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Biomedical subjects

J Vachtenheim

Publications and source records attributed to J Vachtenheim.

At least 37 records · Page 2Linked to original sources
PubMed1990

[Tenoxicam in the long-term treatment of active rheumatoid arthritis].

The authors present the results of six months treatment with Tenoxicam (Tilcotil) in 30 patients with active rheumatoid arthritis. In no instance was it necessary to discontinue treatment, only one female patient complained of transient vertigo. During the final evaluation of the therapeutic effect as regards painfulness, sensitivity on palpation, oedema, restriction of movements, the author did not observe a satisfactory effect only in 8.5-24%. As regards hand grip, 20 m walk and consumption of analgesics the effect was also very satisfactory. Only four patients used occasionally Paracetamol or Alnagon, 1-2 tablets per day. The results achieved with this treatment indicate that it is a very good preparation suited for prolonged therapy of active rheumatoid arthritis, incl. patients of advanced age. Tenoxicam is particularly suited for a single dose per day (20 mg). It can be recommended also combined with gold therapy and treatment with antimalaric drugs.

Adult↗
PubMed1990

[Possibilities of dialysis therapy in irreversible renal failure in rheumatoid arthritis with secondary amyloidosis].

The authors discuss their initial experience with the treatment of secondary amyloidosis in rheumatoid arthritis with irreversible renal failure in patients included in a regular dialyzation programme. The hitherto assembled 15-month experience justifies the inclusion of patients with this cause of irreversible renal failure in a dialyzation programme. The reverse is not only wrong from the medical aspect but is inhuman and interferes with the life of families of these patients. Although the procedure during a regular dialyzation programme of these patients with rheumatoid arthritis with secondary amyloidosis is more complicated, more pretentious and more responsible, it is our medical duty to carry this burden together with the patient.

Amyloidosis↗
PubMed1988

Tyrosinase protein is expressed also in some neural crest derived cells which are not melanocytes.

Some neural crest cells give rise to pigment cells in early ontogenesis. We tested here whether tyrosinase--a key enzyme in melanogenesis--was present in some pigment neural crest derivatives in adult hamsters. Interestingly enough, inactive tyrosinase protein was detected, using indirect immunofluorescence, in the satellite cells of spinal ganglia and Schwann cells of sciatic and facial nerves in normal adult animals. The results of cell blotting from spinal ganglia were similar to the fluorescence findings. Thus, our results seem to support the hypothesis that Schwann cells, satellite cells of spinal ganglia, and melanocytes may be more intimately related developmentally than other neural-crest-derived cells. Moreover, since we detected tyrosinase protein in cells which normally do not produce melanosomes, it could be deduced that, during the melanocyte's differentiation from its cell precursor, the expression of tyrosinase protein might precede the point when melanosomes begin to differentiate from known cytoplasmic structures.

Animals↗
PubMed1987

Tyrosinase of hamster melanoma: its purification and estimation by radioimmunoassay.

1. Tyrosinase was purified from melanosomal fraction of hamster melanoma. 2. A radioimmunoassay was developed to quantitate the tyrosinase protein in hamster serum and hamster melanoma tissue using polyclonal anti-tyrosinase antibodies and 125I-labeled enzyme. 3. The serum tyrosinase levels were found to be about 0.24 micrograms and 1.14-4.48 micrograms/ml in normal hamsters and melanoma-bearing hamsters, respectively. 4. Tyrosinase protein in serum correlated significantly with the enzyme activity in hamsters with melanoma (r = 0.733). 5. In the cytosol fraction of hamster melanoma, a level of 2.2 micrograms of tyrosinase/mg protein was determined. 6. The usefulness and possible applications of the tyrosinase radioimmunoassay are discussed.

Animals↗
PubMed1986

Specific inhibition by antityrosinase antibodies of tyrosinase-mediated melanogenesis.

Polyclonal antibodies to hamster melanoma tyrosinase were raised in rabbits, and series of immunoinhibition experiments with a purified enzyme and specific immunoglobulins were carried out. Tyrosinase activity was determined by a set of radiochemical and spectrophotometric methods utilizing tyrosine, dopa, dopamine, or dihydroxyindole (DHI) as substrates. The quantitative data obtained indicated that the complexing of tyrosinase with its specific antibody inhibited melanogenesis in a specific manner: dopachrome formation from dopa and dopamine conversion to melanin were not affected and all other enzyme activities comprising the DHI oxidation step were inhibited to various degrees. Additionally, tyrosine hydroxylation was also slightly inhibited. The data obtained implied that melanogenesis was restricted at the point of DHI oxidation. From observations on the immunoinhibition of a DHI oxidation at varying dopa-cofactor concentrations, we propose that dopa-cofactor may be bound at separate site than DHI and thus may act as a positive allosteric effector for DHI oxidation by tyrosinase. Study of tyrosinase immunoinhibition by the antibodies against the enzyme thus seems to provide a valuable system for investigating the tyrosinase-mediated melanogenesis.

Animals↗
PubMed1985

A spectrophotometric assay for mammalian tyrosinase utilizing the formation of melanochrome from L-dopa.

A simple spectrophotometric method for a rapid determination of tyrosinase (EC 1.14.18.1) is described. The basis of the assay is the incubation of the enzyme with L-dopa in the presence of an optimal concentration of Zn2+ ions and the measurement of the formation of melanochrome, as indicated by the rise in absorbance at 540 nm. Final absorbance change reflects probably two activities of tyrosinase: the oxidation of dopa to dopaquinone and the conversion of 5,6-dihydroxyindole to melanochrome. Using a purified preparation from hamster melanoma, the assay was found to be more sensitive than the commonly used dopachrome assay. Comparison with some other currently available methods for assaying tyrosinase is presented and potential applications of the assay are discussed.

Animals↗
PubMed1984

An animal model for the survival of tyrosinase isozymes in serum.

Two tyrosinase isozymes were purified from pigmented hamster melanoma and injected i.v. into rats. It was shown that while T1 (sialylated) isozyme survived in the circulation, native asialo (T2) isozyme and neuraminidase-desialylated T1 isozyme disappeared from the circulation in a few minutes. Desialylated fetuin had a marked inhibitory effect on the removal of asialo-T1 tyrosinase. These data indicate that the enzyme tyrosinase shares the common pattern of clearance from circulation known for the majority of serum glycoproteins. The electrophoretic pattern of tyrosinase isozymes partially purified from the sera of melanoma-bearing animals were compared with those from the soluble fraction of the tumors. In hamsters, melanoma tissue revealed both T1 and T2 isozymes while serum exhibited T1 and very weak T2, supporting the mechanism of clearance demonstrated in rats. In mice bearing Cloudman S-91 or B-16 melanomas, only T1 isozyme was seen in sera and in tumors.

Animals↗