scholarly journals Noncanonical effects of vasopressin in angiogenesis

2019 ◽  
Vol 23 (5) ◽  
pp. 575-581
Author(s):  
I. I. Khegay
Keyword(s):  
Hyaluronic Acid ◽  
Von Willebrand Factor ◽  
Secretory Activity ◽  
Αvβ3 Integrin ◽  
Membrane Glycoproteins ◽  
Adhesive Properties ◽  
Intercellular Matrix ◽  
And Migration ◽  
Von Willebrand ◽  
Willebrand Factor

The molecular action of vasopressin depends on the localization of hormonal receptors. The basic physiological effects of vasopressin are manifested in the blood vasculature, renal inner medulla and brain. To date, new information concerning the tissue-specific spreading of vasopressin receptors has been accumulated, and it needs to be summarized. Platelets and endotheliocytes expressing V1a and V2 receptor types, respectively, are related to less investigated targets of the hormone. Vasopressin induces the initial reversible stage of platelet activation, required for interaction with intercellular matrix proteins. Platelet adhesion on endothelium activates cellular secretion of growth factors and enzymes for intercellular matrix glucosamine metabolism. Platelet hyaluronidase HYAL2 hydrolyses high-molecular hyaluronic acid to shorter fragments. Unlike intact hyaluronic acid with a molecular weight of several megadaltons, generally showing distinctive antiangiogenic properties, intermediate fractions of hyaluronan hydrolysis in a range from 2.5 to 200 kilodaltons have a stimulating effect on angiogenesis. Intercellular contacts between platelets and endotheliocytes are stabilized due to adhesive transmembrane glycoprotein PECAM-1 interaction. Resulting PECAM-1 heterodimers acquire conformation with high affinity to integrins αvβ3. Integrin activation forms contact links between endothelium and fibrillar proteins. Activated endotheliocytes secrete von Willebrand factor and P-selectin. These proteins are accumulated in Weibel–Palade bodies. Vasopressin stimulates cAMP-dependent ACAP-regulated exocytosis of Weibel–Palade bodies. von Willebrand factor possesses adhesive properties and additionally accelerates interaction of cells with the intercellular matrix. Adhesion on fibrillar collagen and membrane glycoproteins in cooperation with effects of PECAM-1–αvβ3 integrin complexes fixes cell aggregates in the surrounding interstitium and promotes proliferating endotheliocyte migration in according to the direction of local growth factor gradients during angiogenesis. Neurohormonal regulation of platelet and endotheliocyte secretory activity functionally link proliferation and migration of endotheliocytes during angiogenesis and integrate it according to the adaptive capacity of the entire organism.

Role of Platelet Membrane Glycoproteins and Von Willebrand Factor in Adhesion of Platelets to Subendothelium and Collagen

1987 ◽  
Vol 516 (1 Blood in Cont) ◽  
pp. 52-65 ◽  
Author(s):  
KJELL S. SAKARIASSEN ◽  
EDITH FRESSINAUD ◽  
JEAN-PIERRE GIRMA ◽  
DOMINIQUE MEYER ◽  
HANS R. BAUMGARTNER
Keyword(s):  
Von Willebrand Factor ◽  
Platelet Membrane ◽  
Membrane Glycoproteins ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Adhesion Of Platelets

scholarly journals Adhesive properties of the beta 3 integrins: comparison of GP IIb-IIIa and the vitronectin receptor individually expressed in human melanoma cells.

1991 ◽  
Vol 113 (2) ◽  
pp. 451-461 ◽  
Author(s):  
N Kieffer ◽  
L A Fitzgerald ◽  
D Wolf ◽  
D A Cheresh ◽  
D R Phillips
Keyword(s):  
Von Willebrand Factor ◽  
Cell Attachment ◽  
Melanoma Cells ◽  
Human Melanoma ◽  
Adhesive Properties ◽  
Vitronectin Receptor ◽  
Hel Cells ◽  
Alpha V Beta 3 ◽  
Von Willebrand ◽  
Willebrand Factor

