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At least 181 records · Page 10Linked to original sources
PubMed1996

[Coagulation-inhibiting proteins; implications for cerebrovascular disorders].

BACKGROUND: Deficiencies in ATIII, PC, and PS are associated with a higher incidence of thromboembolic events. An analysis was made of these three proteins in 239 cases of non-embolic stroke; the incidence of their deficiency and the presence of intersexual variations were evaluated. Two different methods were used to measure PS, functional PS and free PS, comparing the values and the incidence of the deficiency. RESULTS: ATIII, PC, free PS, and functional PS deficiencies were found in 2.93%, 7.5%, 9.52% and 13.72%, respectively. The observed PS values showed statistically significant differences between sexes. CONCLUSION: There was a higher incidence of PS and PC deficiencies in patients with stroke, which were associated with a poorer prognosis. PS differed between sexes and both methods were valid for its quantitation.

Aged↗
PubMed1998

Fibrinogen Caracas I: a dysfibrinogenemia with a hemorrhagic diathesis associated with diminished fibrin fiber diameter and reduced fibrin gel porosity.

Fibrinogen Caracas I is a dysfibrinogenemia with a mild bleeding diathesis and a defective wound healing. We have characterized this abnormal fibrinogen using transmission electron microscopy (TEM) in combination with turbidity and permeation studies. Turbidometric and permeability analysis showed that the abnormal fibrin had a significantly decreased mass:length ratio and fiber diameter. In addition, the permeability studies of plasma fibrin clots showed that the gel porosity of the abnormal fibrinogen was reduced. Images of the abnormal fibrin structure obtained using TEM showed that the fibers were thinner, much less branched and less ordered than normal fibers. Diminished fibrin fiber diameter and reduced fibrin gel porosity have been taken as hallmarks of thrombophilic dysfibrinogenemias. The results of the present study show that these features are not necessarily predictive of thrombophilia. Further studies performed on a larger number of dysfibrinogenemias need to be conducted in order to establish the implications of these parameters on the clinical outcome.

Coagulation Protein Disorders↗
PubMed1996

Amelioration of disordered hepatic protein synthesis by the deleted form of hepatocyte growth factor in models of liver failure in rats.

Because the liver plays an important role in protein synthesis and cholesterol metabolism and reductions in these functions are observed in almost all hepatic disorders, the effects of the deleted form of hepatocyte growth factor (dHGF) on disordered hepatic protein synthesis were studied in various liver-injured rat models using Wistar male rats. In the 70% hepatectomized rats, plasma clotting time was prolonged and the serum level of total protein and the liver protein content were decreased. The treatment of the animals with dHGF (100-500 micrograms kg-1, i.v., twice daily) ameliorated these parameters at 48 or 72 h. The administration of carbon tetrachloride or D-galactosamine to hepatectomized rats induced a marked prolongation of plasma clotting time and hypoproteinaemia. In the animals treated with dHGF (500 micrograms kg-1, i.v., twice daily) these parameters were rapidly reversed compared with those of control groups. In a hepatocellular necrosis model induced by dimethylnitrosamine, the plasma clotting time was extremely prolonged, and liver protein content, serum total protein, albumin, HDL-cholesterol (as an index of lipoprotein) and plasma lecithin-cholesterol acyltransferase activity severely reduced. In this severely injured model, dHGF (5-500 micrograms kg-1, i.v., twice daily for 28 days) dose-dependently prevented the loss of liver protein content and improved the disordered plasma coagulability and serum protein levels. These results suggest that dHGF is useful for ameliorating the disorders in hepatic functions such as protein synthesis.

Animals↗
PubMed2002

Complexities in ETS-domain transcription factor function and regulation: lessons from the TCF (ternary complex factor) subfamily. The Colworth Medal Lecture.

The ETS-domain transcription factor family can be divided into a series of subfamilies. Elk-1 represents the founding member of the ternary complex factor (TCF) subfamily. By focusing on the TCF subfamily, we can demonstrate the complexities that exist in the function and regulation of ETS-domain transcription factors. This article focuses on Elk-1 in detail and summarizes the functions of other TCFs. The key themes covered include the domain structure of the TCFs, the mechanisms of complex formation with serum response factor, regulation of TCFs by mitogen-activated protein kinase cascades, and transcriptional regulatory properties of the TCFs. Finally, the emerging role of the TCFs in vivo is discussed. A picture is developing indicating that, while these proteins exhibit significant sequence and functional conservation, key differences in their structure and regulation are being identified which may relate to unique functions of these proteins in vivo.

Amino Acid Sequence↗