NEWS

    Young Investigator Awards

    To honour the contributions of Désiré Collen to research on fibrinolysis, proteolysis and thrombolysis, the International Society for Fibrinolysis and Proteolysis (ISFP) has decided to create “D. Collen Young Investigator Awards”, that will be awarded every two years at the occasion of the congress of the ISFP.

    The following criteria were set:

  • Restricted to PhD/young post-doc level (under 40 years).
  • Five abstracts submitted to the congress are selected by the scientific program committee (on the basis of grading and contents). The first authors of submitted abstracts will have the option to indicate whether they wish to compete for one of these awards.
  • The selected abstracts will be presented in a special oral communications session.
  • After this session, the scientific program committee will select one abstract as winner, receiving 5000 USD, whereas the 4 others will each receive 1000 USD.
  • The awards were given for the first time at the ISFP congress in Amsterdam (August 24-28, 2010) and will be given again at the 21st Congress of the ISFP in Brighton (July 1-5, 2012).

    For more information, contact the Executive Director of the ISFP.

    • Society Journal

    The Journal of Thrombosis and Haemostasis (ISTH) is the official journal of the ISFP (see Editorial by R.L. Medcalf and P.M. Mannuci in J.Thromb.Haemostasis 4, 2006)


    Future ISFP Congresses

    The 21st International Congress of the ISFP will be held in Brighton, July 1-5, 2012, President Colin Longstaff.
    Proposals to host the 22th International Congress of the ISFP in 2014 can be submitted to the Executive Director.

    Membership of ISFP
    Please invite your colleagues to join the ISFP, which is a non-profit organization that promotes all aspects of research in fibrinolysis and proteolysis. The membership fee entitles you to a reduced registration fee at our international congress. Membership application forms are available at the ISFP Web site.

    The membership fee (60 euro or 100 euro for 2 years) gives you lower registration fees at our congresses and several other advantages. Free membership is available for scientists under 30 years.


    Your views
    Please feel free to contact the Executive Director or any member of Council with your views on the society. The next meeting of Council will be during the ISTH Congress in Kyoto, 2011.

    ISFP Bylaws

    ISFP membership invitation

    Obituary: Michael Ernest Nesheim, February 5, 1945 – June 4, 2011

    On June 4, 2011 Michael Ernest Nesheim, a colleague of much renown in the field of thrombosis, haemostasis and fibrinolysis, passed away after a brief battle with cancer.

    Michael received his Ph.D. from the University of Minnesota in 1977 in the field of metabolic biochemistry. Unfortunately for Michael, while working to complete his doctoral thesis his funding was cut. Since Michael had a young family to support, he accepted a job as a half time technician in the laboratory of Kenneth Mann, who at the time was studying prothrombin at the Mayo clinic in Rochester Minnesota. During this initial period in the Mann lab, Michael was constantly encouraged by Ken to complete his dissertation and find a suitable postdoctoral position. During Christmas break, while both Michael and Ken were working late, Michael entered Ken’s office with a tube gel containing a single band. This band represented the successful isolation of factor V and in response to this news Ken declared that Michael had found a postdoctoral position. In the following years Michael continued to research factor V and the prothrombinase complex. Among his many achievements were the isolation and characterization of factor V (1), its activation by thrombin to fVa (2), the formation and function of prothrombinase and the development of an empirically validated mathematical model that described the kinetics of the membrane bound complex (3). His efforts were rewarded by his selection as the first recipient of the Edward C. Kendall Mayo Clinic Alumni Association Research Award (1981).

