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C H Bauer

Publications and source records attributed to C H Bauer.

10 recordsLinked to original sources
PubMed1987

[A plastic substitute for the superior sagittal sinus in pigs].

The substitute of the superior sagittal sinus by a new method namely a vessel prosthesis (Gore-Tex) and special connecting pieces in relationship with drug treatment is represented. The method is very simple and can also be carried out by microsurgically untrained operators. Moreover, this method allows a clear faster operation without using a bypass. The sinus was ligated, partially resected or incised and replaced by the described prosthesis in 15 pigs. 3 experiments were without any assertion at all. The sufficiency of the prosthesis was provable in 10 of the 12 remaining pigs. With that a high sufficiency quota was obtained in comparison with the literature. An open prosthesis for a longer time makes possible the formation of a collateral circulation. Furthermore, the prosthesis enables the microsurgical implantation of bigger pontine veins.

Animals↗
PubMed1980

Alterations of D-galactose metabolism in Morris hepatomas.

Studies on Morris hepatomas demonstrate that the specific activity of the enzymes of the Leloir pathway are subject to a variation in tumor tissue. The key enzyme of the galactose pathway, uridine diphosphogalactose 4'-epimerase, is elevated 5- to 9-fold in the rapidly growing and poorly differentiated Tumors 3924A and 7777; in line 9618A2, an even 28-fold increase was found. The observed correlation between enzyme activity, growth rate, and degree of differentiation of the hepatoma suggests that the differences are not coincidental variations. Conversely, the activity of uridine diphosphoglucose: galactose-1-phosphate uridyltransferase was diminished by 40 to 70% as compared to host liver, and the level of galactokinase showed only minor changes. The uptake of galactose and galactosamine by the hepatoma is heavily impaired, whereas the transport of other hexoses and amino sugars (2-deoxyglucose, L-fucose, N-acetylglucosamine, N-acetylmannosamine) is hardly affected. It appears that part of the carrier-mediated diffusion for hexoses is altered without a decisive impact on the whole system. Moreover, autoradiographic analysis of [14C]galactose-labeled tumor plasma membranes revealed a shift of the incorporation pattern from high- to lower-molecular-weight galactopolypeptides. Our results indicate that specific alterations of the D-galactose metabolism are a characteristic feature of Morris hepatomas.

Animals↗
PubMed1978

Decrease of human serum fucosyltransferase as an indicator of successful tumor therapy.

Surgical removal of colon carcinomas leads to a decrease in the rate of incorporation of [14C]fucose into its endogenous acceptor in human serum; normal incorporation rates are attained within 14 days. A similar time course has been determined for alpha2- and alpha3-fucosyltransferase when either desialo- or desialodegalactofetuin are employed as exogenous acceptors. A correlation has also been seen between transferase activity and the therapeutic response of patients with breast cancer. These results indicate that the determination of fucosyltransferase activity can facilitate the diagnosis of neoplasia, and the success of surgery, chemotherapy, or radiation.

Aged↗
PubMed1978

Pathophysiology of failure to thrive in gastrointestinal disorders.

What will be our GI approach to a child with FTT syndrome? Detailed history and physical examination will give us the clue and often the probable diagnosis. Several laboratory tests are helpful in establishing the fact that there is malabsorption. Among them are a complete blood count with smear, quantitative stool fat excretion, serum protein and chemistry screen panel, prothrombin time, and oral tolerance and absorption--i.e., of glucose, iron, vitamin A, and xylose. Specialized procedures may be used to nail down the diagnosis: radiology, biopsy, duodenal intubation, etc. These should never be employed as routine screening tests, however. In outlining a comprehensive and successful therapy, the attending physician will find it helpful to consider the particular pathophysiologic mechanisms of a specific disease. Exact diagnosis makes the therapy both rational and effective.

Adolescent↗
PubMed1977

Glycosyltransferases and glycosidases in Morris hepatomas.

