Solution studies of the quaternary structure and assembly of human von Willebrand factor

Biochemistry ◽  
1985 ◽  
Vol 24 (16) ◽  
pp. 4468-4475 ◽  
Author(s):  
Joseph Loscalzo ◽  
Michael Fisch ◽  
Robert I. Handin
Keyword(s):  
Von Willebrand Factor ◽  
Quaternary Structure ◽  
Solution Studies ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Von Willebrand Factor Multimers and the Relaxation Response: A One-Year Study

Entropy ◽  
2021 ◽  
Vol 23 (4) ◽  
pp. 447
Author(s):  
Carlo Dal Lin ◽  
Laura Acquasaliente ◽  
Sabino Iliceto ◽  
Vincenzo De Filippis ◽  
Giuseppe Vitiello ◽  
...  
Keyword(s):  
Endothelial Function ◽  
Von Willebrand Factor ◽  
Quaternary Structure ◽  
Regulatory Element ◽  
Protein Carbonyl ◽  
Relaxation Response ◽  
Study Results ◽  
One Year ◽  
Von Willebrand ◽  
Willebrand Factor

Background and aim: Mental stress represents a pivotal factor in cardiovascular diseases. The mechanism by which stress produces its deleterious ischemic effects is still under study but some of the most explored pathways are inflammation, endothelial function and balancing of the thrombotic state. In this scenario, von Willebrand factor (vWF) is a plasma glycoprotein best known for its crucial hemostatic role, also acting as key regulatory element of inflammation, being released by the activated vascular endothelium. Antistress techniques seem to be able to slow down inflammation. As we have recently verified how the practice of the Relaxation Response (RR), which counteracts psychological stress, causes favorable changes in some inflammatory genes’ expressions, neurotransmitters, hormones, cytokines and inflammatory circulating microRNAs with coronary endothelial function improvement, we aimed to verify a possible change even in serum levels of vWF. Experimental procedure: We measured vWF multimers and the total protein carbonyl contents in the sera of 90 patients with ischemic heart disease (and 30 healthy controls) immediately before and after an RR session, three times (baseline, 6 months, 12 months), during a one-year follow-up study. Results: According to our data, large vWF multimers decrease during the RR, as does the plasma total carbonyl content. Conclusion: vWF levels seem to vary rapidly between anti-inflammatory and antithrombotic behaviors dependent on psychological activity, leading to relaxation and also possibly changes in its quaternary structure.

scholarly journals Disulfide Bonds and the Quaternary Structure of Factor VIII/von Willebrand Factor

1978 ◽  
Vol 62 (3) ◽  
pp. 702-709 ◽  
Author(s):  
Richard B. Counts ◽  
Stefan L. Paskell ◽  
Susan K. Elgee
Keyword(s):  
Factor Viii ◽  
Von Willebrand Factor ◽  
Disulfide Bonds ◽  
Quaternary Structure ◽  
Von Willebrand ◽  
Willebrand Factor

Glycoprotein VI Is a Major Collagen Receptor for Platelet Activation: It Recognizes the Platelet-Activating Quaternary Structure of Collagen, Whereas CD36, Glycoprotein IIb/IIIa, and von Willebrand Factor Do Not

Blood ◽  
1998 ◽  
Vol 91 (2) ◽  
pp. 491-499 ◽  
Author(s):  
Beate Kehrel ◽  
Sonja Wierwille ◽  
Kenneth J. Clemetson ◽  
Olaf Anders ◽  
Michael Steiner ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Quaternary Structure ◽  
Glycoprotein Vi ◽  
Fibrinogen Binding ◽  
Step Model ◽  
Normal Expression ◽  
Platelet Signaling ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Specific Sequences

Abstract Simple collagen-related peptides (CRPs) containing a repeat Gly-Pro-Hyp sequence are highly potent platelet agonists. Like collagen, they must exhibit tertiary (triple-helical) and quaternary (polymeric) structure to activate platelets. Platelet signaling events induced by the peptides are the same as most of those induced by collagen. The peptides do not recognize the α2β1 integrin. To identify the signaling receptor involved, we have evaluated the response to the CRP, Gly-Lys-Hyp(Gly-Pro-Hyp)10-Gly-Lys-Hyp-Gly of platelets with defined functional deficiencies. These studies exclude a primary recognition role for CD36, von Willebrand factor (vWF), or glycoprotein (GP) IIb/IIIa. Thus, both CD36 and vWF-deficient platelets exhibited normal aggregation, normal fibrinogen binding, and normal expression of CD62 and CD63, measured by flow cytometry, in response to the peptide, and there was normal expression of CD62 and CD63 on thrombasthenic platelets. In contrast, GPVI-deficient platelets were totally unresponsive to the peptide, indicating that this receptor recognizes the Gly-Pro-Hyp sequence in collagen. GPVI-deficient platelets showed some fibrinogen binding in response to collagen but failed to aggregate and to express CD62 and CD63. Collagen, but not CRP-XL, contains binding sites for α2β1. Therefore, it is possible that collagen still induces some signaling via α2β1, leading to activation of GPIIb/IIIa. Our findings are consistent with a two-site, two-step model of collagen interaction with platelets involving recognition of specific sequences in collagen by an adhesive receptor such as α2β1 to arrest platelets under flow and subsequent recognition of another specific collagen sequence by an activatory receptor, namely GPVI.

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