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Biomedical subjects

K Kowalski

Publications and source records attributed to K Kowalski.

At least 19 recordsLinked to original sources
PubMed1991

Functional properties of crossed spinocerebellar tract neurones with cell bodies in the S1 segment.

Functional properties of a crossed spinocerebellar tract with cell bodies located in laminae VII and IX of the S1 segment were investigated using intracellular recording. The neurones were found to be excited by group I and II muscle afferents and afferents of skin, joint and interosseus nerves. Volleys from group II muscle afferents and cutaneous afferents evoked inhibition in these cells. It is concluded that S1 spinocerebellar neurones convey a similar type of information to that of dorsal spinocerebellar tract and ventral spinocerebellar tract neurones but integrate it in a different way.

Animals↗
PubMed1991

Dynorphin expression and Fos-like immunoreactivity following inflammation induced hyperalgesia are colocalized in spinal cord neurons.

Fos and Fos-related proteins are increased in spinal dorsal horn neurons following noxious stimulation. The laminar location of neurons that exhibit this increase is coincident with those that exhibit an increase in dynorphin in a rat model of peripheral inflammation and hyperalgesia. In order to determine whether the increase in Fos or related proteins and dynorphin occurs in the same dorsal horn neurons, two kinds of double-labeling methods were used: in situ hybridization histochemistry to label dynorphin mRNA autoradiographically, and immunocytochemistry to label Fos and Fos-related proteins, or a double immunocytochemical method that labeled Fos and Fos-related proteins and dynorphin peptide with distinct chromagens. With both methods more than 80% of the neurons in laminae I, II, V and VI exhibiting an increase in either dynorphin mRNA or peptide following peripheral inflammation also colocalized increased nuclear Fos-like immunoreactivity. However, the number of neurons displaying increased Fos-like immunoreactivity was substantially greater than the number of neurons colocalizing increased dynorphin. These data suggest that the activation of nuclear Fos and Fos-related proteins may be related to the induction of dynorphin gene expression in a subpopulation of spinal cord neurons following peripheral inflammation and hyperalgesia.

Animals↗
PubMed1991

No happy ending: pregnancy loss and bereavement.

Bleeding in pregnancy signals not only danger but often failure and loss and the start of bereavement. This chapter identifies types of loss experienced in pregnancy and the bereavement process. In addition, the social aspects of bereavement as they concern marital relationships are identified. The impact of the personal losses of those in the helping profession also are discussed. Working with parents experiencing perinatal death should include interventions involved with physical care, psychological support, and aspects of perinatal death education. Follow-up care is critical to the ongoing assessment and evaluation of parents' progress through the bereavement process. Specific aspects of follow-up care are suggested, including data and information regarding parent support groups.

Abortion, Spontaneous↗
PubMed1989

Dynamics of the Adair model for ligand-receptor binding.

The dynamics of the Adair model for ligand-receptor binding involving the case with interacting receptors is investigated. Using the methods of formal reaction kinetics, the existence, uniqueness, and asymptotic stability of equilibria within the model are demonstrated. The approximate solutions to the Adair model are found.

Kinetics↗
PubMed1988

The pontocerebellar efferents from the pontine reticular tegmental nucleus in the rabbit: differential projections to the paramedian sublobules as revealed with tracing of retrograde axonal transport of horseradish peroxidase.

Projections from the nucleus reticularis tegmenti (NRTP) pontis to the cerebellar paramedian lobule were studied using a horseradish peroxidase retrograde transport technique. The rabbit's NRTP consists of a medial principal part (the nucleus papillioformis: PLF) and smaller lateral part (the processus tegmentosus lateralis: PTL). The PLF can be subdivided into a dorsomedial part--zone A, a ventrolateral part--zone C, and a main part--zone B. Zone B is furthermore divisible into the subzones: B1, B2, and B3. In addition, some cells of zone B3 invade the fiber bundles of the medial lemniscus. Experimental data have indicated a topographically organized bilateral projection from the NRTP to the anterior, the middle and the posterior folia of the paramedian lobule with some degree of contralateral dominance. In contrast to an earlier report in cats we find that not only the ventral, but also the dorsal region of the NRTP send projections onto the paramedian lobule. The neurons sending axons to the paramedian lobule are localized mainly in the middle and to a some degree in the posterior thirds of the NRTP. Zones A, B1 and B3 project onto all of sublobules of the paramedian lobule. While zone A projects primarily onto the anterior sublobules (e, f), zone B1 emanates to the middle paramedian sublobules (c, d), Zone B3 sends fibers mainly into the posterior sublobules (a, b) and to a some degree to the middle paramedian sublobules. Zone B2 distributes a few axons exclusively to the middle folia of the paramedian lobule, while the middle part of the PTL gives rise to small bilateral projection to sublobules c and d of the paramedian lobule. Neurons of zone C send projections into the middle folia of the paramedian lobule. These findings are discussed in relationship to other morphological and physiological data on neurons of the pontine reticular tegmental nucleus.

