scholarly journals Primary structure of the majorO-glycosidically linked carbohydrate unit of human von Willebrand factor

1989 ◽  
Vol 6 (3) ◽  
pp. 263-270 ◽  
Author(s):  
Bruno Samor ◽  
Jean-Claude Michalski ◽  
Claudine Mazurier ◽  
Maurice Goudemand ◽  
Pieter De Waard ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Primary Structure ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Carbohydrate Unit

Primary structure of the propeptide and factor VIII-binding domain of bovine von Willebrand factor

1997 ◽  
Vol 1339 (1) ◽  
pp. 4-8 ◽  
Author(s):  
Nathalie Janel ◽  
Anne-Sophie Ribba ◽  
Ghislaine Chérel ◽  
Danièle Kerbiriou-Nabias ◽  
Dominique Meyer
Keyword(s):  
Factor Viii ◽  
Von Willebrand Factor ◽  
Primary Structure ◽  
Binding Domain ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals Primary structure of a new tetraantennary glycan of the N-acetyllactosaminic type isolated from human factor VIII/von Willebrand factor

1986 ◽  
Vol 158 (2) ◽  
pp. 295-298 ◽  
Author(s):  
Bruno SAMOR ◽  
Jean-Claude MICHALSKI ◽  
Henri DEBRAY ◽  
Claudine MAZURIER ◽  
Maurice GOUDEMAND ◽  
...  
Keyword(s):  
Factor Viii ◽  
Von Willebrand Factor ◽  
Primary Structure ◽  
Human Factor ◽  
Human Factor Viii ◽  
Von Willebrand ◽  
Willebrand Factor

scholarly journals The complete primary structure of type XII collagen shows a chimeric molecule with reiterated fibronectin type III motifs, von Willebrand factor A motifs, a domain homologous to a noncollagenous region of type IX collagen, and short collagenous domains with an Arg-Gly-Asp site.

1991 ◽  
Vol 115 (1) ◽  
pp. 209-221 ◽  
Author(s):  
M Yamagata ◽  
K M Yamada ◽  
S S Yamada ◽  
T Shinomura ◽  
H Tanaka ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Von Willebrand Factor ◽  
Primary Structure ◽  
Extracellular Proteins ◽  
Type Iii ◽  
Fibronectin Type Iii ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Fibronectin Type ◽  
Complete Primary Structure

Extracellular matrix molecules are generally categorized as collagens, elastin, proteoglycans, or other noncollagenous structural/cell interaction proteins. Many of these extracellular proteins contain distinctive repetitive modules, which can sometimes be found in other proteins. We describe the complete primary structure of an alpha 1 chain of type XII collagen from chick embryonic fibroblasts. This large, structurally chimeric molecule identified by cDNA analysis combines previously unrelated molecular domains into a single large protein 3,124 residues long (approximately 340 kD). The deduced chicken type XII collagen sequence starts at the amino terminus with one unit of the type III motif of fibronectin, which is followed by one unit homologous to the von Willebrand factor A domain, then one more fibronectin type III module, a second A domain from von Willebrand factor, 6 units of type III motif and a third A domain, 10 consecutive units of type III motif and a fourth A domain, a domain homologous to the NC4 domain peptide of type IX collagen, and finally two short collagenous regions previously described as part of the partially sequenced collagen type XII molecule; an Arg-Gly-Asp potential cell adhesive recognition sequence is present in a hydrophilic region at the terminus of one collagenous domain. Antibodies raised to type XII collagen synthesized in a bacterial expression system recognized not only previously reported bands (220 kD et cetera) in tendons, but also bands with apparently different molecular sizes in fibroblasts and 4-d embryos. The antibodies stained a wide variety of extracellular matrices in embryos in patterns distinct from those of fibronectin or interstitial collagens. They prominently stained extracellular matrix associated with certain neuronal tissues, such as axons from dorsal root ganglia and neural tube. These studies identify a novel chimeric type of molecule that contains both adhesion molecule and collagen motifs in one protein. Its structure blurs current classification schemes for extracellular proteins and underscores the potentially large diversity possible in these molecules.

Primary Structure of the Factor VIII Binding Domain of Human, Porcine and Rabbit von Willebrand Factor

1993 ◽  
Vol 194 (3) ◽  
pp. 1019-1024 ◽  
Author(s):  
J.M. Lavergne ◽  
Y.C. Piao ◽  
V. Ferreira ◽  
D. Kerbiriounabias ◽  
B.R. Bahnak ◽  
...  
Keyword(s):  
Factor Viii ◽  
Von Willebrand Factor ◽  
Primary Structure ◽  
Binding Domain ◽  
Von Willebrand ◽  
Willebrand Factor

Comparison of the primary structure of the functional domains of human and porcine von Willebrand factor that mediate platelet adhesion

1992 ◽  
Vol 182 (2) ◽  
pp. 561-568 ◽  
Author(s):  
Bruce R. Bahnak ◽  
Jean-Maurice Lavergne ◽  
Valérie Ferreira ◽  
Danièle Kerbiriou-Nabias ◽  
Dominique Meyer
Keyword(s):  
Von Willebrand Factor ◽  
Primary Structure ◽  
Platelet Adhesion ◽  
Functional Domains ◽  
Von Willebrand ◽  
Willebrand Factor
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