Glycoprotein IIb-IIIa (alpha IIb beta 3) and the vitronectin receptor (alpha v beta 3), two integrins that share the common beta 3 subunit, have been reported to function as promiscuous receptors for the RGD-containing adhesive proteins fibrinogen, vitronectin, fibronectin, von Willebrand factor, and thrombospondin. The present study was designed to establish a cell system for the expression of either GP IIb-IIIa or the vitronectin receptor in an otherwise identical cellular environment and to compare the adhesive properties of these two integrins with those of native GP IIb-IIIa and the vitronectin receptor constitutively expressed in HEL cells or platelets. M21 human melanoma cells lack GP IIb-IIIa and use the vitronectin receptor to attach to vitronectin, fibrinogen, fibronectin, and von Willebrand factor. To study the functional properties of GP IIb-IIIa in these cells, we transfected GP IIb into M21-L cells, a variant of M21 cells (Cheresh, D.A., and R.C. Spiro. 1987. J. Biol. Chem. 262:17703-17711), which lack the expression of functional alpha v and are therefore unable to attach to vitronectin, fibrinogen, and von Willebrand factor. Transfectants expressing GP IIb were isolated by immunomagnetic beads and surface expression of the GP IIb-IIIa complex was documented by FACS analysis and immunoprecipitation experiments performed with 125I-labeled M21-L/GP IIb cells. Comparative functional studies demonstrated that GP IIb-IIIa expressed in M21-L/GPIIb cells as well as native GP IIb-IIIa constitutively expressed in HEL-5J20 cells (an HEL variant lacking alpha v beta 3) mediated cell attachment to immobilized fibrinogen, but not to vitronectin or von Willebrand factor, whereas the vitronectin receptor expressed in M21 cells and HEL-AD1 cells (an HEL variant expressing alpha v beta 3) mediated cell attachment to fibrinogen, vitronectin, and von Willebrand factor. Similarly, PGl2-treated resting platelets attached to immobilized fibrinogen but not to vitronectin or von Willebrand factor, and this attachment could be inhibited by mAb A2A9 (directed against a functional site on the GP IIb-IIIa complex). However, in contrast to platelets, which adhered to vitronectin and von Willebrand factor after stimulation by thrombin or PMA, activation of the protein kinase C pathway in M21-L/GP IIb or HEL cells did not induce cell adhesion to vitronectin or von Willebrand factor.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals Adhesive properties of the carbohydrate-modified von Willebrand factor (CHO-vWF)

Blood ◽  
1988 ◽  
Vol 71 (4) ◽  
pp. 947-952 ◽  
Author(s):  
AB Federici ◽  
C De Romeuf ◽  
PG De Groot ◽  
B Samor ◽  
R Lombardi ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
Platelet Rich Plasma ◽  
Significant Loss ◽  
Total Carbohydrate ◽  
Adhesive Properties ◽  
Normal Platelet ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract In this cooperative study, we explored the role of the carbohydrate moiety (CHO) of von Willebrand factor (vWF) in supporting platelet adhesion. Because of previous discrepant results, all purification steps and CHO modifications by various enzymes were critically evaluated. Under our conditions, CHO-modified vWF preparations contained less than 5% of the initial sialic acid ([Neu]-ase-vWF) and less than 45% ([Neu-Gal]-ase-vWF) or 21% ([Neu-Gal-eF]-ase-vWF) of the D-galactose. These preparations usually showed increased electrophoretic mobility but no significant loss of high-mol-wt multimers when proteolysis had been prevented. Some degree of proteolysis was noted in some carbohydrate-modified vWFs, but the degree of degradation observed did not correlate with the removal of D- galactose. Platelet adhesion to various matrices increased after removal of the terminal sialic acid ([Neu]-ase-vWF) and approximately 45% of the D-galactose ([Neu-Gal]-ase-vWF), but returned to normal values when greater than 70% of the total carbohydrate had been removed by endoglycosidase F [Neu-Gal-ef]-ase-vWF). These changes in reactivity were also reflected in the spontaneous aggregation in normal platelet- rich plasma (PRP) after CHO removal.

scholarly journals Further characterization of platelet-type von Willebrand's disease in Japan

Blood ◽  
1984 ◽  
Vol 64 (6) ◽  
pp. 1254-1262 ◽  
Author(s):  
H Takahashi ◽  
M Handa ◽  
K Watanabe ◽  
Y Ando ◽  
R Nagayama ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Platelet Rich Plasma ◽  
Sodium Dodecyl ◽  
Membrane Glycoproteins ◽  
Glycoprotein Ib ◽  
Normal Platelet ◽  
Platelet Receptor ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract We studied four patients who showed aggregation of platelets in platelet-rich plasma at lower concentrations of ristocetin than those required for normal platelet-rich plasma and who demonstrated an increased capacity of the platelets to bind normal von Willebrand factor. The four patients were from two Japanese families. Platelets from one family aggregated spontaneously in vitro, and platelets from both families aggregated upon the addition of normal plasma and cryoprecipitate, in the absence of ristocetin or other agonists. Analysis of the multimeric composition of von Willebrand factor by sodium dodecyl sulfate-agarose gel electrophoresis revealed a decrease in large multimers or a decrease in both large and intermediate multimers in plasma, but normal multimers in platelets. 1-Deamino-[8-D- arginine]-vasopressin caused by an immediate appearance of larger multimers in plasma, followed by the rapid disappearance of these multimers from circulating plasma. Analysis of platelet membrane glycoproteins from the patients showed that there were two distinct bands in the glycoprotein I region; one migrated in a slower region and the other in a faster region than normal glycoprotein Ib. We suggest that the platelet receptor abnormality in these patients is related to this abnormality of glycoprotein Ib.

