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Biomedical subjects

M H Denninger

Publications and source records attributed to M H Denninger.

12 recordsLinked to original sources
PubMed1994

[Hippocampothalamic infarction. A limited form of infarction in the posterior cerebral artery area].

Infarction of the hippocampus and the right ventroposterolateral thalamus was observed. Angiography revealed a posterior cerebral artery occluded near its origin, immediately upstream from the posterior communicating artery. The infarction was limited to the areas irrigated by the branches originating in the proximal part of the artery. More distal branches for the calcarine scissure and the temporooccipital gyruses were not involved.

Adult↗
PubMed1992

US-guided percutaneous liver biopsy with plugging of the needle track: a prospective study in 72 high-risk patients.

The efficiency, accuracy, and safety of ultrasound-guided liver biopsy with plugging of the needle track were prospectively assessed in 72 patients at high risk for hemorrhage. Seventy-eight biopsy procedures were performed in 72 consecutive patients prospectively classified into four different groups on the basis of coagulation parameters. Sixty-two patients (86%) had severe or moderately severe coagulation disorders. Fifty-four biopsy procedures were performed in 50 patients with diffuse liver disease, and 24 were performed in 24 patients with focal liver lesions. The biopsy track was embolized with gelatin particles and thrombin. Biopsy specimens adequate for histologic diagnosis were obtained in 69 of the 72 patients (96%). In focal lesions, accuracy and sensitivity in the diagnosis of malignancy were 75% and 89%, respectively. Two serious bleeding complications (2.8%) were encountered in two of the patients with major coagulation disorders. Liver biopsy with plugging of the needle track is a practical technique and is a feasible alternative to the transjugular approach. Respective indications for both methods depend on the severity of coagulation disorders and the presence of focal lesions.

Adult↗
PubMed1988

Portal vein thrombosis with ruptured oesophageal varices as presenting manifestation of hereditary protein C deficiency.

The protein C system is essential in limiting the activation of coagulation in vivo. We report the case of a 45 year old man with portal vein thrombosis complicated by ruptured oesophageal varices. Low concentration of plasma protein C was found in the patient and subsequently in one brother with a history of venous thromboembolism, and also in one son and one nephew who were asymptomatic. Hereditary protein C deficiency should be considered in patients with portal hypertension due to portal vein thrombosis.

Esophageal and Gastric Varices↗
PubMed1987

ADP-induced platelet aggregation depends on the conformation or availability of the terminal gamma chain sequence of fibrinogen. Study of the reactivity of fibrinogen Paris 1.

Fibrinogen Paris I contains a mutant gamma chain that is longer than the normal chain, resulting in altered fibrin polymerization and cross-linking. Because these functions involve the carboxy-terminal region of the gamma chain, we decided to determine whether fibrinogen Paris I or the isolated Paris I gamma chain supports normal ADP-induced platelet aggregation, a function that requires the ultimate 12 residues of the normal gamma chain (400 through 411). Aggregation of ADP-stimulated normal platelets was defective with fibrinogen Paris I and markedly depressed with the gamma Paris I chain. These findings prompted us to characterize the carboxy-terminal structure of the region of the gamma Paris I chain responsible for this activity. The carboxy-terminal cyanogen bromide (CNBr) peptide of the normal gamma chain (385 through 411) or that from gamma Paris I was isolated by differential adsorption to triethylene-tetramine resin or by reverse-phase high-performance liquid chromatography (HPLC). The CNBr peptide from the Paris I gamma chain was identical to that of the normal gamma chain in its retention time on HPLC, its amino acid composition, and its sequence. Thus, the primary structure of the gamma Paris I chain from residue 384 through 411 is normal, indicating that a peptide insertion has occurred upstream from residue 384, resulting in an impairment of those physiologic functions attributable to the carboxy-terminal end of the gamma chain from position 384 (ie, cross-linking, ADP-induced platelet aggregation, and at least a portion of the gamma chain polymerization site). These observations demonstrate that the gamma chain platelet recognition site in the fibrinogen molecule is necessary but not alone sufficient to support normal ADP-induced platelet aggregation. There appears to be an additional requirement for normal conformation of the gamma chain or availability of its terminal sequence during the interaction of fibrinogen with platelets.

Adenosine Diphosphate↗
PubMed1985

Interaction of human alpha-thrombin and gamma-thrombin with antithrombin III, protein C and thrombomodulin.

Conversion of human alpha-thrombin to gamma-thrombin by limited proteolysis resulted in a decrease in the inactivation rate of the enzyme by antithrombin III. The second-order rate constants were similar but significantly different: 11 +/- 1.7 X 10(3) and 7 +/- 0.5 X 10(3) M-1 s-1 for alpha- and gamma-thrombin respectively. This difference is probably related to a slight change in reactivity of the catalytic site, rather than to a structural alteration of the recognition site for antithrombin III. The rate of protein C activation, measured in the absence of thrombomodulin, was greatly reduced by conversion of alpha-thrombin to gamma-thrombin. In addition, gamma-thrombin failed to displace alpha-thrombin from its complex with thrombomodulin, as demonstrated by measuring either the rate of protein C activation by thrombin-thrombomodulin, or the fibrinogen clotting activity of thrombin-thrombomodulin, in the presence of competing diisopropylphospho-thrombin. It is concluded that the recognition sites involved in protein-C-thrombin and thrombomodulin-thrombin interactions are both dramatically affected by the loss of peptide material occurring during the conversion of alpha-thrombin to gamma-thrombin and/or by the resulting conformational changes.

Animals↗