scholarly journals Perspectives series: cell adhesion in vascular biology. Role of PSGL-1 binding to selectins in leukocyte recruitment.

1997 ◽  
Vol 100 (3) ◽  
pp. 485-491 ◽  
Author(s):  
R P McEver ◽  
R D Cummings
Keyword(s):  
Cell Adhesion ◽  
Vascular Biology ◽  
Leukocyte Recruitment

Leukocyte recruitment in colon cancer: Role of cell adhesion molecules, nitric oxide, and transforming growth factor β1

2002 ◽  
Vol 122 (4) ◽  
pp. 1122-1132 ◽  
Author(s):  
Xavier Bessa ◽  
J.Ignasi Elizalde ◽  
Francesc Mitjans ◽  
Virgínia Piñol ◽  
Rosa Miquel ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Colon Cancer ◽  
Cell Adhesion ◽  
Growth Factor ◽  
Adhesion Molecules ◽  
Cell Adhesion Molecules ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β1 ◽  
Leukocyte Recruitment

scholarly journals Ephs and Ephrins in Adult Endothelial Biology

2020 ◽  
Vol 21 (16) ◽  
pp. 5623 ◽  
Author(s):  
Dianne Vreeken ◽  
Huayu Zhang ◽  
Anton Jan van Zonneveld ◽  
Janine M. van Gils
Keyword(s):  
Endothelial Cells ◽  
Endothelial Function ◽  
Vascular Development ◽  
Vascular Biology ◽  
Protein Family ◽  
Tissue Homeostasis ◽  
Leukocyte Recruitment ◽  
Eph Receptors ◽  
Ephrin Ligands

Eph receptors and their ephrin ligands are important guidance molecules during neurological and vascular development. In recent years, it has become clear that the Eph protein family remains functional in adult physiology. A subset of Ephs and ephrins is highly expressed by endothelial cells. As endothelial cells form the first barrier between the blood and surrounding tissues, maintenance of a healthy endothelium is crucial for tissue homeostasis. This review gives an overview of the current insights of the role of ephrin ligands and receptors in endothelial function and leukocyte recruitment in the (patho)physiology of adult vascular biology.

Histamine Regulates Binding of Cross-Linked Fibrinogen to Endothelium: Role of Histaminylation in Vascular Biology

Blood ◽  
2012 ◽  
Vol 120 (21) ◽  
pp. 3304-3304
Author(s):  
Thung S. Lai ◽  
Charles S Greenberg
Keyword(s):  
Endothelial Cells ◽  
Smooth Muscle ◽  
Cell Adhesion ◽  
Endothelial Cell ◽  
Vascular Smooth Muscle ◽  
Biogenic Amines ◽  
Vascular Biology ◽  
Factor Xiiia ◽  
Cross Linking

Abstract Abstract 3304 Recent studies have demonstrated that a wide variety of biogenic amines can be covalently cross-linked to intracellular and extracellular proteins. This “aminylation” reaction regulates several important reactions in vascular biology. Serotinylation of small GTPases recently was shown to regulate cell signaling events, platelet activation and promote vascular smooth muscle cell proliferation. The role of extracellular crosslinking of biogenic amines to plasma and extracellular matrix proteins is not well established and could play a role in altering transglutaminase reactions in vascular tissue. Tissue translutaminase (TGM-2) crosslinking of the a-C domain of fibrinogen has been shown to promote clustering of RGD domains, enhance binding of the cross-linked polymers to endothelial cells and promote cell adhesion. While Factor XIIIa prefers to crosslink fibrin, the TGM-2 molecule which is abundantly expressed by erythrocytes, endothelial and vascular smooth muscle cells does not show any preference for fibrin compared to fibrinogen. TGM-2 is a sulfhydryl rich calcium-dependent enzyme that could cross-link a variety of biogenic amines to fibrinogen. We investigated the preference of TGM-2 crosslinking of biogenic amines to fibrinogen in vitro and determined whether the crosslinking would modify the transglutaminase-dependent binding of fibrinogen to endothelial cells. We found histamine was the most effective primary amine inhibitor of the TGM2-mediated cross-linking reaction (Histamine > putrescine >>> serotonin, dopamine, noradrenaline). 1.25 mM histamine inhibited > 75% TGM2-mediated fibrinogen and fibrin cross-linking. The ability of TGM-2 crosslinked fibrinogen complexes to bind to confluent human umbilical vascular endothelial cell (HUVEC) was also studied. Free [125I]-fibrinogen bound to endothelial cells with low affinity, however the binding was increased ∼7 fold when fibrinogen was cross-linked by TGM2. The increase in crosslinked fibrinogen binding was dependent on TGM2 and Ca+2 concentration. Unlabeled crosslinked fibrinogen inhibited the binding by more than 85%. In contrast, unlabeled fibrinogen actually enhanced the binding 1.7 fold suggesting that fibrinogen and cross-linked fibrinogen formed multivalent complexes with cross-linked fibrinogens on the endothelial cell surface. When bound complex were eluted from HUVEC cells after binding experiments, >95% of bound materials were extensively crosslinked and could not enter a 5–15% polyacrylamide gel. In contrast, no high molecular weight material was eluted when non-crosslinked fibrinogen was used in the binding experiments. When fibrinogen was cross-linked in the presence of 8 to 500 micromolar of histamine, the binding was inhibited by ∼75 to 90 %, respectively. In summary, TGM-2 cross-linked fibrinogen showed enhanced binding to endothelial cells as previously reported for purified aC domains of fibrinogen. The binding of fibrinogen to endothelial cells is known to enhance endothelial cell adhesion and leukocyte transmigration, reactions that are involved in wound healing, angiogenesis and inflammation. The TGM-2 crosslinked fibrinogen/fibrinogen complexes may serve as proinflammatory, prothrombotic and proangiogenic factors in vivo. Histaminylation of fibrinogen by TGM-2 could provide a mechanism to regulate these vascular events. Fibrinogen could also serve to control local histamine function as only free histamine can bind to histamine receptors. Transglutaminase mediated histaminylation of fibrinogen could have multiple effects on acute and chronic inflammatory reactions. Disclosures: No relevant conflicts of interest to declare.