THE EFFECT OF PHORBOL DIESTERS AND INTERLEUKINS ON THE SECRETION OF VON WILLEBRAND FACTOR BY HUMAN ENDOTHELIAL CELLS IN CULTURE

1987 ◽  
Author(s):  
J C Giddings ◽  
L Shall
Keyword(s):  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Umbilical Vein ◽  
Interleukin 1 ◽  
Interleukin 2 ◽  
Morphological Evidence ◽  
Adhesive Properties ◽  
Umbilical Vein Endothelial Cells ◽  
Von Willebrand ◽  
Willebrand Factor

Human umbilical vein endothelial cells (EC) were cultured in the presence of 4p-phorbol 12-myristate 13-acetate (PMA, 10ug/l), interleukin 1 (IL-1, 1 unit/ml) and interleukin 2 (IL-2, 1 unit/ml), and secretion of von Willebrand factor activity (vWF, Ristocetin co-factor) and von Willebrand factor antigen (vWFAG, ELISA Technique) measured at intervals. Confluent control EC were treated with PMA, IL-1 and IL-2, and the supernatant medium assayed for release of vWF and vWFAg. Treated cells were also examined for vWFAg by immuno-fluorescence. The levels of both vWF and vWFAg in cultures containing IL-1 were significantly higher than those in control cultures after 5-6 days growth. Moreover, vWF and vWFAg increased significantly in the supernatant of confluent control EC incubated further in the presence of IL-1. Furthermore, the characteristic fluorescence pattern of endothelial vWFAg was markedly reduced in EC treated with IL-1. The levels of vWF and vWFAg in cultures containing PMA were also significantly higher than those of control cultures. In these conditions, however, the growth of cells appeared to be enhanced, and confluence was observed after about 6 days in the presence of PMA compared to 9 - 10 days in control cultures. The mean levels of vWF and vWFAg in the supernatant of EC incubated with PMA were higher than the control values but the differences were not statistically significant. Immunofluorescence of PMA-treated cells suggested that vWFAg might be less granular than in control cells but the differences were not as marked as those seen with IL-1. The results of all assays in the presence of IL-2 were not significantly different from those of control cells. In all instances no morphological evidence of endothelial injury was observed and more than 90% of cells remained viable at the termination of cultures. The results indicated that the synthesis and release of vWF were increased in the presence of PMA, and secretion of vWF was stimulated by IL-1. The data suggest that secreted vWF might contribute to the previously reported enhanced procoagulant and adhesive properties of EC treated with these substances.

Retention Test Homburg To Monitor the Adhesive Properties of von Willebrand Factor after Substitution or Desmopressin Therapy

2005 ◽  
Vol 31 (04) ◽  
pp. 441-448
Author(s):  
J. Ulrich Wieding ◽  
Juliane Matern ◽  
Heinz Köstering ◽  
Cornelia Wermes ◽  
Ernst Wenzel
Keyword(s):  
Von Willebrand Factor ◽  
Retention Test ◽  
Adhesive Properties ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Phospholipase abolishes the effect of stimulated platelets on the thrombin activation of factor VIII

Blood ◽  
1988 ◽  
Vol 71 (1) ◽  
pp. 173-177
Author(s):  
ME Rick ◽  
DM Krizek
Keyword(s):  
Factor Viii ◽  
Von Willebrand Factor ◽  
Calcium Ionophore ◽  
Platelet Membrane ◽  
Activate Factor ◽  
Membrane Glycoproteins ◽  
Membrane Phospholipids ◽  
Thrombin Activation ◽  
Von Willebrand ◽  
Willebrand Factor

Factor VIII functions as a cofactor in the intrinsic coagulation pathway and must first be activated to function optimally in this capacity. Low concentrations of thrombin activate factor VIII, and the presence of stimulated platelets is known to enhance the activation of factor VIII complexed to von Willebrand factor. The current studies show that platelets stimulated by thrombin, collagen, or calcium ionophore will increase the activation of isolated factor VIII by thrombin. Ongoing platelet release is not necessary for the enhanced factor VIII activation, nor is platelet von Willebrand factor or platelet membrane glycoproteins Ib or IIb/IIIa. Platelet membrane phospholipids, on the other hand, are important for the enhanced activation of factor VIII by thrombin because the effect of stimulated platelets is abolished by incubation of the stimulated platelets with phospholipases. These results suggest that the enhanced activation of factor VIII by thrombin in the presence of stimulated platelets may be mediated by factor VIII binding to platelet phospholipid or to a receptor whose functional integrity is dependent on surrounding membrane phospholipid.

