[Factors influencing course of hospitalization in patients with hip fractures: Complications, length of stay and hospital mortality]. / Einflussfaktoren auf den stationären Verlauf von Patienten mit hüftgelenknahen Femurfrakturen: Komplikationen, Liegezeit und Krankenhaussterblichkeit.

BACKGROUND: Time of surgery, age, sex, and co-morbidities influence the complication and mortality rate in patients with hip fractures. Patients with relevant co-morbidities, who were hospitalized at the weekend have a higher mortality rate. Complications prolong length of stay (LOS), which results in higher costs and shortage of bed capacity. OBJECTIVES: The influence of various factors on hospitalization with emphasis on complications, LOS, and clinical mortality should be observed. MATERIALS AND METHODS: Retrospectively, 242 patients with hip fractures (>64a) were observed. In addition to age and sex, time of hospitalization and surgery, intensive care therapy, hospital mortality, LOS, comorbidities, ASA, and complications were recorded. Times were assigned to the work week or the weekend or regular or on-call duty service. RESULTS: 29.8 % were hospitalized at the weekend, 66.1% on on-call duty, 24.1% were operated on the weekend, 67.4% on on-call duty. 86.3% were operated <48 h after admission. The mortality rate was 8.3%. Longer time to surgery results in more frequent intensive care therapy, prolongs the LOS, and increases overall complications. Advanced age increases mortality and LOS. A higher value of the ASA classification leads to increased mortality; co-morbidities lead to more frequent intensive care therapy. Surgical complications prolong LOS of 10.8d (86.4%). CONCLUSION: Hospitalization is influenced by age, ASA and co-morbidities as well as by time to surgery and operation in day or late and nighttime service. Early surgery and prevention of surgical complications reduce LOS.

[ProFI reduction of pediatric pulled elbow]. / Die ProFI-Reposition der Pronatio dolorosa infantum.

BACKGROUND: Pulled elbow is a common injury in children under the age of 5 years which is usually treated by manual reduction. Supination of the forearm is recommended as opposed to pronation or other maneuvers. The author has developed a manipulative intervention for reduction of pulled elbow in young children on the basis of the pronation technique and called ProFI reduction. PATIENTS AND METHODS: The ProFI method was performed on 41 children and the group was analyzed prospectively according to effectiveness of the ProFI repositioning. RESULTS: Among the 41 children the initial diagnosis was incorrect in 7 cases (17%) and in 11 children (27%) more than one doctor's visit was necessary to reposition successfully. Repositioning with the ProFI method was immediately successful in all cases. CONCLUSION: The application of the ProFI method as a modified pronation technique was shown to provide excellent effectiveness with respect to the patients treated.

The presence of secretoneurin in human synovium and synovial fluid.

Secretoneurin is a neuropeptide formed from the proprotein secretogranin II. It is found in afferent nerve fibres and has chemotactic activity for monocytes, neutrophils and fibroblasts. We investigated the presence of secretoneurin in synovial fluid and synovium from patients with osteoarthritis and rheumatoid arthritis. The secretoneurin immunoreactive material found in synovial fluid was identified by high performance liquid chromatography as the free peptide secretoneurin. Its level in hip joints was 15.6, in knee joints of osteoarthritis patients 17.3 and in rheumatoid patients significantly lower (8.6 fmol/ml). Immunocytochemistry provided evidence for the presence of sub-intimal secretoneurin-immunoreactive nerve fibres in knee synovium in osteoarthritic patients. In rheumatoid synovium, only very few immunoreactive fibres were found these being mostly localised in deep stroma. The results show that secretoneurin is present in osteoarthritic joint and suggest that secretoneurin levels are down-regulated in rheumatoid joint. Therefore, secretoneurin may participate in acute or mild phases of inflammation but is unlikely to have a major role when more severe inflammation is present such as that seen in rheumatoid joint.

Release of secretoneurin and noradrenaline from hypothalamic slices and its differential inhibition by calcium channel blockers.

Secretoneurin is a newly discovered peptide found in high concentrations in brain. We have studied the release of secretoneurin and noradrenaline from superfused hypothalamic slices from rat brain. Both electrical stimulation and potassium induced depolarisation released secretoneurin and noradrenaline from these slices in a calcium-dependent manner. Electrical stimulation caused a preferential release of noradrenaline when compared to the secretion elicited by high potassium. The time course of secretoneurin release was more protracted than that of noradrenaline. The calcium channel blocker omega-conotoxin inhibited only the electrically induced release of noradrenaline, whereas nifedipine inhibited only that of secretoneurin. These results establish that secretoneurin is secreted from neurons. Inhibition of this release by nifedipine is consistent with the concept that secretion from large dense core vesicles occurs at sites different from that of small vesicles and depends on calcium influx via L-type calcium channels.

Messenger RNA levels of chromogranin B, secretogranin II, and VGF in rat brain after AF64A-induced septohippocampal cholinergic lesions.

