241 Isolation and characterization of the gene of plasminogen activator inhibitor 2

Kruithof, E.K.O.; Cousin, E.

doi:10.1016/0268-9499(88)90588-7

Cited by 2 publications

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“…Elevated levels of PAI-1 in plasma are associated with an increased risk ofthromboembolism suggesting a critical role of PAI-I in the in vivo regulation of fibrinolysis [2]. PAI-1 is a single-chain glycoprotein and is a member of the serine proteinase inhibitor (serpin) family [3][4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Characterization of common neoantigenic epitopes generated in plasminogen activator inhibitor‐1 after cleavage of the reactive center loop or after complex formation with various serine proteinases

Debrock

Declerck

1995

FEBS Letters

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Plasminogen activator inhibitor-I (PAl-l), an important risk factor for thrombotic diseases, is a member of the superfamily of serine proteinase inhibitors. To define structural rearrangements occurring during interaction between PAI-I and its target proteinases we have raised monoclonal antibodies against the PAI-IIt-PA complex. Thirteen out of 401 monoclonal antibodies reacted preferentially with the PAI-IIt-PA complex as compared to free PAI-I or free t-PA. Detailed characterization revealed the presence of two non-overlapping neoantigenic epitopes in the PAI-IIt-PA complex. Both neoantigenic epitopes were also exposed after complex formation between PAI-I and either urokinase-type plasminogen activator, plasmin or thrombin as well as after cleavage of the reactive site loop of non-inhibitory substrate type PAI-I variants. Thus, we have identified two neoantigenic epitopes, localized entirely in PAl-l, and commonly exposed after complex formation of active PAI-I with various proteinases or after cleavage of substrate PAI-I. These monoclonal antibodies should facilitate further studies on the mechanism of interaction between various PAI-I forms and its target proteinases.

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Section: Introductionmentioning

confidence: 99%

Characterization of common neoantigenic epitopes generated in plasminogen activator inhibitor‐1 after cleavage of the reactive center loop or after complex formation with various serine proteinases

Debrock

Declerck

1995

FEBS Letters

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“…It is considered to be the major physiological inhibitor of tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA) (Sprengers & Kluft, 1987;Alessi et al, 1988). Increased levels of PAI-1 in plasma are often associated with an increased thrombotic risk (Declerck et al, 1994;Kruithof, 1988).…”

Section: Introductionmentioning

confidence: 99%

Plasminogen activator inhibitor 1 (PAI-1) in its active conformation: crystallization and preliminary X-ray diffraction data

Willems

Rabijns

Aertgeerts

et al. 1999

Acta Crystallogr D Biol Cryst

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Because of its intrinsic lability, wild-type plasminogen activator inhibitor 1 (PAI-1) cannot be crystallized in its active conformation. Therefore, a stable variant of PAI-1 was used to retain the active conformation during crystallization. Four different crystallization conditions were evaluated in detail and two major types of crystals were detected. Whereas solutions consisting of either (i) cacodylate and sodium acetate, (ii) lithium sulfate and polyethylene glycol 4K, or (iii) imidazole, sodium chloride and sodium potassium phosphate buffer revealed thin platelet crystals, a solution (iv) containing ammonium acetate, citrate and polyethylene glycol 4K appeared to enhance the formation of clustered brush-like crystals. Crystals grown under condition (iii) were found to be suitable for X-ray data collection and consequent structural investigation. Data collection was 79.8% complete with a maximum resolution of 2.92 A. Importantly, PAI-1 retained its functional properties under all conditions.

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241 Isolation and characterization of the gene of plasminogen activator inhibitor 2

Cited by 2 publications

References 0 publications

Characterization of common neoantigenic epitopes generated in plasminogen activator inhibitor‐1 after cleavage of the reactive center loop or after complex formation with various serine proteinases

Characterization of common neoantigenic epitopes generated in plasminogen activator inhibitor‐1 after cleavage of the reactive center loop or after complex formation with various serine proteinases

Plasminogen activator inhibitor 1 (PAI-1) in its active conformation: crystallization and preliminary X-ray diffraction data

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