Animals↗
PubMed1979

Modification of human placental lactogen with plasmin. Preparation and characterization of a modified hormone with increased biologic activity.

To determine the structure needed for the biologic activity of human placental lactogen (hPL), we have cleaved hPL with the proteolytic enzyme plasmin. Plasmin modified hPL (PL-hPL) was purified by gel chromatography. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis before and after reduction showed that cleavage had occurred within the Cys53-Cys165 loop and tryptic peptide maps revealed that a single peptide consisting of residues 135 to 140 had been removed. 5-Dimethylaminonaphthalene-1-sulfonyl end group analysis and digestion with carboxypeptidase B confirmed that cleavage was complete and only the single hexapeptide was removed. In a membrane binding assay for lactogenic activity PL-hPL was 2- to 3-fold more potent than hPL. Using growth hormone receptors from rabbit liver membranes, PL-hPL was also more potent than hPL, but still much less potent than growth hormone. The lactogenic activity of PL-hPL in an in vitro bioassay was 75% above that of unmodified hormone. It is concluded that plasmin cleaves homologous peptides from hPL and growth hormone and that removal of the hexapeptide from hPL results in enhanced biologic activity.

Amino Acids↗
PubMed1979

Preparation of a disulfide-linked dimer of human placental lactogen fragment 1--134 with immunologic and biologic activity.

In order to determine the chemical features of human placental lactogen (hPL) necessary for its biologic activity we prepared the following fragments from the plasmin-cleaved hormone: reduced and alkylated 1--134, reduced and alkylated 141--191, and a 1--134 dimer joined through the single cysteinyl residue at position 53. In a radioimmunoassay using antibodies against native hPL, the two reduced and alkylated fragments produced nonparallel displacement and had less than 1% of the activity of hPL. The ability of reduced and alkylated 1--134 to bind to mammary gland receptors was less than 5% of that of hPL; reduced and alkylated 141--191 showed no detectable activity in the same assay. The 1--134 dimer, in contrast, had 20% of the immunologic activity and 30% of the ability to bind to lactogenic receptors relative to the native hormone. In an in vitro bioassay the lactogenic activity of the 1--134 dimer was equivalent to that of the native hormone. The circular dichroic spectra of hPL, reduced and alkylated 1--134, and 1--134 dimer indicated that the dimer had regained much of the helical content of the native hormone. Antibodies produced to reduced and alkylated 1--134 did not significantly crossreact with either native hPL or 1--134 dimer. From these data we conclude that the information for the lactogenic activity of hPL is contained in the first 134 amino acid residues and that the proper conformation is necessary for its biologic expression.

Amino Acids↗
PubMed1977

Dimeric ("big") human placental lactogen. Immunological and biological activity.

Dimeric ("big") human placental lactogen has been isolated in near homogeneous form from placental tissue. It consists of a disulfide-linked (stable) form and a noncovalently associated (unstable) form of the native hormone. The two forms were separated by exposure to denaturing conditions and resolution by gel exclusion chromatography. Both forms retained immunological activity, ability to bind mammary membranes, and ability to induce mammary N-acetyllactosamine synthetase in vitro. On a molar basis, stable dimeric placental lactogen was more active than placental lactogen in the radioimmunoassay indicating that the immunological determinants on both monomeric units could bind to antibody. On a molar basis, stable dimeric placental lactogen was equally active with monomeric placental lactogen in competing for mammary gland membrane binding sites, indicating that only one active site in the molecule could interact with the membrane at a time. Stable dimeric placental lactogen was also active in an in vitro bioassay using the induction of N-acetyllactosamine synthetase. It is concluded that dimer formation does not alter the biologically active portion of the placental lactogen molecule. Since the carboxyl-terminal region (residues 182-191) is involved in the interchain disulfide bonds of dimeric placental lactogen, this portion of the molecule is probably not necessary for its biological activity.

Animals↗
PubMed1977

Team nursing coverage of prenatal-intrapartum patients at a university hospital. An innovation in obstetric nursing.

A unique approach in utilization of nursing personnel was instituted at the University of Colorado Medical Center to alleviate the following patient care problems: 1) lack of continuity of care of obstetric patients, 2) inadequate prenatal instruction, and 3) the unpredictability of patient census in the labor and delivery area. Half the nurses from the labor and delivery area were organized into four teams of two nurses each who acquired a case load of patients for antepartum care. When a patient was admitted to the hostpial in labor, the nurse from her team who was on call came in and provided all nursing care during the intrapartum period. The problems and benefits of this new approach to nursing care are discussed.

Colorado↗