Determination of the Kinetic Constants of Tissue Factor/Factor Vii/Factor Viia and Antithrombin/Heparin Using Surface Plasmon Resonance

Björquist, Petter; Boström, S.

doi:10.1016/s0049-3848(97)00007-8

Cited by 38 publications

(22 citation statements)

References 24 publications

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“…39,40 The model was modified to take into account for the mass transport effect by assuming that the analyte was driven toward the sensor chip surface (A surface ) or back again to the bulk solution (A bulk ) with the same mass transfer coefficient (k t ). 41 When the analyte reaches the sensor chip surface, it binds to the ligand resulting in the formation of the ligandanalyte (LA) complex, characterized by the association rate constants (k on ) and the dissociation rate constant (k off ):…”

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confidence: 99%

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Imaging and kinetics of the bimolecular complex formed by the tumor suppressor p53 with ubiquitin ligase COP1 as studied by atomic force microscopy and surface plasmon resonance

Moscetti¹,

Bizzarri²,

Cannistraro³

2018

IJN

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p53 plays an important role in the safeguard of the genome but it is frequently downregulated mainly by E3 ubiquitin ligases among which COP1 plays an important role. The overexpression of COP1 has been reported to occur in several tumors and may be indicative of its overall oncogenic effect, which in turn might be originated by a direct interaction of COP1 with p53. Such an interaction may constitute a rewarding target for anticancer drug design strategies; therefore, a deeper understanding of its underlying molecular mechanism and kinetics is needed. The formation of a single p53–COP1 bimolecular complex was visualized by atomic force microscopy imaging on a mica substrate. The kinetic characterization of the complex, performed by atomic force spectroscopy and surface plasmon resonance, provided a K D value of ∼10 −8 M and a relative long lifetime in the order of minutes, both at the single-molecule level and in bulk solution. The surprisingly high affinity value and low dissociation rate of the p53–COP1 bimolecular complex, which is even stronger than the p53–MDM2 complex, should be considered a benchmark for designing, development and optimization of suitable drugs able to antagonize the complex formation with the aim of preventing the inhibitory effect of COP1 on the p53 oncosuppressive function.

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confidence: 99%

“…Data were fitted by using the Langmuir isotherm (Equation 5), including a term for the bulk refractive index (RI) contribution, which is assumed to be the same for all samples and which is used as the response-axis offset. 39,40 R K…”

mentioning

confidence: 99%

Imaging and kinetics of the bimolecular complex formed by the tumor suppressor p53 with ubiquitin ligase COP1 as studied by atomic force microscopy and surface plasmon resonance

Moscetti¹,

Bizzarri²,

Cannistraro³

2018

IJN

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“…The cellular initiation of coagulation by the TF ⅐ VIIa complex is tightly regulated by the plasma-derived serine protease inhibitor (serpin) antithrombin III (ATIII) 1,2 and the cell-associated Kunitz-type inhibitor TF pathway inhibitor (TFPI-1). 3,4 Whereas inhibition of TF ⅐ VIIa by ATIII results in dissociation of the complex, 5,6 binding of Kunitz-type inhibitors to TF ⅐ VIIa increases the stability of the complex, 5,7 indicating that the latter mechanism of inhibition may provide a more sustained downregulation of the TF pathway. An inhibitor homologous to TFPI-1, TFPI-2, has been identified, 8,9 but the role of TFPI-2 in the physiological regulation of TF ⅐ VIIa function is unclear.…”

mentioning

confidence: 99%

Reversible Regulation of Tissue Factor–Induced Coagulation by Glycosyl Phosphatidylinositol–Anchored Tissue Factor Pathway Inhibitor

Ott

Miyagi

Miyazaki

et al. 2000

ATVB

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Abstract-Endothelial and tumor cells synthesize tissue factor pathway inhibitor (TFPI-1), which regulates tissue factor (TF) function by TF ⅐ VIIa ⅐ Xa ⅐ TFPI-1 quaternary complex formation (where VIIa and Xa are coagulation factors) and by translocation of these complexes into glycosphingolipid-rich microdomains of the cell membrane. Recombinant TFPI-1 added exogenously to cells is targeted to a degradation pathway. This study analyzes whether quaternary complex formation with endogenous TFPI-1 results also in internalization and degradation. We demonstrate that endogenous TFPI-1 and recombinant TFPI-1 differ in their distribution on the cell surface. Recombinant TFPI-1 is found in phospholipid-and glycosphingolipid-rich membrane domains, whereas endogenous TFPI-1 preferentially localizes to glycosphingolipid-rich microdomains. On quaternary complex formation, endogenous TFPI-1 remains protease sensitive and accessible for antibodies on intact cells, demonstrating that it is not appreciably internalized. Rather, regulation of TF by TFPI-1 is restored within 12 hours, consistent with dissociation of quaternary complexes on the cell surface. Endogenous TFPI-1 can be released from the cell surface by phospholipase treatment, indicating that TFPI-1 either is a glycosyl phosphatidylinositol (GPI)-anchored protein or binds to a GPI-linked receptor. We demonstrate that expression of a recombinant GPI-anchored form of TFPI-1 targets TF ⅐ VIIa complexes to glycosphingolipid-rich membrane fractions. Thus, GPI anchoring of TFPI-1 is sufficient for regulation of TF ⅐ VIIa complex function by a pathway of reversible inhibition rather than internalization and degradation.

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“…35 Hence the hypothesis of a physiologically relevant TF-independent mechanism of action for rFVIIa was proposed because a TF-dependent mechanism could not explain the relatively high plasma concentrations of rFVIIa required for hemostatic efficacy. Since the Kd for FVIIa binding to TF is around 0.5 nM 36 and the concentration of rFVIIa required for effective hemostasis is approximately two orders of magnitude higher, it seems unlikely that a TF-rFVIIa interaction is the only mechanism responsible for improvement of hemostasis.…”

Section: Tissue Factor-independent Enhancement Of Thrombin Generationmentioning

confidence: 99%

Mechanism of Action of Recombinant Activated Factor VII

Lisman

Groot

2003

Transfus Alt Transfus Med

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Determination of the Kinetic Constants of Tissue Factor/Factor Vii/Factor Viia and Antithrombin/Heparin Using Surface Plasmon Resonance

Cited by 38 publications

References 24 publications

Imaging and kinetics of the bimolecular complex formed by the tumor suppressor p53 with ubiquitin ligase COP1 as studied by atomic force microscopy and surface plasmon resonance

Imaging and kinetics of the bimolecular complex formed by the tumor suppressor p53 with ubiquitin ligase COP1 as studied by atomic force microscopy and surface plasmon resonance

Reversible Regulation of Tissue Factor–Induced Coagulation by Glycosyl Phosphatidylinositol–Anchored Tissue Factor Pathway Inhibitor

Mechanism of Action of Recombinant Activated Factor VII

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