Proinflammatory Mediators Enhance the Osteogenesis of Human Mesenchymal Stem Cells after Lineage Commitment.
Authors: Croes M, Oner F, Kruyt M, Blokhuis T, Bastian O, Dhert W, Alblas J
PLoS ONE, 2015;10(7):e0132781.
Species: Human
Sample Type: Whole Cells
Application: Flow
Adenosine triphosphate prevents serum deprivation-induced apoptosis in human mesenchymal stem cells via activation of the MAPK signaling pathways.
Authors: Berlier J, Rigutto S, Dalla Valle A, Lechanteur J, Soyfoo M, Gangji V, Rasschaert J
Stem Cells, 2015;33(1):211-8.
Species: Human
Sample Type: Whole Cells
Application: Flow
Human dermis harbors distinct mesenchymal stromal cell subsets.
Authors: Vaculik C, Schuster C, Bauer W, Iram N, Pfisterer K, Kramer G, Reinisch A, Strunk D, Elbe-Burger A
J. Invest. Dermatol., 2012;132(3):563-74.
Species: Human
Sample Type: Whole Cells
Application: Flow
Cultivation and characterization of cornea limbal epithelial stem cells on lens capsule in animal material-free medium.
Authors: Albert R, Vereb Z, Csomos K, Moe M, Johnsen E, Olstad O, Nicolaissen B, Rajnavolgyi E, Fesus L, Berta A, Petrovski G
PLoS ONE, 2012;7(10):e47187.
Species: Human
Sample Type: Whole Cells
Application: Flow
The impact of proliferative potential of umbilical cord-derived endothelial progenitor cells and hypoxia on vascular tubule formation in vitro.
Authors: Zhang Y, Fisher N, Newey SE
Stem Cells Dev., 2009;18(2):359-75.
Species: Human
Sample Type: Whole Cells
Application: Flow
Donor-derived mesenchymal stem cells suppress alloreactivity of kidney transplant patients.
Authors: Crop MJ, Baan CC, Korevaar SS, Ijzermans JN, Alwayn IP, Weimar W, Hoogduijn MJ
Transplantation, 2009;87(6):896-906.
Species: Human
Sample Type: Whole Cells
Application: Flow

Endoglin (CD105) is a 90 kDa type I transmembrane glycoprotein of the zona pellucida (ZP) family of proteins (1-3). Endoglin and betaglycan/T beta RIII are type III receptors for TGF beta superfamily ligands, sharing 71% aa identity in the transmembrane (TM) and cytoplasmic domains. Endoglin is highly expressed on proliferating vascular endothelial cells, chondrocytes, and syncytiotrophoblasts of term placenta, with lower amounts on hematopoietic, mesenchymal and neural crest stem cells, activated monocytes, and lymphoid and myeloid leukemic cells (2-5). Human Endoglin cDNA encodes 658 amino acids (aa) including a 25 aa signal sequence, a 561 aa extracellular domain (ECD) with an orphan domain and a two-part ZP domain, a TM domain and a 47 aa cytoplasmic domain (1-3). An isoform with a 14 aa cytoplasmic domain (S-endoglin) can oppose effects of long (L) Endoglin (6, 7). The human Endoglin ECD shares 65-72% aa identity with mouse, rat, bovine, porcine and canine Endoglin. Endoglin homodimers interact with TGF-beta 1 and TGF-beta 3 (but not TGF-beta 2), but only after binding T beta RII (8). Similarly, they interact with activin-A and BMP-7 via activin type IIA or B receptors, and with BMP-2 via BMPR-1A/ALK-3 or BMPR-1B/ALK-6 (9). BMP-9, however, is reported to bind Endoglin directly (10). Endoglin modifies ligand-induced signaling in multiple ways. For example, expression of Endoglin can inhibit TGF-beta 1 signals but enhance BMP7 signals in the same myoblast cell line (11). In endothelial cells, Endoglin inhibits T beta RI/ALK5, but enhances ALK1-mediated activation (12). Deletion of mouse Endoglin causes lethal vascular and cardiovascular defects, and human Endoglin haploinsufficiency can a cause the vascular disorder, hereditary hemorrhagic telangiectasia type I (13, 14). These abnormalities confirm the essential function of Endoglin in differentiation of smooth muscle, angiogenesis, and neovascularization (2-4, 12-14). In preeclampsia of pregnancy, high levels of proteolytically generated soluble Endoglin and VEGF R1 (sFLT1), along with low placental growth factor (PlGF), are pathogenic due to antiangiogenic activity (15).

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