfate proteoglycan core protein; IGFBP: Insulin-like growth factor-binding protein; IL: Interleukin; IQGAP2: Ras GTPase-activating-like protein; LAMA1: Laminin alpha 1 subunit; MMP: Matrix metalloproteinase; NOV: Nephroblastoma overexpressed protein, also known as IGFBP-9; PARP1: Poly [ADP-ribose] polymerase 1; PCDH7: Protocadherin-7; PLAU: Urokinase-type plasminogen activator; PTGIS: Prostacyclin synthase; RARRES2: Retinoic acid receptor responder 2 protein; SBSN: Suprabasin; SEMA7A: Semaphorin-7A; SERPINE1: Serpin family E member 1, also known as PAI-1; SERPINE2: Serpin family E member 2; SLIT2: Slit homolog 2 protein; SPARC: Secreted protein acidic and rich in cysteine, also known as Osteonectin; TGFB1: Transforming growth factor beta 1; THBS2: Thrombospondin 2; TIMP1: Tissue inhibitor of metalloproteinases 1; VCAN: Versican core protein; VCL: Vinculin