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Biomedical subjects

M Jochum

Publications and source records attributed to M Jochum.

At least 109 records · Page 6Linked to original sources
PubMed1990

[Is there a favorable time for the management of femoral shaft fractures in polytrauma?].

Despite the wide-spread opinion, that early stabilisation of femur fractures in multiply injured patients is of advantage, there are no publications that unambiguously prove this statement. In contrast, primary fracture stabilisation of the femur with concomitant thoracic trauma seems to increase the rate of complications. The biochemical data of the prospective study presented here suggest, that operative stabilisation of femoral fractures imposes an additional trauma on the already compromised organism. The period between days 2 to 4, when the primary activation of humoral and cellular mediators has returned to normal levels, seems to be the best time for osteosyntheses of these fractures. The operation in this period allows intramedullary fixation--the biologically and biomechanically best fixation procedure--with low risk.

Acute-Phase Proteins↗
PubMed1989

[Insufficiency of intra-abdominal immunity to infection in purulent peritonitis--sequela of disordered foreign body opsonization].

Despite a high concentration of serum proteins and intact phagocytes peritonitis exudates contain a large number of viable, pathogenic bacteria. The reason for this biological paradox is unknown. Our investigations reveal a pronounced defect in humoral opsonization of foreign particles in peritonitis exudate. We evaluated a modified chemiluminescence system allowing the determination of opsonic activity in serum and exudate. In serum we found a close correlation between opsonic activity and immunologically measurable levels of C3-complement and IgG. In purulent peritonitis exudates, however, the actual opsonizing activity was much less than expected according to the opsonin concentrations. We found a pronounced difference between immunologically determined opsonin levels and impaired opsonic function. Employing crossed immunoelectrophoresis massive C3-splitting into smaller fragments could be demonstrated in peritonitis exudates. In these exudates we found very high concentrations of granulocyte proteolytic (elastase) and oxidative (myeloperoxidase) enzymes which may lead to a functional destruction of opsonins followed by impaired opsonization in peritonitis exudate. The great number of bacteria and foreign particles in addition can cause a pronounced physiological consumption of complement components. The almost complete breakdown of intact C3-complement in intraabdominal exudate explains the deficient host defence in patients with severe peritonitis.

Bacterial Infections↗
PubMed1989

Phospholipase A in acute lung injury after trauma and sepsis: its relation to the inflammatory mediators PMN-elastase, C3a, and neopterin.

Inflammatory mediators involved in the pathogenesis of the adult respiratory distress syndrome (ARDS) are products of the humeral cascade systems like the complement cascade and substances released from neutrophil granulocytes and macrophages like proteases, O2-radicals and arachidonate products. Phospholipase A2 (PLA) was shown by Vadas et al. to be correlated with circulatory shock in the sepsis syndrome, the probably most important underlying disease of ARDS. In a clinical study in 48 patients at risk for ARDS after trauma and sepsis we found plasma PLA elevated (52 +/- 5 U/l) in sepsis, with a positive correlation to the complement split product C3a (r = 0.42, p less than 0.01) and neopterin (r = 0.49, p less than 0.05), which serves as a marker of macrophage stimulation. Elastase-alpha 1PI and C3a showed higher plasma levels in patients with ARDS compared with non-ARDS patients, whereas the neopterin and PLA concentrations were not different with regard to ARDS. The relation between PLA and neopterin shown in the study is consistent with the possibility of macrophages being a source of the plasma PLA, as reported in experimental studies.

Biopterins↗
PubMed1989

Inhibition of proteinases with recombinant eglin C during experimental Escherichia coli septicemia in the pig.

Administration of the proteinase inhibitor eglin C reduces the symptoms of capillary leakage in a porcine model of septic shock. This was assessed by measurements of blood pressure, plasma protein concentration, hematocrit, and duration of urine production. Eglin C plasma levels around 1.2 microM resulted from a dose of 1.9 mg.kg-1.h-1 for 4 h and were therapeutically effective. A higher dose of eglin C (7.7 mg.kg-1.h-1 for 4 h) induced levels of approximately 5.6 microM in plasma and was not superior. This observation indicates that lysosomal proteases from neutrophils or degranulation of mast cells play a crucial role in the increase of capillary permeability during septicemia.

Animals↗
PubMed1988

Enzymatically active cathepsin B dissociating from its inhibitor complexes is elevated in blood plasma of patients with septic shock and some malignant tumors.