scholarly journals Platelet-collagen interaction: inhibition by ristocetin and enhancement by von Willebrand factor-platelet binding

Blood ◽  
1986 ◽  
Vol 68 (4) ◽  
pp. 927-937
Author(s):  
FM LaDuca ◽  
RE Bettigole ◽  
WR Bell ◽  
EB Robson
Keyword(s):  
Platelet Aggregation ◽  
Von Willebrand Factor ◽  
Platelet Rich Plasma ◽  
Platelet Membrane ◽  
Type I ◽  
Membrane Glycoproteins ◽  
Platelet Binding ◽  
Von Willebrand ◽  
Willebrand Factor

The contribution of von Willebrand factor (vWF)-platelet binding to platelet-collagen interaction was examined in vitro. The binding of vWF to platelets was mediated and regulated by ristocetin. Subthreshold concentrations of ristocetin (less than or equal to 1 mg/mL), insufficient to cause ristocetin-induced platelet aggregation (RIPA), were added to platelet-rich plasma (PRP) prior to the addition of collagen. The collagen-induced platelet aggregation (CIPA) was modified by ristocetin and the degree of alteration was dependent on the ristocetin concentration. Response as a function of ristocetin concentration was designated the Collagen-Platelet Aggregation Response (CoI-PAR). In normal PRP the CoI-PAR was a progressive inhibition followed by decreasing inhibition and then an enhanced response. The enhanced response occurred over a narrow range of ristocetin concentrations (0.8 to 1.0 mg/mL). In the absence of vWF (severe von Willebrand's disease, Type I, vWF less than 1%) the CoI-PAR was a progressive, eventually complete inhibition with no enhanced response (with ristocetin concentrations up to 3.0 mg/mL). With addition of vWF to this PRP an enhanced response was observed at a ristocetin concentration inversely proportional to the vWF level. PRP from a patient with severe Hemophilia A showed a response within the normal range. Subthreshold ristocetin did not cause plasma protein precipitation or platelet release of 3H-serotonin, nor induce micro platelet aggregate formation. Digestion of platelet membrane glycoproteins (GP(s] with chymotrypsin demonstrated that upon removal of GPI, RIPA was absent, CIPA retained and the CoI-PAR was progressive inhibition, with no enhancement. With removal of GPs I, II, and III, RIPA, CIPA, and the CoI-PAR were absent. A dose-response 125I-vWF- platelet binding occurred with increasing ristocetin concentrations which was unchanged by the addition of collagen. These results demonstrated that ristocetin-platelet association inhibited CIPA, and vWF-platelet binding enhanced platelet-collagen adhesion and platelet aggregation. The in vitro-enhanced CIPA represents a vWF-dependent aggregation of sufficient magnitude to overcome the inhibitory effect of ristocetin. These studies demonstrate an influential interaction of ristocetin, vWF, and collagen with the platelet membrane and imply an important hemostatic contribution of vWF-platelet binding in platelet- collagen interaction.

Purification of the Porcine Platelet GP IIb-IIIa Complex and the Propolypeptide of von Willebrand Factor

1998 ◽  
Vol 80 (08) ◽  
pp. 302-309 ◽  
Author(s):  
Teresa Royo ◽  
Matilde Vidal ◽  
Lina Badimon
Keyword(s):  
Molecular Weight ◽  
Von Willebrand Factor ◽  
Platelet Adhesion ◽  
Membrane Glycoproteins ◽  
Single Chain ◽  
Inhibitory Effects ◽  
Adhesive Proteins ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Human Receptor

SummaryPlatelet membrane glycoproteins (GP) are involved in platelet adhesion and aggregation. The glycoprotein IIb-IIIa complex (GP IIbIIIa) is a Ca2+-dependent heterodimer that binds fibrinogen and other adhesive proteins, thereby mediating platelet aggregation and adhesion. We have purified two major glycoproteins from pig platelets by Concanavalin A-Sepharose, Heparin-Sepharose and Sephacryl S-300 HR chromatography (Fitzgerald et al. Anal Biochem, 1985): i) the GP IIb-IIIa complex, GP IIb Mr = 140,000 and GP IIIa a single chain of Mr = 95,000-100,000; and ii) a predominant glycoprotein of high molecular weight, the propolypeptide of von Willebrand factor (Mr = 80,000-100,000). Western-blot analysis of the purified GP IIb-IIIa showed that only certain monoclonal antibodies against the human receptor specifically recognize the porcine complex. Differences between the porcine and human GP IIb-IIIa glycoproteins could partially explain the decreased inhibitory effects of GP IIb/IIIa-antagonists (against the human receptor) in porcine platelets.

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