PubMed Health⌕ Search

Biomedical subjects

K Cauley

Publications and source records attributed to K Cauley.

11 recordsLinked to original sources
PubMed2001

Service learning: integrating student learning and community service.

Health professions education is directly effected by changes in health care service delivery and financing systems. In the United States, as the health care industry increasingly shifts to a market economy, service delivery venues are moving away from acute care facilities and into community-based settings. Additionally, there is increased emphasis on primary prevention programs, often provided in public health settings. For health professions programs that traditionally provide clinical training in hospitals and long-term care facilities, there are unique challenges associated with identifying new venues in order to insure that students are exposed to a wide variety of patients with a range of chronic to acute disease conditions. One set of tools that has demonstrated usefulness during these kinds of transitions is service learning. This teaching methodology emphasizes increased partnership with clinical training sites, extensive orientation to patient populations and community resources, structured reflection and instilling the ethic of service in future health care providers. Although this article describes utilization of service learning in the context of current conditions in the United States, we hope that the principles presented here can be readily adapted in any setting.

Journal Article↗
PubMed2000

"The history of health in Dayton": a community-academic partnership.

Academic institutions have always found it a challenge to persuade community members to participate in academic research projects. Starting an open dialogue is usually the critical first step. To begin this dialogue with community members in Dayton, Ohio, in 1999, staff from Wright State University decided to organize a community forum, "The History of Health in Dayton." The forum was intended as the first project of a new research organization, the Alliance for Research in Community Health (ARCH), established with federal funding from the Health Resources and Services Administration in 1998. ARCH was created as a bridge between the Department of Family Medicine of Wright State University School of Medicine and the Center for Healthy Communities, a health advocacy and service organization committed to health professions education. ARCH's mission is to improve the health of citizens of Dayton through research involving community participation. Through ARCH, community members help researchers define priorities, resolve ethical issues, refine procedures, and interpret results. Guidelines for participatory research, proposed by the National Primary Care Research Group in 1998 and adopted by the alliance, emphasize the importance of open dialogue among researchers, subjects, academics, and community members. The initial response to the forum was enthusiastic, with a majority of community residents expressing interest in attending future presentations.

Community Health Planning↗
PubMed1997

Kainate/AMPA receptors expressed on human fetal astrocytes in long-term culture.

Long-term cultivation of primary human fetal brain cells has yielded a homogeneous population of glial progenitors of extended life span. These human astrocyte precursor (HAP-1) cells have been in culture for greater than 1 year, are diploid, and do not form colonies in soft agar. The culture was established in 10% fetal calf serum (FCS), although cells greatly increase their proliferative rate when both basic fibroblast growth factor and FCS are present in the culture media. HAP-1 cells express the cytoskeletal proteins glial fibrillary acidic protein, vimentin, and nestin. HAP-1 cells express the AMPA/kainate receptor subunit genes GluRs 1, 3, and 4 and the kainate receptor subunit genes GluR6, KA1, and KA2. Immunohistochemistry confirms the expression of GluR subunit proteins. HAP-1 cells demonstrate a kainate-responsive current found to be blockable by CNQX. HAP-1 cells will serve in the study of human glial cells and ligand-gated ion channels and in the identification of compounds which might act as agonists or antagonists at these receptor-ion channel complexes.

6-Cyano-7-nitroquinoxaline-2,3-dione↗
PubMed1996

Nicotinic receptor subunits alpha 3, alpha 4, and beta 2 and high affinity nicotine binding sites are expressed by P19 embryonal cells.