The mRNA levels of secretogranin II, chromogranin B, and VGF were compared in brains of control and AF64A-treated rats. This toxin induces specific lesions of the septohippocampal cholinergic pathway. As a consequence of this treatment, the chromogranin B message was elevated in the dentate gyrus granule cells of the hippocampus. In the paraventricular nucleus of the hypothalamus, a concomitant elevation of the messages of secretogranin II and corticotropin-releasing factor occurred in the parvocellular neurons, and an increase of those of secretogranin II and VGF occurred in a subgroup of magnocellular neurons. Further increases for secretogranin II were seen in the amygdaloid nuclei and the reticular thalamic nuclei and increases for chromogranin B in the temporal cortex, substantia nigra compacta, and ventral tegmental area. These results indicate that the toxin-induced lesion of the cholinergic pathway innervating the hippocampus apparently leads to the stimulation of several defined groups of neurons that react with an increase in the mRNA levels of their secretory peptides. We suggest that changes in mRNA expression of these peptides are useful parameters for defining neurons under chronic stimulation.

[Special problems of nutrition therapy in patients with terminal kidney insufficiency with chronic ambulatory hemodialysis]. / Spezielle Probleme der Ernährungstherapie bei Patienten mit terminaler Niereninsuffizienz unter chronisch ambulanter Hämodialyse.

The treatment of end-stage chronic renal failure with intermittent ambulatory hemodialysis induces additional catabolic stimulus. Thus, the protein requirements of maintainance hemodialysis patients with 1.2 to 1.4 g/kg/day are higher than in the predialysis state. An energy intake of 35 to 38 kcal/kg/day contributes to an optimal anabolic utilization of incorporated protein. The catabolic response in case of complications or stress situations demands supplementation of nutrients.

[Special problems of nutritional therapy in chronic kidney insufficiency in the pre-dialysis stage]. / Spezielle Probleme der Ernährungstherapie bei chronischer Niereninsuffizienz in der Prädialysephase.

The main objectives of medical and nutritional management of patients with chronic renal failure are to slow down the progression of renal disease and to prevent secondary complications due to hypertension, uremic metabolic disturbances, and bone disease. The importance of nutritional measures for this purpose is increasingly recognized. In the setting of vitamin D and calcium deficiency secondary hyperparathyroidism and retention of phosphate result in renal osteodystrophy. An increase in dietary calcium and avoidance of foods rich in phosphate are important. In some patients supplementation of vitamin D3 may be necessary while calcium homeostasis is monitored during follow up. The dietary protein content can influence the severity of the uremic state. Normal or increased consumption of protein may accelerate the progression of renal disease due to the accumulation of nitrogenous products. In addition, uremia itself may cause loss of appetite and thus accumulation of endogenous nitrogen compounds as a result of protein catabolism. Protein restriction under such circumstances may cause malnutrition and an associated increase in morbidity and mortality. Thus, dietary management must consist of individually designed restriction of total protein intake with ingestion of high value protein. This allows balanced nitrogen metabolism with a reduction in circulating uremic toxins.

Phylogenetic distribution of peptides related to chromogranins A and B.

The presence of chromogranin-related peptides in a wide range of species was investigated by one and two-dimensional electrophoresis followed by immunoblotting. Antisera against bovine chromogranins A and B and the peptide WE-14 (chromogranin A316-329) were used. Chromogranins were identified by their heat stability, by their electrophoretic behavior, and by immunological cross-reaction with antisera. In all species investigated ranging from mammals to birds, amphibians, fish, and arthropods, chromogranin A- and B-like proteins could be demonstrated. For all species, there was an immunological cross-reaction with antisera against bovine chromogranins. The molecular sizes and isoelectric points of the chromogranins were similar in all species. The antiserum against WE-14 cross-reacted with pig, rat, and chicken chromogranins. It is concluded that the chromogranins A and B have a widespread phylogenetic distribution with a significant conservation of molecular size, isoelectric points, and immunological epitopes. This is consistent with the concept that these peptides have a specific function.

Rickettsia prowazekii requires host cell serine and glycine for growth.

The growth requirement of Rickettsia prowazekii for the amino acids serine and glycine was assessed in both wild-type cell lines and a mutant cell line. X-irradiated L929 cells supported the growth of R. prowazekii when the cells were incubated in Eagle minimal essential medium supplemented with serum. In contrast, in this medium, X-irradiated Vero cells did not support the growth of rickettsiae unless cycloheximide, serine, or glycine was added. Other nonessential amino acids, additional glucose, and potential products of host cell metabolism of serine and glycine were nonstimulatory. The concentration of serine or glycine required to support rickettsial growth had no effect on the doubling time of uninfected, unirradiated Vero cells. A comparison of intracellular amino acid pools indicated that the serine and glycine concentrations in mock-infected Vero cells were approximately 31 and 14% of the respective concentrations in mock-infected L929 cells. The pools of both amino acids in Vero cells increased markedly upon treatment of the cells with cycloheximide. Interconversion of serine and glycine catalyzed by serine hydroxymethyltransferase was detected in cell-free extracts of purified rickettsiae. However, this enzymatic activity did not permit rickettsial growth in a glycine-requiring clone (772-56d) of the Chinese hamster ovary cell CHO-K1 in the absence of glycine supplementation. These data indicate that R. prowazekii depends on the host cell for serine or glycine.

