Ann Gils
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Ann Gils has a total of 10 co-authors. Here are the top co-authors by number of shared publications:
Bonno Bouma
1 shared publicationDirk Hendriks
1 shared publicationEls Brouwers
1 shared publicationIrènE Juhan-Vague
1 shared publicationJudith Leurs
1 shared publication- Marie-Christine Alessi
Laboratory of Hematology, Centre de Référence Des Pathologies Plaquettaires, C2VN, INRAE, INSERM, Aix Marseille Université Marseille France
1 shared publication
Latest Publications
- 1 September 2004
- Published by Bentham Science Publishers Ltd. in Current Medicinal Chemistry
- Vol. 11 (17) , 2323-2334
Plasminogen Activator Inhibitor-1
Plasminogen activator inhibitor-1 (PAI-1) is an important component of the plasminogen / plasmin system as it is the main inhibitor of tissue-type and urokinase-type plasminogen activator. Consequently, PAI- 1 plays an important role in cardiovascular diseases (mainly through inhibition of t-PA) and in cell migration and tumor development (mainly through inhibition of u-PA). As a member of the serpin superfamily, PAI-1 shares important structural properties with other serpins. However, PAI-1 also exhibits unique conformational and functional properties. The current paper provides an overview of the knowledge on PAI-1 gathered since its discovery two decades ago. We are discussing (a) its structural properties and their subsequent association with the functional properties, (b) its role in a wide variety of (patho)physiological processes and (c) a number of strategies to interfere with its functional properties eventually aiming at pharmacological modulation of this risk factor.
- 1 September 2004
- Published by Bentham Science Publishers Ltd. in Current Medicinal Chemistry
- Vol. 11 (17) , 2323-2334
Plasminogen Activator Inhibitor-1
Plasminogen activator inhibitor-1 (PAI-1) is an important component of the plasminogen / plasmin system as it is the main inhibitor of tissue-type and urokinase-type plasminogen activator. Consequently, PAI- 1 plays an important role in cardiovascular diseases (mainly through inhibition of t-PA) and in cell migration and tumor development (mainly through inhibition of u-PA). As a member of the serpin superfamily, PAI-1 shares important structural properties with other serpins. However, PAI-1 also exhibits unique conformational and functional properties. The current paper provides an overview of the knowledge on PAI-1 gathered since its discovery two decades ago. We are discussing (a) its structural properties and their subsequent association with the functional properties, (b) its role in a wide variety of (patho)physiological processes and (c) a number of strategies to interfere with its functional properties eventually aiming at pharmacological modulation of this risk factor.
- 1 June 2003
- Published by Wolters Kluwer Health in Arteriosclerosis, Thrombosis, and Vascular Biology
- Vol. 23 (6) , 1122-1127
Development of a Genotype 325–Specific proCPU/TAFI ELISA
Objective— A Thr/Ile polymorphism at position 325 in the coding region of proCPU has been reported. Immunological assays, fully characterized (including genotype dependency), are required for the quantitation of proCPU levels. Methods and Results— We have generated a panel of monoclonal antibodies against human, plasma-derived proCPU. Two combinations exhibiting distinct reactivities were selected for measurement of proCPU in plasma. T12D11/T28G6-HRP yielded values of 10.1±3.1 μg/mL (mean±SD, n=86; normal donors), and T32F6/T9G12-HRP yielded values of 5.4±3.0 μg/mL. Grouping according to the 325 genotype demonstrated that T12D11/T28G6-HRP was independent to this polymorphism whereas T32F6/T9G12-HRP revealed a complete lack of reactivity with the Ile/Ile genotype (ie, 0.0±0.0, 4.2±1.7, and 7.3±2.9 μg/mL for the Ile/Ile, Ile/Thr, and Thr/Thr isoforms, respectively). Commercially available antigen assays appeared to be partially dependent on the 325 genotype (eg, 44±8.9% and 100±30% for the Ile/Ile and Thr/Thr isoforms, respectively). Conclusions— Our data demonstrate that great care should be taken when evaluating proCPU antigen values as a putative causative agent or as a diagnostic risk marker for cardiovascular events.
- 1 June 2003
- Published by Wolters Kluwer Health in Arteriosclerosis, Thrombosis, and Vascular Biology
- Vol. 23 (6) , 1122-1127
Development of a Genotype 325–Specific proCPU/TAFI ELISA
Objective— A Thr/Ile polymorphism at position 325 in the coding region of proCPU has been reported. Immunological assays, fully characterized (including genotype dependency), are required for the quantitation of proCPU levels. Methods and Results— We have generated a panel of monoclonal antibodies against human, plasma-derived proCPU. Two combinations exhibiting distinct reactivities were selected for measurement of proCPU in plasma. T12D11/T28G6-HRP yielded values of 10.1±3.1 μg/mL (mean±SD, n=86; normal donors), and T32F6/T9G12-HRP yielded values of 5.4±3.0 μg/mL. Grouping according to the 325 genotype demonstrated that T12D11/T28G6-HRP was independent to this polymorphism whereas T32F6/T9G12-HRP revealed a complete lack of reactivity with the Ile/Ile genotype (ie, 0.0±0.0, 4.2±1.7, and 7.3±2.9 μg/mL for the Ile/Ile, Ile/Thr, and Thr/Thr isoforms, respectively). Commercially available antigen assays appeared to be partially dependent on the 325 genotype (eg, 44±8.9% and 100±30% for the Ile/Ile and Thr/Thr isoforms, respectively). Conclusions— Our data demonstrate that great care should be taken when evaluating proCPU antigen values as a putative causative agent or as a diagnostic risk marker for cardiovascular events.