These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Binding and covalent processing of fibrinogen by hepatocytes and endothelial cells.
    Author: Barsigian C, Martinez J.
    Journal: Blood Coagul Fibrinolysis; 1990 Oct; 1(4-5):551-5. PubMed ID: 1983462.
    Abstract:
    In contrast to most plasma glycoproteins, asialofibrinogen and aglycofibrinogen manifest relatively normal in vivo survivals, suggesting that molecular determinants other than the carbohydrate may be involved in their catabolism. To analyse the metabolic properties of fibrinogen further, we analysed the interaction of normal fibrinogen with suspensions of rabbit hepatocytes or human umbilical vein endothelial cells. In so doing, we identified a novel type of fibrinogen - cell interaction which has the distinguishing characteristic of involving covalent transglutaminase-mediated fibrinogen cross-linking. In this report, we highlight some of the major distinguishing characteristics of this novel type of transglutaminase-mediated fibrinogen - cell interaction.
    [Abstract] [Full Text] [Related] [New Search]