Controlled exposure to retinoic acid (RA) induces the murine embryonal carcinoma cell line P19S18O1A1 (P19) to differentiate into a variety of cell types. One of the cell types exhibits neuronal-like morphology and expresses neuronal markers including neurofilament proteins, glutamate receptors, and the cholinergic enzymes choline acetyl-transferase and acetylcholinesterase. In this study we use Northern blot analysis, double-label immunocytochemistry, and single cell RNA analysis using polymerase chain reaction to show that RA-treated P19 cells with neuronal-like morphology also express neuronal nicotinic acetylcholine receptor (nAChR) subunits alpha 3, alpha 4, and beta 2. Greater than 80% of RA-treated P19 cells with a neuronal-like phenotype express nAChR alpha 4 subunit transcripts and both alpha 4 and beta 2 protein. The RA-induced expression of alpha 3 transcripts accounts for a comparably small number of nAChR-containing cells (< 20%) of which half coexpress alpha 4 transcripts. Expression of high-levels of alpha 4 RNA is dependent upon both cell-cell contact and RA exposure. The appearance of nAChR subunits also coincides with RA-induced expression of high affinity [3H]-nicotine binding receptors. The P19 cell line offers an inducible neuronal cell system to study mammalian neuronal nicotinic receptor expression and the development of high affinity nicotinic binding sites similar to those expressed in the mammalian central nervous system.

Animals↗
PubMed1996

Kainic acid induced excitotoxicity and cfos expression in fibroblasts transfected with glutamate receptor subunit, GluR1.

Glutamate receptors participate in the majority of fast excitatory neurotransmission in the mammalian brain. Excessive excitation of these receptors has been linked to neuronal dysfunction and death through a process termed excitotoxicity. In this study we demonstrate that transfection of a single non-NMDA glutamate receptor subunit, GluR1, into cultured fibroblasts is sufficient to confer kainic acid mediated excitotoxicity similar to that seen in neuronal cells. Death of transfected cells requires at least 24 h of continuous exposure to kainic acid and can be blocked with a glutamate receptor antagonist. Also, the induction of protooncogene cfos transcripts occurs 30 min following kainic acid administration, and Fos protein accumulated in the nucleus within 90 min. These observations suggest that the signaling system(s) required to initiate gene expression and kainic acid excitotoxicity from a neuronal ionotropic receptor to the nucleus is present in these nonneuronal cells. Finally, antibodies prepared to amino acids 185-449 of GluR1 are demonstrated to be useful for fluorescence-activated sorting of live cells transfected with a GluR1 expression vector. This supports the conclusion that this region of the protein is located extracellularly.

Animals↗
PubMed1994

Autoantibodies to glutamate receptor GluR3 in Rasmussen's encephalitis.

Rasmussen's encephalitis is a progressive childhood disease of unknown cause characterized by severe epilepsy, hemiplegia, dementia, and inflammation of the brain. During efforts to raise antibodies to recombinant glutamate receptors (GluRs), behaviors typical of seizures and histopathologic features mimicking Rasmussen's encephalitis were found in two rabbits immunized with GluR3 protein. A correlation was found between the presence of Rasmussen's encephalitis and serum antibodies to GluR3 detected by protein immunoblot analysis and by immunoreactivity to transfected cells expressing GluR3. Repeated plasma exchanges in one seriously ill child transiently reduced serum titers of GluR3 antibodies, decreased seizure frequency, and improved neurologic function. Thus, GluR3 is an autoantigen in Rasmussen's encephalitis, and an autoimmune process may underlie this disease.

Animals↗
PubMed1994

Kappa B enhancer-binding complexes that do not contain NF-kappa B are developmentally regulated in mammalian brain.

DNA-binding complexes which are temporally regulated in developing rat brain have been identified by their ability to interact with the kappa B enhancer sequence in electrophoretic mobility-shift assays. These complexes, referred to as developing-brain factors (DBFs) 1 and 2, are abundant in nuclear extracts from developing rat brain through postnatal day 2 and decline to nearly undetectable levels by postnatal day 7. DBFs were not detected in extracts from cultured cell lines or in tissues other than the developing brain. The highest level of DBF DNA-binding activity was observed in developing cortex, and the lowest in cerebellum. In UV crosslinking experiments, a labeled kappa B oligonucleotide probe crosslinked 110- and 115-kDa proteins from DBF complexes. DBFs are likely to be involved in the regulation of transcriptional events which take place during brain development.

