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Biomedical subjects

W Klee

Publications and source records attributed to W Klee.

At least 37 records · Page 2Linked to original sources
PubMed1992

[Modification of the concentration of creatinine and sodium in blood serum and urine and the fractional elimination of sodium by electrolyte therapy in calves].

In 32 calves, creatinine and sodium concentrations were determined in blood and urine samples taken simultaneously four times during two periods of two days each (control period: milk or milk replacer; trial period: oral electrolyte solution). Creatinine urine/serum ratios and fractional elimination of sodium (FENa) were calculated. The influence of the type of liquid feed on these parameters was evaluated statistically. Calves fed milk replacer had higher urine sodium concentrations and FENa than calves fed whole milk. All parameters determined were influenced by intake of oral electrolyte solution: creatinine concentrations in serum and urine decreased, whereas sodium concentrations in serum and urine, as well as FENa, increased. It is concluded that sodium content of liquid feed significantly influences FENa.

Animal Feed↗
PubMed1992

[Elimination kinetics of several clinically relevant enzymes in the blood plasma of cattle after intravenous bolus infusion of homologous preparations].

Extracts of homologous organs (liver, muscle) and of colostrum were infused intravenously in cattle of two different age groups: heifers (n = 9, each preparation was infused in 3 animals) and calves (n = 6, preparations from liver and muscle were infused in 3 animals each). Parameters of elimination kinetics were determined for some clinically relevant enzymes. Enzyme elimination was quicker in the younger animals. The volume of enzyme distribution was comparable to plasma volume. Biological half-lives in calves and heifers respectively were: CK from muscle 3.46 +/- 0.65 h and 8.27 +/- 3.27 h, AST from muscle 9.74 +/- 1.38 h and 33.48 +/- 3.74 h, AST from liver 14.99 +/- 0.81 h and 16.71 +/- 0.58 h, GLDH from liver 14.61 +/- 1.88 h and 25.09 +/- 4.13 h, SDH from liver 13.95 +/- 2.25 h and 17.68 +/- 0.81 h, GGT from colostrum 1.69 +/- 0.95 h (only heifers).

Animals↗
PubMed1990

[Boogenic human diseases].

Basing on observations from practice and clinic, a survey is given (in two tables) concerning the disturbances of human health due to the handling of cattle, and their causes.

Animals↗
PubMed1989

[Epidemiologic, clinical and pathologo-anatomic studies of the inflammation of the carpal joint extensors in cattle].

A retrospective study of 24 cases of inflammation of carpal extensors (m. extensor carpi radialis, m. extensor digitorum communis, m. abductor digiti I longus) was conducted. The findings of anamnestic, clinical, and post-mortem investigations are described. Half of the patients were first calf heifers at the ages of 2 1/2 to 3 years. The rest of the animals were older cows (with one exception). In all of the young cows the disease had become apparent within 11 weeks post partum. The most striking clinical finding is the posture of the animals when lying down: the affected forelimbs are extended forward. Palpation reveals a homogeneous firm swelling of the cranial portion of the forearm. Most of the patients also had pododermatitis in hind and/or front legs, and exhibited signs of a systemic reaction in the form of "polysynovitis" and raised serum total protein concentrations. Post mortem examination revealed a hemorrhagic edematous impregnation of the distal part of the radial carpal extensor muscle and particularly of its fascia. The tendon and tendon sheath had unclear contours and were swollen. Histologically the lesions are typical of subacute granulating inflammation. As to the cause, it is assumed that the ailment is a significant complication of some other disease of the locomotion system. Type and localization of the lesions suggest a traumatic etiology. Therapeutic results have been unsatisfactory.

Animals↗
PubMed1986

Bradykinin-activated transmembrane signals are coupled via No or Ni to production of inositol 1,4,5-trisphosphate, a second messenger in NG108-15 neuroblastoma-glioma hybrid cells.

