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Sammanfattning

We recently characterized a heparin-deficient mouse strain generated by targeting the gene for N-deacetylase/N-sulfotransferase-2 (NDST-2). The NDST-2(-/-) mice show severe defects in their organization of mast cell (MC) secretory granules, with an almost total absence of the various heparin-binding MC proteases. In the present report we have studied the consequences of heparin/MC protease deficiency for extravascular coagulation and fibrinolysis. Addition of prothrombin to peritoneal cells-a mixture of macrophages, lymphocytes, and MCs-resulted in formation of thrombin but the accumulation of thrombin occurred faster in the NDST-2(-/-) cells than in normal controls. Further, the generated thrombin was subsequently inactivated in the NDST-2(+/+) cell cultures but not in the NDST-2(-/-) cells. Plasminogen was activated to plasmin at an apparently higher rate in peritoneal cells from NDST-2 null mice than in the normal controls. Similar to thrombin, the generated plasmin was inactivated by NDST-2(+/+) but not by the NDST-2(-/-) cells. Subsequent experiments with normal cells showed that cell surface-associated MC chymase, in a strongly heparin-dependent manner, was responsible for both the thrombinin-activating- and plasmin-inactivating activities. These results show that MC chymase-heparin complexes have the potential to regulate extravascular coagulation processes, as well as the plasminogen activator/plasmin system.

Nyckelord

heparin proteoglycan; plasmin; thrombin

Publicerad i

FASEB Journal
2001, volym: 15, nummer: 14, sidor: 2763-2765
Utgivare: FEDERATION AMER SOC EXP BIOL

SLU författare

  • Tchougounova, Elena

    • Institutionen för veterinärmedicinsk kemi, Sveriges lantbruksuniversitet

  • Pejler, Gunnar

    • Institutionen för veterinärmedicinsk kemi, Sveriges lantbruksuniversitet

Associerade SLU-program

Framtidens djurhälsa och djurvälfärd (tom Jan 2017)

UKÄ forskningsämne

Biokemi
Molekylärbiologi

Publikationens identifierare

  • DOI: https://doi.org/10.1096/fj.01-0486fje

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/66603