    Michael moved to Kingston, Ontario in 1984 to start his individual research program at Queen’s University. He quickly rose through the ranks at Queen’s, and in 1989 was promoted to full Professor of Biochemistry and Medicine. While Michael continued to conduct research on the prothrombinase complex, most of his research at Queen’s was devoted to the field of fibrinolysis. Michael described the kinetics of plasminogen activation by tPA (4), the importance of Lys-plasminogen as an intermediate in plasminogen activation (5), and characterized and quantified the contribution of plasmin-modified fibrin as a cofactor in this process (6). Arguably though, Michael’s biggest scientific achievement came in 1996 when he described the isolation and characterization of the Thrombin Activatable Fibrinolysis Inhibitor, or TAFI (7). Subsequently, he identified the mechanism by which TAFI attenuates fibrinolysis (8) and described the consequences of TAFI activation during the process of fibrinolysis.

    Michael was an outstanding mentor and teacher who thoroughly enjoyed this aspect of his career. Michael’s passion was in mathematics and he was pleased to pass on his vast knowledge. Students from all over campus including those in the biochemistry, chemistry, pathology, pharmacology and medicine departments sought his help in modeling their data. Many benefited from his passion for mathematics and his ability to apply it to biological systems. Michael’s enthusiasm for science inspired those who worked with him.

    Michael’s contributions to research on coagulation and fibrinolysis earned him a Distinguished Career Award at the XXIInd Congress of the International Society on Thrombosis and Haemostasis (ISTH; Boston, 2009) and in 2010 he was invited to deliver a plenary lecture on the Biochemistry of TAFI at the 20th Congress of the International Society on Fibinolysis and Proteolysis (ISFP) in Amsterdam. Michael was also an active member in the research community. He served as a member of the Editorial Board of the Journal of Biological Chemistry, reviewed manuscripts for numerous journals and funding agencies and served as a Council Member of the ISFP (2008 – 2011) and a cochair on the Fibrinolysis Scientific and Standardization committee of the ISTH (2001 – 2011). In recognition of his numerous contributions, the ISFP Council has named a plenary lecture at the 21st Congress of the ISFP (Brighton, 2012) after Michael.

    Michael’s kind nature, patience, aptitude and enthusiasm for science and ability to tell an entertaining story or joke made him a popular person wherever he traveled. He will certainly be missed.

    References

    1. Nesheim ME, Myrmel KH, Hibbard L, Mann KG. Isolation and characterization of single chain bovine factor V. J Biol Chem. 1979; 254(2): 508-17.
    2. Nesheim ME, Mann KG. Thrombin-catalyzed activation ofsingle chain bovine factor V. J Biol Chem. 1979; 254(4):1326-34.
    3. Nesheim ME, Tracy RP, Mann KG. "Clotspeed," a mathematical simulation of the functional properties of prothrombinase. J Biol Chem. 1984; 259(3):1447-53.
    4. Horrevoets AJG, Pannekoek H, Nesheim ME. A steady-state template model that describes the kinetics of fibrin-stimulated [Glu1]- and [Lys78]plasminogen activation by native tissue-type plasminogen activator and variants that lack either the finger or kringle-2 domain. J Biol Chem. 1996; 272(4):2183-91.
    5. Fredenburgh JC, Nesheim ME. Lys-plasminogen is a significant intermediate in the activation of Glu-plasminogen during fibrinolysis in vitro. J Biol Chem. 1992; 267(36):26150-6.
    6. Walker JB, Nesheim ME. A kinetic analysis of the tissue plasminogen activator and DSPAalpha1 cofactor activities of untreated and TAFIa-treated soluble fibrin degradation products of varying size. J Biol Chem. 2001; 276(5):3138-48.
    7. Bajzar L, Manuel R, Nesheim ME. Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. J Biol Chem. 1995; 270(24):14477-84.
    8. Wang W, Boffa MB, Bajzar L, Walker JB, Nesheim ME. A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor. J Biol Chem. 1998; 273(42):27176-81.

    Jonathan H. Foley and Kenneth G. Mann*

    University of Vermont 208 S Park Drive CRF, Room 235 Colchester VT 05446 USA

    *The authors would like to thank Paul Kim, Michael Cook, Michael Boffa, Laszlo Bajzar and the ISFP Council for their useful comments.