Protein Disulfide Isomerase Catalyzes the Formation of Disulfide-Linked Complexes of Thrombospondin-1 with Thrombin–Antithrombin III

Milev, Youli; Essex, David W.

doi:10.1006/abbi.1998.0963

Cited by 32 publications

(37 citation statements)

References 26 publications

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“…In fact, extracellular thiol-disulfide exchange has increasingly been recognized as a way to regulate protein function. For example, vitronectin forms intermolecular disulfide bonds with thrombin (40,41) and thrombospondin with thrombin⅐anti-thrombin complex (42). Both of these reactions result in functional variations.…”

Section: Discussionmentioning

confidence: 99%

Shear-induced Disulfide Bond Formation Regulates Adhesion Activity of von Willebrand Factor

Choi

Aboulfatova

Pownall

et al. 2007

Journal of Biological Chemistry

101

140

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von Willebrand factor (VWF) is the largest multimeric adhesion ligand circulating in blood. Its adhesion activity is related to multimer size, with the ultra-large forms freshly released from the activated endothelial cells being most active, capable of spontaneously binding to platelets. In comparison, smaller plasma forms circulating in blood bind platelets only under high fluid shear stress or induced by modulators. The structure-function relationships that distinguish the two types of VWF multimers are not known. In this study, we demonstrate that some of the plasma VWF multimers contain surface-exposed free thiols. Physiological and pathological levels of shear stresses (50 and 100 dynes/cm 2 ) promote the formation of disulfide bonds utilizing these free thiols. The shear-induced thiol-disulfide exchange increases VWF binding to platelets.

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Section: Discussionmentioning

confidence: 99%

Shear-induced Disulfide Bond Formation Regulates Adhesion Activity of von Willebrand Factor

Choi

Aboulfatova

Pownall

et al. 2007

Journal of Biological Chemistry

101

140

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“…More recently, protein disulfide isomerase (PDI) secreted by activated platelets was found to catalyze disulfide exchange reactions on the platelet surface [39]. Thus, the action of PDI revealed the cryptic RGDA on TSP1 [40], catalyzing formation of a TSP1-thrombin/antithrombin complex [41]. The G domain is specific to the TSP family (TSP1-5) [42] and is involved in platelet agglutination [43] and aggregation [43].…”

Section: Structure and Functional Domains Of Tsp1mentioning

confidence: 99%

Thrombospondins: from structure to therapeutics

Bonnefoy

Moura

Hoylaerts

2008

Cell. Mol. Life Sci.

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Thrombospondin-1 (TSP1) is a multi-domain, multi-functional glycoprotein synthesized by many cells. Matricellular TSP1 modulates cell adhesion and proliferation. TSP1 is involved in angiogenesis, inflammation, wound healing and cancer. As a major platelet protein, for a long time it was postulated to control hemostasis via platelet aggregate stabilization. However, these in vitro findings have been questioned in the absence of corroborating clinical data and of obvious hemostatic defects in TSP1 gene-deficient mice.Yet, the past few years have provided indices to implicate TSP1 in hemostasis. In clinical studies, a correlation exists between a welldefined TSP1 polymorphism and a significant risk of myocardial infarction. At the same time, recent in vivo animal model data imply TSP1 in the multimer size control of von Willebrand factor, in smooth muscle cell regulation and in vascular perfusion. These findings shed new light on the role of TSP1 in hemostasis and prothrombotic vascular pathologies. (Part of a Multi-author Review).

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“…However, it now appears that this is not necessarily the case: disulfide bonds can be cleaved and reformed, and this event may have significant consequences for protein function (34). Examples of disulfide bond cleavage/ formation that have an effect on the protein function, and the factors facilitating it, are: thrombospontin-1/protein disulfide isomerase (35), plasmin/annexin II (36), and CD4/thioredoxin (37). Our model for the regulation of the oxygen binding affinity in NGB is thus another example of the potential dynamic role of disulfide bonds in proteins, affecting their structure and function.…”

Section: Table II Rates Of Ligand Binding To Ngb and Cygbmentioning

confidence: 99%

The Redox State of the Cell Regulates the Ligand Binding Affinity of Human Neuroglobin and Cytoglobin

Hamdane

Kiger

Dewilde

et al. 2003

Journal of Biological Chemistry

262

381

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Neuroglobin and cytoglobin reversibly bind oxygen in competition with the distal histidine, and the observed oxygen affinity therefore depends on the properties of both ligands. In the absence of an external ligand, the iron atom of these globins is hexacoordinated. There are three cysteine residues in human neuroglobin; those at positions CD7 and D5 are sufficiently close to form an internal disulfide bond. Both cysteine residues in cytoglobin, although localized in other positions than in human neuroglobin, may form a disulfide bond as well. The existence and position of these disulfide bonds was demonstrated by mass spectrometry and thiol accessibility studies. Mutation of the cysteines involved, or the use of reducing agents to break the S-S bond, led to a decrease in the observed oxygen affinity of human neuroglobin by an order of magnitude. The critical parameter is the histidine dissociation rate, which changes by about a factor of 10. The same effect is observed with human cytoglobin, although to a much lesser extent (less than a factor of 2). These results suggest a novel mechanism for the regulation of oxygen binding; contact with an appropriate electron donor would provoke the release of oxygen. Hence the oxygen affinity would be directly linked to the redox state of the cell.

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Protein Disulfide Isomerase Catalyzes the Formation of Disulfide-Linked Complexes of Thrombospondin-1 with Thrombin–Antithrombin III

Cited by 32 publications

References 26 publications

Shear-induced Disulfide Bond Formation Regulates Adhesion Activity of von Willebrand Factor

Shear-induced Disulfide Bond Formation Regulates Adhesion Activity of von Willebrand Factor

Thrombospondins: from structure to therapeutics

The Redox State of the Cell Regulates the Ligand Binding Affinity of Human Neuroglobin and Cytoglobin

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