Platelet and Shear Rate Promote Tumor Cell Adhesion to Human Endothelial Extracellular Matrix - Absence of a Role for Platelet Cyclooxygenase

1989 ◽  
Vol 61 (03) ◽  
pp. 485-489 ◽  
Author(s):  
Eva Bastida ◽  
Lourdes Almirall ◽  
Antonio Ordinas
Keyword(s):  
Cell Adhesion ◽  
Shear Rate ◽  
Tumor Cell ◽  
Umbilical Vein ◽  
Blood Platelets ◽  
Flow Conditions ◽  
Tumor Cell Adhesion ◽  
Rate Dependent ◽  
Static Conditions

SummaryBlood platelets are thought to be involved in certain aspects of malignant dissemination. To study the role of platelets in tumor cell adherence to vascular endothelium we performed studies under static and flow conditions, measuring tumor cell adhesion in the absence or presence of platelets. We used highly metastatic human adenocarcinoma cells of the lung, cultured human umbilical vein endothelial cells (ECs) and extracellular matrices (ECM) prepared from confluent EC monolayers. Our results indicated that under static conditions platelets do not significantly increase tumor cell adhesion to either intact ECs or to exposed ECM. Conversely, the studies performed under flow conditions using the flat chamber perfusion system indicated that the presence of 2 × 105 pl/μl in the perfusate significantly increased the number of tumor cells adhered to ECM, and that this effect was shear rate dependent. The maximal values of tumor cell adhesion were obtained, in presence of platelets, at a shear rate of 1,300 sec-1. Furthermore, our results with ASA-treated platelets suggest that the role of platelets in enhancing tumor cell adhesion to ECM is independent of the activation of the platelet cyclooxygenase pathway.

scholarly journals Protease nexin-1 deficiency increases mouse hindlimb neovascularisation following ischemia and accelerates femoral artery perfusion

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Sonia Selbonne ◽  
Celina Madjene ◽  
Benjamin Salmon ◽  
Yacine Boulaftali ◽  
Marie-Christine Bouton ◽  
...  
Keyword(s):  
Femoral Artery ◽  
Capillary Density ◽  
Leukocyte Recruitment ◽  
Lower Limbs ◽  
Artery Ligation ◽  
Angiogenic Balance ◽  
Important Player ◽  
Protease Nexin ◽  
Artery Perfusion

AbstractWe previously identified the inhibitory serpin protease nexin-1 (PN-1) as an important player of the angiogenic balance with anti-angiogenic activity in physiological conditions. In the present study, we aimed to determine the role of PN-1 on pathological angiogenesis and particularly in response to ischemia, in the mouse model induced by femoral artery ligation. In wild-type (WT) muscle, we observed an upregulation of PN-1 mRNA and protein after ischemia. Angiography analysis showed that femoral artery perfusion was more rapidly restored in PN-1−/− mice than in WT mice. Moreover, immunohistochemistry showed that capillary density increased following ischemia to a greater extent in PN-1−/− than in WT muscles. Moreover, leukocyte recruitment and IL-6 and MCP-1 levels were also increased in PN-1−/− mice compared to WT after ischemia. This increase was accompanied by a higher overexpression of the growth factor midkine, known to promote leukocyte trafficking and to modulate expression of proinflammatory cytokines. Our results thus suggest that the higher expression of midkine observed in PN-1- deficient mice can increase leukocyte recruitment in response to higher levels of MCP-1, finally driving neoangiogenesis. Thus, PN-1 can limit neovascularisation in pathological conditions, including post-ischemic reperfusion of the lower limbs.

Cell adhesion on chiral surface: The role of protein adsorption

2012 ◽  
Vol 90 ◽  
pp. 97-101 ◽  
Author(s):  
Feng Zhou ◽  
Lin Yuan ◽  
Dan Li ◽  
He Huang ◽  
Taolei Sun ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Protein Adsorption ◽  
Chiral Surface
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