Using fluorogenic substrates and the specific inhibitor E-64, cysteine proteinase (CP) activity was measured in blood plasma of healthy controls (mean = 35.0 mU/l) and patients with cancer and severe septic shock. Whereas moderately elevated activity was observed in some kinds of cancer (mean = 63.9 mU/l), 10-fold increased CP activity was found in septic shock. The plasma CP activity of sepsis patients paralleled the immunologically determined concentration of elastase-alpha 1-proteinase inhibitor complex. On the basis of its substrate specificity and its Michaelis constant for Z-Phe-Arg-NMec the plasma CP was identified as cathepsin B or a cathepsin B-like proteinase (CBP). Kinetic studies revealed that dilution and competition with substrate effects reversible dissociation of CBP from complexes with plasma inhibitors that are most probably the kininogens. The dissociation of CBP was confirmed by gel chromatographic fractionation of the plasma proteins. The results suggest that active CBP can easily dissociate from its plasma inhibitor complexes in vivo and may be involved in pathogenetic extracellular proteolysis.

Cathepsin B↗
PubMed1987

[Possibilities of biochemical differentiation of reactive effusions of the knee joint].

1. Differentiation of reaction effusions: Posttraumatic reaction effusions (fresh meniscus or capsular ligament lesion) displayed a greatly enhanced alkaline phosphatase activity, whereas postoperative reaction effusions that were poor and rich in cells had a comparatively high C3c value relative to the total amount of protein. In punctates from patients with patellar chondropathy and primary synovial reaction (no trauma, no postoperative condition) the lowest parameter values of of the entire study were seen. 2. Decision help with regard to therapy: Via determination of the sensitive inflammation parameter PMN elastase (E-a1PI) it is possible to initiate cartilage-protective therapy directly in case of a cartilage lesion of mild inflammatory character (E-a1PI 300-500 ng/ml), whereas in case of severe inflammation (E-a1PI 500-1000 ng/ml) anti-inflammatory drugs should be employed in the first instance. 3. Therapy control: In the follow-up control of reaction effusions the comparison of concentrations of biochemical parameters before and after intra-articular application of drugs offers a possibility of therapy control. Since with increasing inflammatory nature and disturbance of the blood-synovia barrier the concentration of the measured biochemical parameters (with the exception of glucose) increased in the synovial fluid, successful treatment should result in an absence of such an increase in concentration (or, if at all, in an only slight measure).

Acute-Phase Proteins↗
PubMed1987

Neutral proteinase inhibitors in PMN leukocytes. I. Purification and characterization of a neutral proteinase inhibitor from bovine neutrophils.

An inhibitor of neutral proteinases was isolated from the cytosol of bovine leukocytes by anion exchange chromatography on Mono Q and gel filtration on a HPLC TSK column. The gel filtration resulted in two fractions with inhibitory activity which could be identified by sodium dodecyl sulphate-poly-acrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions as dimer and monomer of the inhibitor. The latter was shown to be homogeneous in SDS-PAGE with an apparent molecular mass of 40 kDa, with calibrated HPLC a molecular mass of 36.5 kDa has been determined. Isoelectric focusing followed by Western blot analysis revealed four bands in the pH range of 5.0 to 5.9. The inhibitor was found in bovine polymorphonuclear neutrophils (PMN), whereas lymphocytes and monocytes lacked this protein. No immunological cross-reactivity between the described cell-derived PMN-inhibitor (PMN-I) and alpha 1-proteinase inhibitor was detectable. The mechanism of inhibition for the serine proteinases chymotrypsin, trypsin, pancreatic elastase and leukocyte elastase was studied. PMN-I could not bind to PMS-chymotrypsin. The reaction of the serine proteinases with the PMN-I was characterized by the determination of the association rate constant kon.

Animals↗
PubMed1987

Influence of the lysosomal elastase inhibitor eglin on the development of interstitial lung edema in E. coli bacteremia in pigs.

Infusion of 3 X 10(10) live E. coli cells into anesthetized piglets induced severe septicemia with characteristic alterations in systemic and pulmonary circulation, lung function and morphology, blood cell counts and plasma protein composition. The simultaneous infusion of the elastase-cathepsin G inhibitor, r-eglin c, in a doses of 3.85 mg/kg X h for 4 hrs, reduced mortality, plasma protein consumption, and accumulation of interstitial fluid in the lungs. These findings are in favour of the concept that during septicemia the balance between liberated lysosomal proteinases and their extracellular inhibitors is severely disturbed. It can be at least partially restored by administration of an exogenous elastase inhibitor.

Animals↗