Access the full text.
Sign up today, get DeepDyve free for 14 days.
G. Lippi, E. Favaloro, M. Franchini, G. Guidi (2009)
Milestones and perspectives in coagulation and hemostasis.Seminars in thrombosis and hemostasis, 35 1
G. Tennent, S. Brennan, A. Stangou, J. O'grady, P. Hawkins, M. Pepys (2007)
Human plasma fibrinogen is synthesized in the liver.Blood, 109 5
R. Doolittle (1981)
Fibrinogen and fibrin.Scientific American, 245 6
V. Chaturvedi, Ashok Kumar (2011)
Isolation of a strain of Pseudomonas putida capable of metabolizing anionic detergent sodium dodecyl sulfate (SDS)Iranian Journal of Microbiology, 3
E. Pretorius, H. Oberholzer, Eureke Smit, E. Steyn, S. Briedenhann, Carl Franz (2008)
Ultrastructural Changes in Platelet Aggregates of HIV Patients: A Scanning Electron Microscopy StudyUltrastructural Pathology, 32
Ryan Adams, C. Schachtrup, Dimitrios Davalos, Igor Tsigelny, K. Akassoglou (2007)
Fibrinogen signal transduction as a mediator and therapeutic target in inflammation: lessons from multiple sclerosis.Current medicinal chemistry, 14 27
Miller (1951)
The dominant role of the liver in plasma protein synthesis; a direct study of the isolated perfused rat liver with the aid of lysine-epsilon-C14J Exp Med, 94
J. Weisel (2005)
Fibrinogen and fibrin.Advances in protein chemistry, 70
B. Lipinski, E. Pretorius (2012)
Novel pathway of iron‑induced blood coagulation: implications for diabetes mellitus and its complications.Polskie Archiwum Medycyny Wewnetrznej, 122 3
Etheresia Pretorius (2007)
The Role of Platelet and Fibrin Ultrastructure in Identifying Disease PatternsPathophysiology of Haemostasis and Thrombosis, 36
L. Miller, C. Bly, M. Watson, W. Bale (1951)
THE DOMINANT ROLE OF THE LIVER IN PLASMA PROTEIN SYNTHESISThe Journal of Experimental Medicine, 94
E. Weinberg (2010)
The hazards of iron loading.Metallomics : integrated biometal science, 2 11
C. Hall, H. Slayter (1959)
The Fibrinogen Molecule: Its Size, Shape, and Mode of PolymerizationThe Journal of Biophysical and Biochemical Cytology, 5
B. Lipinski, E. Pretorius, H. Oberholzer, W. Spuy (2012)
Iron enhances generation of fibrin fibers in human blood: Implications for pathogenesis of strokeMicroscopy Research and Technique, 75
B. Lipinski, E. Pretorius (2012)
Hydroxyl radical-modified fibrinogen as a marker of thrombosis: the role of ironHematology, 17
Dimitrios Davalos, K. Akassoglou (2011)
Fibrinogen as a key regulator of inflammation in diseaseSeminars in Immunopathology, 34
Fibrinogen is key to the maintenance of hemostasis and is an acute phase protein that is part of the coagulation cascade of proteins. It plays a fundamental role in inflammation, particularly as indicator for a proinflammatory state and is a prominent marker for developing vascular inflammatory diseases. The ultrastructure of fibrin nets can be studied using scanning electron microscopy (SEM) with the addition of thrombin to plasma. In inflammatory conditions such as thromboembolic ischemic stroke and diabetes, the fibrin networks are changed to from dense matted fibrin deposits (DMDs) instead of typical netlike appearance. Similar DMDs can also be induced with the addition of FeCl2 and FeCl3. Importantly, the iron‐induced DMDs look similar to those from patients with prothrombotic conditions. Excessive or misplaced tissue iron now is recognized to pose a substantial health risk. The current research therefore investigates the establishment of a laboratory fibrinogen model to study that might mimic fibrin fiber generation that is achieved using plasma from healthy and diseased individuals. Furthermore, to determine whether the addition of iron to purified fibrinogen will show DMDs and whether hydrophilic agents can prevent them. We conclude that SEM is a very effective tool for the visualization of circulatory consequences of the interaction of iron‐induced hydroxyl radicals with human fibrinogen. Furthermore, this novel fibrinogen model provides a convenient method to study the interactions of the intramolecular and intermolecular hydrophobic forces responsible for the maintenance of the tertiary structure of native fibrin(ogen) and the prevention of iron‐induced DMDs formation by hydrophilic agents. Microsc. Res. Tech. 76:268–271, 2013. © 2012 Wiley Periodicals, Inc.
Microscopy Research and Technique – Wiley
Published: Mar 1, 2013
Keywords: ; ; ; ;
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.