Gamma-interferon-induced inhibition of the growth of Rickettsia prowazekii in fibroblasts cannot be explained by the degradation of tryptophan or other amino acids.

We examined the role of amino acid deprivation in gamma-interferon-induced (IFN-gamma) suppression of the growth of Rickettsia prowazekii in mouse L929 cells and human fibroblasts by measuring the amino acid pools in untreated and IFN-gamma-treated cells. In recombinant IFN-gamma-treated cultures of human fibroblasts, tryptophan was undetectable in both the intracellular pool and the extracellular medium. In contrast, tryptophan was not depleted from the intracellular pool or the extracellular medium of L929 cells treated with recombinant IFN-gamma or crude mouse lymphokines. None of the other amino acids measured was severely depleted in IFN-gamma-treated L929 cells and human fibroblasts. Extracts prepared from IFN-gamma-treated human fibroblasts exhibited indoleamine 2,3-dioxygenase activity, converting tryptophan into products that cochromatographed with N-formylkynurenine and kynurenine; however, extracts prepared from untreated human fibroblasts, untreated L929 cells, recombinant IFN-gamma-treated L929 cells, and mouse lymphokine-treated L929 cells did not degrade tryptophan. Human HeLa cells resembled the human fibroblasts in that they degraded tryptophan after IFN-gamma treatment. Similarly, mouse 3T3-A31 cells and mouse embryo fibroblasts resembled mouse L929 cells in that they did not degrade tryptophan. Supplementation of the extracellular medium with additional tryptophan reconstituted the tryptophan pool in mock-infected and R. prowazekii-infected, X-irradiated, IFN-gamma-treated human fibroblasts to values greater than those observed in untreated control cultures. However, reconstitution of the tryptophan pool did not relieve IFN-gamma-induced inhibition of rickettsial growth. Addition of kynurenine or N-formylkynurenine to rickettsia-infected human fibroblasts at concentrations four times the usual tryptophan concentration did not inhibit growth of R. prowazekii. We conclude that neither tryptophan depletion nor depletion of the other amino acids studied explains the inhibitory effect of IFN-gamma on rickettsial growth in mouse L929 cells. In IFN-gamma-treated human fibroblasts, either tryptophan depletion is not involved in the inhibition of rickettsial growth or tryptophan depletion and some other mechanism(s) together contribute to the inhibition of rickettsial growth.

[Incorporation of methionine into a peptic partial hydrolyzate from faba bean protein isolate by plastein reaction with thermitase]. / Untersuchungen zum Methionineinbau in ein peptisches Partialhydrolysat aus Ackerbohnenproteinisolat durch Plasteinreaktion mit Thermitase.

The contents of free methionine methyl esters and methionine as well as the bound quantities of methionine were determined in order to evaluate the effectiveness of the covalent incorporation of methionine into peptic partial hydrolyzate in the course of the plastein reaction with addition of L-, DL- or D-methionine ethyl esters. The plastein reaction was performed with thermitase as reenzyme. The methionine incorporation was found to take place stereospecifically. The incorporation degree of the methionine ester is influenced by a thermitase-catalyzed and a non-enzymatic ester saponification.

[The effect of enzymatic modification on lysinoalanine formation in field-bean protein isolate and beta-casein]. / Einfluss der enzymatischen Modifizierung auf die Lysinoalaninbildung in Ackerbohnenproteinisolat und beta-Casein.

Lysinoalanine (LAL) was determined in alkali-treated partial hydrolysates (PH) of casein, peptides isolated from these PH and in PH of field-bean protein to clarify whether intermolecular or intramolecular LAL bridges are preferentially formed. Furthermore, the formation of LAS in plasteins was studied as a contribution to plastein research. The formation of LAL in the peptide mixtures of beta-casein and the decrease of the LAL content in the PH (as compared to intact proteins) indicates that the formation of LAL favours the intramolecular cross-linking of polypeptide chains. The LAL content decreases as the degree of hydrolysis of the PH of the field-bean protein isolate increases, and depends upon the protease used in the production of the hydrolysates. The LAL contents of the alkali-treated plasteins are less than those of the initial hydrolysates. The decrease of the LAL content is directly proportional to the hydrolysis proceeding during the plastein reaction.

[Formation of plastein gels from peptic digests of field bean protein isolates]. / Untersuchungen zur Bildung von Plasteingelen aus peptisch gespalltenem Ackerbohnenproteinisolat.

Peptic partial hydrolysates of a different hydrolysis degree were prepared from horse bean protein isolate and used for the plastein reaction with thermitase. Whilst unsoluble products were formed from partial hydrolysates of a hydrolysis degree above 60%, plastein gel could be obtained from a less intensely split basic material. By gel chromatography and by determination of the percentage which was unsoluble in 10% trichloroacetic acid, a proteolytic degradation could be made proof on the conditions of the plastein reaction. On addition of DL-methionine ethylesters to the partial hydrolysate an increasing incorporation of methionine into the plastein could be observed with increasing hydrolysis degree.