Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0034065 (pulmonary embolism)
 14,979 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Correlates of the size of infarcts, the time from stroke to death, and the mechanisms of death were studied in 77 consecutive patients who died from infarction in the middle cerebral artery territory. The area of infarcts was assessed by planimetry on schemas of representative brain levels and the results were expressed as a ratio of infarcted area on the whole MCA territory. No clear relationship was found between the size of infarcts in the MCA territory, and any of the characteristics of the patients, but extensive infarcts were more frequent when the internal carotid artery was occluded. No evidence was found of an adverse effect of age, diabetes or initial hyperglycemia on the size of infarcts. The mechanisms of death were not linked to sex, age, high blood pressure, diabetes, blood glucose level at admission, presence and location of an arterial occlusion, or etiology of the infarct. On the contrary, they varied as a function of interval from stroke to death. Transtentorial herniation, the main cerebral cause of death, occurred mainly in the first week and was related to the large size of infarcts. Rare recurrences of stroke and frequent extracerebral mechanisms of death (mainly pneumonia, pulmonary embolism and cardiopathy) occurred later on.
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PMID:Infarcts in the middle cerebral artery territory. Pathological study of the mechanisms of death. 833 39

A conjugate of annexin V and the B-chain of urokinase was prepared and its fibrinolytic properties were studied. First, a mutant of annexin V was constructed with an N-terminal extension of six amino acids (Met-Ala-Cys-Asp-His-Ser) and with Cys316 mutated to Ser; this molecule was expressed in Escherichia coli. The urokinase B-chain was prepared by limited reduction of the interchain disulfide bond between the A- and B-chains of urokinase. These two molecules were then then connected by a disulfide bond and purified to yield a 1:1 stoichiometric conjugate. The conjugate had the same catalytic activity as urokinase against a synthetic substrate, Glt-Gly-Arg-MCA, and a similar plasminogen activating activity. The conjugate showed the same binding affinity for phosphatidylserine-containing membranes as annexin V. The in vitro fibrinolytic activity of the conjugates on clots prepared from platelet-rich plasma was comparable to that of urokinase. However, the conjugate showed 3-4-fold stronger in vivo thrombolytic activity than urokinase in a rat pulmonary embolism model, while having essentially the same plasma clearance rate as urokinase or B-chain. These results show that annexin V is a useful agent for targeting plasminogen activators to phospholipid-containing thrombi.
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PMID:Preparation and characterization of a disulfide-linked bioconjugate of annexin V with the B-chain of urokinase: an improved fibrinolytic agent targeted to phospholipid-containing thrombi. 854 74