Sequencing of the primary adhesion domain of bovine von Willebrand factor

Bakhshi, Meenakshi R.; Myers, Jeanne C.; Howard, Pamala S.; Soprano, Dianne Robert; Kirby, Edward P.

doi:10.1016/0167-4781(92)90171-u

Cited by 13 publications

(4 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The presence of two protein isoforms have been noted for mammalian cell Ristocetin was found to cause aggregation of HWP when incubated with COS-7 cells transfected with human A 1 -do-expressed human A 1 -domains, 20 and these are compatible with the presence of variable glycosylation patterns. 16 Se-main (0 v 72.0% { 9.8%; P õ .001) at relatively low COS-AID Blood 0013 / 5h43$$$243 10-30-97 08:11:37 blda WBS: Blood quence analyses of these respective porcine and human A 1 -comparison of the human A 1 -domains (including or excluding Cys474) showed that interactions of the A 1 -domains with domains revealed differences in putative O-linked glycosylation sites 47 ; residue 500 is changed from 500S (human) to platelets were mediated by the monomeric A 1 -domain expressed on COS-7 cells. We were able to prove that platelet 500P (pig) (Table 1).…”

Section: Cos-7 Cells Transfected Cells Were First Incubated With the Mono-mentioning

confidence: 99%

Activation of Human Platelets by the Membrane-Expressed A1 Domain of von Willebrand Factor

Esch

Crúz

Siegel

et al. 1997

Blood

View full text Add to dashboard Cite

Platelet activation and microthrombus formation are invariable features of xenograft rejection and the vascular injury observed when porcine organs are transplanted into primates. This pathological process could be mediated, at least in part, by aberrant interactions of von Willebrand Factor (vWF) associated with the donor vasculature with host platelets. Unlike human vWF, native porcine vWF (pvWF) interacts with human GPIb independently of shear stress or nonphysiological stimuli, eg, ristocetin. We therefore contrasted the potential of isolated human and porcine vWF–A1-domains to interact with human platelets in vitro. Both human and porcine vWF–A1-domains expressed as glycosyl phosphatidylinositol–linked FLAG fusion proteins on COS-7 cells induced GPIb-dependent aggregation and intracellular Ca++ uptake of platelets, independent of both the remainder of the vWF protein and additional modifying factors. Porcine A1-domains were more potent than human homologues, and in addition ristocetin could boost platelet aggregation only with the human A1-domain. Putative conformational changes in the porcine A1-domain could result in the heightened, ristocetin-independent interactions observed with human platelets and may be of importance for xenograft survival.

show abstract

Section: Cos-7 Cells Transfected Cells Were First Incubated With the Mono-mentioning

confidence: 99%

Activation of Human Platelets by the Membrane-Expressed A1 Domain of von Willebrand Factor

Esch

Crúz

Siegel

et al. 1997

Blood

View full text Add to dashboard Cite

show abstract

“…Four rat PDE4 cDNAs were obtained from Dr. M. Conti (Stanford University, Stanford, USA): a testis 1.0-kb PDE4A, a Sertoli cell 2.4-kb PDE4B, a testis 2.3-kb PDE4C and a Sertoli cell 1.9-kb PDE4D [37]. The bovine left ventricle endothelial cell 2.9-kb von Willebrand factor cDNA [38]was obtained from Dr. D. Kerbiriou-Nabias (INSERM U-143, Paris, France). The human umbilical vein endothelial cell 2.7-kb thrombomodulin cDNA [39]was obtained from Dr. F. Lanza (INSERM U-311, Strasbourg, France).…”

Section: Methodsmentioning

confidence: 99%

Cyclic Nucleotide Hydrolysis in Bovine Aortic Endothelial Cells in Culture: Differential Regulation in Cobblestone and Spindle Phenotypes

Keravis

Komas

Lugnier³

2000

J Vasc Res

View full text Add to dashboard Cite

Cyclic nucleotide phosphodiesterases (PDEs) were investigated in cultured bovine aortic endothelial cells having two phenotypes, cobblestone and spindle, representing, respectively, the resting and angiogenic phenotypes in vivo. Spindle cell homogenates displayed higher hydrolytic activities towards cAMP (52%) and cGMP (10-fold). These increases were due to: (1) increased number of spindle PDE isozymes in the cytosolic fraction (for cAMP: PDE1, PDE2, PDE3 and PDE4 compared to PDE2 and PDE4 in cobblestone; for cGMP: PDE2 and PDE5 compared to PDE2 in cobblestone); (2) increased spindle-specific activities of cytosolic and particulate PDE2, cytosolic PDE3 and particulate PDE4. These changes were associated with an increase in spindle transcripts: 7.5 kb PDE3A (6-fold) and 7.0 kb PDE4D (3-fold). Moreover, cAMP hydrolysis in the two phenotypes was differently regulated by 5 μM cGMP: 60% increase in total cAMP-PDE activity in cobblestone homogenate related to PDE2 stimulation; 30% decrease in spindle homogenate related to PDE3 inhibition. This underlines the roles played by PDE2, PDE3 and PDE5 in the cross-talk involving the two cyclic nucleotides. These changes in PDE isozyme expression along with the cross-talk between cAMP and cGMP may well modulate NO production and consequently might participate in angiogenesis, making PDEs potential targets to modulate angiogenesis.

show abstract

“…Comparison of the primary structure of the glycoprotein Ib binding domains of both human and porcine vWf revealed some differences that may account for the observed behavior [34]. A similar comparison was also done for bovine vWf [35].…”

Section: Vwf Activitymentioning

confidence: 73%

Insights from von Willebrand disease animal models

Denis

1999

Cellular and Molecular Life Sciences (CMLS)

View full text Add to dashboard Cite

von Willebrand disease is a genetic bleeding disorder that arises from abnormalities in von Willebrand factor, an adhesive glycoprotein involved in both primary hemostasis and coagulation. It is the most common inherited bleeding disorder in humans, and over the years several animal species have also been described as suffering from this disease whether through a spontaneous mutation (pigs, dogs) or a genetically engineered one (mouse). These different animal models are extremely useful in exploring the characteristics of von Willebrand disease and in testing new treatments. This review provides an update of the various von Willebrand disease models and the contribution that these models can make to a better understanding of human von Willebrand disease.

show abstract

Sequencing of the primary adhesion domain of bovine von Willebrand factor

Cited by 13 publications

References 16 publications

Activation of Human Platelets by the Membrane-Expressed A1 Domain of von Willebrand Factor

Activation of Human Platelets by the Membrane-Expressed A1 Domain of von Willebrand Factor

Cyclic Nucleotide Hydrolysis in Bovine Aortic Endothelial Cells in Culture: Differential Regulation in Cobblestone and Spindle Phenotypes

Insights from von Willebrand disease animal models

Contact Info

Product

Resources

About