Changes in glycosylation and collagen binding of vitronectin in liver cirrhosis

Suzuki, Risa; Yamada, Sadako; Uchibori-Iwaki, Haruhi; Oda-Tamai, S; Kato, S.; Akamatsu, Norihiko; Yoneda, Atsuko; Ogawa, Haruko

doi:10.1016/s0531-5131(01)00456-3

Cited by 3 publications

(2 citation statements)

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“…Consistent with previous studies, 34,35 we found fibronectin (FN1)-collagen binding was positively influenced by N-glycosylation, and binding by FN1 to collagen dropped more than 2-fold following PNGase F treatment. In agreement with previous studies, 36,37 we found the PPI between vitronectin (VTN) and collagen to be enhanced 2.2-fold following sialidase treatment (Figure 3a).…”

Section: Resultssupporting

confidence: 93%

Deciphering the Roles of N-Glycans on Collagen–Platelet Interactions

Toonstra¹,

Hu²,

Zhang³

2019

J. Proteome Res.

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Collagen is a potent agonist for platelet activation, presenting itself as a key contributor to coagulation via interactions with platelet glycoproteins. The fine details dictating platelet−collagen interactions are poorly understood. In particular, glycosylation could be a key determinant in the platelet−collagen interaction. Here, we report an affinity purification coupled to a mass spectrometry-based approach to elucidate the function of N-glycans in dictating platelet−collagen interactions. By integrative proteomic and glycoproteomic analysis of collagen−platelet interactive proteins with N-glycan manipulation, we demonstrate that the interaction of platelet adhesive receptors with collagen is highly N-glycan regulated, with glycans on many receptors playing positive roles in collagen binding, with glycans on other platelet glycoproteins exhibiting inhibitory roles on the binding to collagen. Our results significantly enhance our understanding of the details of glycans influencing the platelet−collagen interaction.

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Section: Resultssupporting

confidence: 93%

Deciphering the Roles of N-Glycans on Collagen–Platelet Interactions

Toonstra¹,

Hu²,

Zhang³

2019

J. Proteome Res.

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“…The vitronectins in untreated plasma exist mainly in native inactive form and exhibit low collagen binding. Urea treatment of cirrhotic and normal plasma revealed that the ratio of active to inactive vitronectin in cirrhotic plasma increased to more than twice that in normal plasma, promoting the incorporation of vitronectin from plasma into the matrix proceeds in spite of the fact that the vitronectin concentration in cirrhotic plasma was only 70% of that in normal plasma (Suzuki, R., et al 2001). It is important to elucidate the changes in the glycosylation and biological activities of vitronectin in cirrhotic plasma and compare them with those of liver regeneration.…”

Section: Matrix Restructuring During Liver Regeneration Is Regulated mentioning

confidence: 99%

Matrix Restructuring During Liver Regeneration is Regulated by Glycosylation of the Matrix Glycoprotein Vitronectin

Ogawa¹,

Sano²,

Sobukawa³

et al. 2012

Liver Regeneration

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Deciphering the roles of N-glycans on collagen-platelet interactions

Toonstra¹,

Hu²,

Zhang³

2018

Preprint

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Collagen is a potent agonist for platelet activation, presenting itself as a key contributor to coagulation via interactions with platelet glycoproteins. The fine-details dictating plateletcollagen interactions are poorly understood. In particular, glycosylation could be a key determinant in the platelet-collagen interaction. Here we report an affinity purification coupled to mass spectrometry-based approach to elucidate the function of N-glycans in dictating plateletcollagen interactions. By integrative proteomic and glycoproteomic analysis of collagen-platelet interactive proteins with N-glycan manipulation, we demonstrate that the interaction of platelet adhesive receptors with collagen are highly N-glycan regulated, with glycans on many receptors playing positive roles on collagen binding, with glycans on other platelet glycoproteins exhibiting inhibitory roles on the binding to collagen. Our results significantly enhance our understanding of the details of glycans influencing the platelet-collagen interaction.3 Platelets are crucial mediators of primary hemostasis and endothelial repair, however, chronic pathological platelet activation also plays a critical role in progressive vascular occlusion diseases. 1 Blood vessel damage exposes collagen within the subendothelial surface which serves as the primary target site of platelet action. 1 Contact between platelet receptor proteins and nascent exposed collagen instigates platelet activation and initiates the coagulation cascade. The coagulation cascade is well defined, however, a detailed understanding of fine details dictating the platelet-collagen interaction remains elusive. Post-translational modifications, including protein glycosylation are potential key regulators of protein-protein interactions, and have been shown to contribute to platelet protein adhesion to collagen. 2 3 The majority of critical collagen binding platelet membrane proteins, including GPIbα, GPIIb/IIIa, CD36, GPVI, and GPIX, are glycoproteins. Previous studies have reported the significant impact glycosylation on plateletcollagen adhesion for both N-glycosylation (glycoprotein VI (GPVI), integrin β1 (ITGB1)), 4 5 and O-glycosylation (glycoprotein Ib α (GP1BA), integrin αIIb, integrin α5 (ITGA5), and GPVI). 6 7 8 In addition, to other mechanisms, N-and O-glycosylation have been shown to play critical roles in many facets of the hemostatic system, including, expression, liver clearance 9 10 11 12 13 14 , catalytic activity, 15 signal transduction, 16 as well as the proper function of von Willebrand factor (VWF) in the clotting process. 15 17 18 19 20 21 However, there is a conspicuous dearth of information regarding the specific role of N-glycosylation dictating the binding of platelet proteins to collagen. Studies that have analyzed the impact of glycosylation on particular platelet protein function have relied predominantly on recombinant techniques for protein expression. The glycosylation of recombinant proteins varies widely based on cell type that is used to generate the proteins...

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Changes in glycosylation and collagen binding of vitronectin in liver cirrhosis

Cited by 3 publications

References 5 publications

Deciphering the Roles of N-Glycans on Collagen–Platelet Interactions

Deciphering the Roles of N-Glycans on Collagen–Platelet Interactions

Matrix Restructuring During Liver Regeneration is Regulated by Glycosylation of the Matrix Glycoprotein Vitronectin

Deciphering the roles of N-glycans on collagen-platelet interactions

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