The addition of bradykinin to NG108-15 cells results in a transient hyperpolarization followed by prolonged cell depolarization. Injection of inositol 1,4,5-trisphosphate or Ca2+ into the cytoplasm of NG108-15 cells also elicits cell hyperpolarization followed by depolarization. Tetraethylammonium ions inhibit the hyperpolarizing response of cells to bradykinin or inositol 1,4,5-trisphosphate. Thus, the hyperpolarizing phase of the cell response may be due to inositol 1,4,5-trisphosphate-dependent release of stored Ca2+ into the cytoplasm, which activates Ca2+-dependent K+ channels. The depolarizing phase of the cell response to bradykinin is due largely to inhibition of M channels, thereby decreasing the rate of K+ efflux from cells and, to a lesser extent, to activation of Ca2+-dependent ion channels and Ca2+ channels. In contrast, injection of inositol 1,4,5-trisphosphate or Ca2+ into the cytosol did not alter M channel activity. Incubation of NG108-15 cells with pertussis toxin inhibits bradykinin-dependent cell hyperpolarization and depolarization. Bradykinin stimulates low Km GTPase activity and inhibits adenylate cyclase in NG108-15 membrane preparations but not in membranes prepared from cells treated with pertussis toxin. Reconstitution of NG108-15 membranes from cells treated with pertussis toxin with nanomolar concentrations of a mixture of highly purified No and Ni [guanine nucleotide-binding proteins that have no known function (No) or inhibit adenylate cyclase (Ni)] restores bradykinin-dependent activation of GTPase and inhibition of adenylate cyclase. These results show that [bradykinin . receptor] complexes interact with No or Ni and suggest that No and/or Ni mediate the transduction of signals from bradykinin receptors to phospholipase C and adenylate cyclase.

Adenylate Cyclase Toxin↗
PubMed1986

Use of specific antibodies to quantitate the guanine nucleotide-binding protein Go in brain.

We immunized rabbits with purified guanine nucleotide-binding proteins (G proteins) from bovine brain and obtained an antiserum, RV3, that reacts specifically with the alpha subunit (39 kDa) of a G protein of unknown function, termed Go, as well as with the beta subunit (35 kDa) common to all G proteins. RV3 showed no crossreactivity with the alpha subunits of the stimulatory (Gs) or inhibitory (Gi) G proteins associated with adenylate cyclase, nor with that of the rod outer segment G protein, transducin. Immunoblots with crude and affinity-purified antiserum showed that RV3 specifically recognizes the Go alpha subunit and the beta subunit in crude brain membranes. Using RV3, we found approximately equal amounts of Go in brain membranes from frog, chicken, rat, cow, and man. Quantitative immunoblotting gave Go alpha subunit/ beta subunit ratios approximately equal to 1 in cerebral cortex, raising the possibility that free Go alpha subunit (unassociated with beta subunit) may exist in brain. The concentration of Go alpha subunit in cortex is about 5 times that of Gi alpha subunit. The results show that Go is an immunochemically distinct, highly conserved protein distributed throughout the brain, with particularly high concentrations in forebrain.

Animals↗
PubMed1985

Antibodies against the carboxyl-terminal 5-kDa peptide of the alpha subunit of transducin crossreact with the 40-kDa but not the 39-kDa guanine nucleotide binding protein from brain.

We tested 18 antisera showing reactivity against the alpha subunit of transducin, the guanine nucleotide binding protein from rod outer segment, for crossreactivity against the 40- and 39-kDa guanine nucleotide binding proteins purified from bovine brain. A single antiserum, CW6, showed crossreactivity, and this was predominantly against the 40-kDa protein. Immunoblots of the tryptic fragments of transducin alpha subunit with multiple antisera raised against that subunit showed that only CW6 recognizes a COOH-terminal 5-kDa peptide that includes the site of pertussis toxin ADP-ribosylation. Antibodies against the 5-kDa peptide, affinity-purified from CW6, specifically react with the 40-kDa brain protein on immunoblots. The results show that the 39- and 40-kDa guanine nucleotide binding proteins from brain differ immunochemically and that the COOH-terminal 5-kDa peptide of transducin alpha subunit is homologous to a region in the 40-kDa brain protein. We speculate that this homologous region may be in a domain that confers specificity for receptor interactions of guanine nucleotide binding proteins.

Adenosine Diphosphate Ribose↗
PubMed1984

[Morphologic knowledge of polyneuropathy in progressive scleroderma].

The occurrence of polyneuropathy in connection with systemic sclerosis is extremely rare. Proliferative changes leading to mechanical compression of the nerves have been ascribed to an etiological involvement. In the case reported here, polyneuropathy could be verified morphologically (nervebiopsy). The elevated IgG in the cerebrospinal fluid suggests inflammatory changes of the nerves to be the cause of polyneuropathy.

Axons↗