The following three parameters were studied in Morris hepatomas of different growth rates: (a) the specific activity of guanosine dephosphate (GDP)-fucose:glycoprotein fucosyltransferase and cytidine monophosphate (CMP)-N-acetylneuraminic acid:glycoprotein sialyltransferase, (B) the content of GDP-fucosee and CMP-N-acetylneuraminic acid, and (c) the activity of alpha-L-fucosidase and neuraminidase. Fucosyltrasferase activities were significantly elevated in all hepatomas investigated. Especially high levels of enzyme were measured in the rapidly growing tumors 7777, 66, and 3924A. The increase varied between 2- and 3-fold when compared with the corresponding host liver. Conversely, the activity of the sialytransferase was greatly decreased in all hepatoma lines with a rapid or intermediate growth rate. In the fast-growing tumor 9618A2, the activity was reduced to 8%. GDP-fucose and CMP-N-acetylneuraminic acid were determined by the isotope dilution technique. In normal rat liver from Buffalo or ACl rats, the concentration of GDP-fucose was 6.5+/-0.9 and 9.5+/-1.1nmoles/g, wet weight, respectively. In the fast-growing hepatomas 3924A and 9121, levels up to 21.5 nmoles/g, wet weight, were found, However, the content of CMP-N-acetylneuraminic acid in hepatomas was indluenced to a lesser extent by the degree of differentiation of the tumor. In the most rapidly growing tumor, 9618A2, a level of alpha-L- fucosidase seven times higher than in host liver was determined. Moreover, there existed a correlation bewteen the age of the hepatoma and enzyme activity. Within the 2nd week after inoculation, fucosidase activity increased from 130 to 343 nmoles/hr/mg of protein. Neuraminidase was measured in a new linked assay system. The activity of this enzyme was lowered by 50% or was at least unchanged when compared to the activity in host liver. Our results indicate that specific alterations of fucose metabolism are a characteristic feature of Morris hepatomas.

Animals↗
PubMed1976

Galactose metabolism in regenerating rat liver.

1. Rats trained on a controlled lighting and feeding schedule were subjected to partial hepatectomy or sham operation. 2. After a large period of about 6h the activity of UDP-galactose 4-epimerase increased threefold, reaching a maximum 4 days after partial hepatectomy, and returned to normal values within a fortnight. 3. The enzyme pattern of the UDP-galactose-glycoprotein galactosyltransferase was biphasic, one peak appearing at 20 h, the second at 72 h after partial hepatectomy. 4. The rise in enzyme activities could be blocked by the injection of actinomycin D, and the Km values for UDP-glucose and UDP-galactose were nearly identical in regenerating and adult liver. It is therefore concluded that the increase in enzyme activity is due to synthesis de novo of enzyme protein.

Animals↗
PubMed1974

Studies on the golgi apparatus. Cumulative inhibition of protein and glycoprotein secretion by D-galactosamine.

1. The administration of d-galactosamine leads to inhibition of protein and glycoprotein secretion by rat liver. To test the secretory function, the secretion times for galactose-and fucose-containing glycoproteins were determined; they were lengthened from 6 to 9min and from 8 to 13min respectively. 2. The Golgi apparatus was enriched 100-120-fold relative to the homogenate. A new linked-assay system for the marker enzyme, UDP-galactose-N-acetyl-d-glucosamine galactosyltransferase, is presented. The activity of the enzyme was measured spectrophotometrically by following the formation of UDP coupled to nicotinamide nucleotide reduction. The Michaelis constants were calculated to be 0.11mm for UDP-galactose with N-acetyl-d-glucosamine as exogenous acceptor and 19mm for N-acetyl-d-glucosamine itself. 3. The physiological substrate of the galactosyltransferase, UDP-galactose, can be replaced by UDP-galactosamine, which accumulates after d-galactosamine administration. Under conditions in vitro the rate of d-galactosamine transfer to an endogenous acceptor protein of the Golgi fraction reaches 9% of that with d-galactose; this finding is noteworthy, because normally a non-acetylated amino sugar does not occur in glycoproteins. 4. The albumin content of the Golgi-rich fraction was diminished to 55% of the reference value 6h after the injection of 375mg of d-galactosamine hydrochloride/kg body wt. The transfer of d-[1-(14)C]galactose to an endogenous acceptor protein fell to 60% compared with Golgi-rich fractions from untreated animals. Analysis of the Golgi-rich fraction by polyacrylamide-gel electrophoresis showed a decrease or loss of several protein bands. 5. Protein synthesis can be restored by up to 80% if the UTP pool, decreased after d-galactosamine administration, is filled up by several injections of uridine. 6. From the results presented it can be concluded that the disturbed secretion of proteins and glycoproteins was due to a cumulative effect of galactosamine by: (a) inhibition of protein synthesis leading to a diminution of the endogenous acceptor pool of the galactosyltransferase; (b) inhibition of the galactosyltransferase activity by galactosamine metabolites and (c) replacement of UDP-galactose by UDP-galactosamine.

Animals↗