Structure-function relationship of human von Willebrand factor

Girma, Jean‐Pierre; Meyer, Dominique; Verweij, CL; Pannekoek, H; Sixma, JJ

doi:10.1182/blood.v70.3.605.605

Cited by 151 publications

(63 citation statements)

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“…Another region of the mosquito β integrin that shows extensive conservation when compared to β integrins from other species is located in the extracellular region between amino acids 172 -401. It includes the I-domain, a member of the A type domain superfamily, of which the von Willebrand factor is the prototype molecule (Girma et al , 1987;Verweij et al , 1986). The I type domain is a region of approximately 200 amino acids that is present in one or more copies in many proteins involved in cell-cell, cellmatrix and matrix-matrix interactions (Michishita et al , 1993), and which contains an Mg 2+ -binding site (Lee et al , 1995).…”

Section: Resultsmentioning

confidence: 99%

Beta‐integrin of Anopheles gambiae: mRNA cloning and analysis of structure and expression

Mahairaki

Lycett

Blass

et al. 2001

Insect Molecular Biology

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We have isolated an mRNA encoding a beta integrin subunit of the malaria mosquito Anopheles gambiae. Our analysis predicts a protein that is very similar to betaPS, the fruitfly orthologue. The gene is expressed during all developmental stages and it is found in all body parts, including the midgut. Finally, the expression of the gene does not seem to be modulated during blood meals, except for a substantial increase 48 h posthaematophagy, when digestion is nearly complete.

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Section: Resultsmentioning

confidence: 99%

Beta‐integrin of Anopheles gambiae: mRNA cloning and analysis of structure and expression

Mahairaki

Lycett

Blass

et al. 2001

Insect Molecular Biology

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“…Together, these N-and O-linked carbohydrate chains account for 19 percent, by weight, of each VWF monomer. 15 Finally, before secretion into the plasma, VWF dimers become assembled into long multimeric structures, which may involve as many as 100 individual VWF monomers. 16 Multimerization involves another round of disulfide bond formation, this time involving the N-terminal regions of the individual dimers.…”

Section: Synthesis and Secretionmentioning

confidence: 99%

ABO blood group determines plasma von Willebrand factor levels: a biologic function after all?

Jenkins¹,

O’Donnell²

2006

Transfusion

374

334

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For many years, an association between ABO histo-blood group and risk of thrombosis has been recognized. Blood group non-O (A, B, and AB) individuals have consistently been found to demonstrate increased incidence of both arterial and venous thrombotic disease, compared to group O individuals. This increased risk is attributable to the fact that ABO blood group influences plasma levels of a coagulation glycoprotein named von Willebrand factor (VWF). VWF levels are 25 percent higher in non-O compared to group O individuals. The mechanism by which ABO group determines plasma VWF levels has not been determined. ABO(H) carbohydrate antigenic determinants, however, are expressed on the N-linked glycan chains of circulating plasma VWF. This review will focus on the carbohydrate structures of VWF and recent studies suggesting that subtle variations in these structures (particularly differences in ABO blood group antigen expression) may have clinically significant effects on VWF proteolysis and clearance.

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“…The I domain-Uke region serves important recognition functions in several of these proteins. The Al domain of vWF binds glycoprotein lb and heparin while both the Al and A3 domains are involved in binding to collagen (Girma et al 1987). The domain in CMP may also have an important role in interaction with cartilage and proteoglycan (Argraves et al 1987b).…”

Section: Alpha Subunitsmentioning

confidence: 99%