24 research outputs found
VE-cadherin is expressed in liver sinusoidal endothelial cells in rats and humans.
<p>(A) Immunofluorescent co-staining of human liver cryosections with anti-VE-cadherin (green) and anti-CD32b (red) antibodies. (B) Immunofluorescent co-staining of rat liver cryosections with anti-VE-cadherin (green) and anti-LYVE-1 (red) antibodies. (C) Immunofluorescent co-staining of isolated rat LSECs with anti-VE-cadherin (green) and anti-Stabilin-2 (red) antibodies. Toto3 (blue) was used to counterstain the cell nuclei. Images were acquired using laser scanning confocal microscopy. Bars 11.9 ”m (A, B), 14.14 ”m (C). (D) Reverse transcriptase-PCR with mRNA isolated from rat hepatoma McA-RH7777 cell line (1), freshly isolated rat LMECs (2), and freshly isolated rat LSECs (3). Primers specific for VE-cadherin or ÎČ-actin were used.</p
Endothelial Notch signaling controls insulin transport in muscle
Abstract The role of the endothelium is not just limited to acting as an inert barrier for facilitating blood transport. Endothelial cells (ECs), through expression of a repertoire of angiocrine molecules, regulate metabolic demands in an organâspecific manner. Insulin flux across the endothelium to muscle cells is a rateâlimiting process influencing insulinâmediated lowering of blood glucose. Here, we demonstrate that Notch signaling in ECs regulates insulin transport to muscle. Notch signaling activity was higher in ECs isolated from obese mice compared to nonâobese. Sustained Notch signaling in ECs lowered insulin sensitivity and increased blood glucose levels. On the contrary, ECâspecific inhibition of Notch signaling increased insulin sensitivity and improved glucose tolerance and glucose uptake in muscle in a highâfat dietâinduced insulin resistance model. This was associated with increased transcription of Cav1, Cav2, and Cavin1, higher number of caveolae in ECs, and insulin uptake rates, as well as increased microvessel density. These data imply that Notch signaling in the endothelium actively controls insulin sensitivity and glucose homeostasis and may therefore represent a therapeutic target for diabetes
E- and N-cadherin are absent in liver sinusoidal endothelial cells.
<p>(A, B) Immunofluorescent co-staining of rat liver cryosections with anti-E-cadherin (A, green) or anti-N-cadherin (B, green) and anti-LYVE-1 (A, B, red) antibodies. (C, D) Immunofluorescent co-staining of human liver cryosections with anti-E-cadherin (C, green) or anti-N-cadherin (D, green) and anti-VE-cadherin (C, D, red) antibodies. Images were acquired using laser scanning confocal microscopy. Bars 14.14 ”m (A, B, D), 11.9 ”m (C). (E) Reverse transcriptase-PCR with mRNA of freshly isolated rat LSECs. Primers specific for VE-cadherin (1), E-cadherin (2), N-cadherin (3) or ÎČ-actin (4) were used.</p
α-catenin, ÎČ-catenin, p120-catenin, and plakoglobin co-localize with VE-cadherin in rat liver sinusoidal endothelial cells.
<p>(A-D) Immunofluorescent co-staining of rat liver cryosections with anti-α-Catenin (A, green), anti-ÎČ-Catenin (B, green), anti-p120-Catenin (C, green), anti-Plakoglobin (D, green), anti-VE -cadherin (A-D, red), anti-Stabilin-2 (A, blue), and anti-LYVE-1 (B-D, blue) antibodies. Images were acquired using laser scanning confocal microscopy. Bars 11.9 ”m.</p