Age Factors↗
PubMed1993

Selective distribution of kainate receptor subunit immunoreactivity in monkey neocortex revealed by a monoclonal antibody that recognizes glutamate receptor subunits GluR5/6/7.

A monoclonal antibody (4F5) was generated against a portion of the putative extracellular domain of glutamate receptor subunit GluR5. Western blot analyses and immunocytochemistry of transfected human embryonic kidney 293 cells confirmed that monoclonal antibody 4F5 was specific for GluR5, -6, and -7 (the three identified members of the kainate receptor subunit class), but did not recognize GluR1, -2, or -3 (the AMPA/kainate receptor subunit class). The antibody was subsequently used to examine immunocytochemically the regional, laminar, and cellular distribution of GluR5/6/7 receptor subunits at the light and electron microscopic levels in monkey neocortex. Receptor subunit immunoreactivity was present throughout all cortical areas examined, but exhibited marked cellular, laminar, and regional specificity. Typically, pyramidal cell somata and apical dendrites were well stained. Electron microscopy revealed an extensive cytoplasmic localization of GluR5/6/7 immunoprecipitate, with intense staining of many postsynaptic densities, all of which were associated with asymmetric synapses located on dendritic shafts or dendritic spines. There was no evidence of stained glial cells or presynaptic axon terminals. In most areas, labeled cells and dendrites were concentrated in layers II, III, and V while layers I, IV, and VI typically possessed the fewest and/or least intensely stained elements. A consistent feature in many areas was groups of clustered layer V pyramidal cells and bundles of ascending apical dendrites. Regionally, motor areas and higher-order association areas of the frontal, parietal, and occipital lobes were more densely stained than primary sensory areas (somatic sensory and visual cortex), which was confirmed quantitatively. These data indicate a high degree of selectivity in the distribution of kainate receptors composed of GluR5/6/7 subunits, and suggest that functional specificity and diversity in the ubiquitous excitatory amino acid-utilizing axonal systems in neocortex are achieved in part by the differential association of particular glutamate receptor subunits with specific cortical circuits. In addition, the regional, laminar, and morphological characteristics of GluR5/6/7-immunoreactive neurons bear a strong similarity to those of the neocortical neurons with heightened vulnerability in certain neurodegenerative disorders.

Analysis of Variance↗
PubMed1990

Multiple nicotinic acetylcholine receptor genes are expressed in goldfish retina and tectum.

cDNAs encoding a novel nAChR structural subunit (GFn alpha-3) and a ligand-binding subunit (GF alpha-3) have been isolated from a goldfish retina cDNA library. The protein encoded by GFn alpha-3 shares 88% amino acid similarity with that encoded by GFn alpha-2, a structural subunit gene previously identified to be expressed in this system (Cauley et al., 1989). The ligand-binding subunit (GF alpha-3) is likely the goldfish homolog of the rat alpha-3 gene (Boulter et al., 1986). Northern blots and S1 protection experiments show that GFn alpha-3 and GF alpha-3 genes are expressed in retina and brain. GFn alpha-3 identifies multiple RNAs differing in their 3' untranslated regions. In situ hybridization analysis demonstrates GFn alpha-3, GFn alpha-2, and GF alpha-3 expression by cells of the retinal ganglion cell layer. Unlike GFn alpha-2 and GF alpha-3, GFn alpha-3 is expressed at highest levels by cells of the retina's inner nuclear layer. In the optic tectum, both GF alpha-3 and GFn alpha-3 genes are expressed by cells of the periventricular zone, as well as more superficial layers. These results suggest the presence of multiple nAChR systems in retina and tectum. In addition, they indicate that tectal nAChRs may arise from remote (ganglion cell) as well as local (tectal cell) synthesis.

Animals↗
PubMed1989

Identification of a novel nicotinic acetylcholine receptor structural subunit expressed in goldfish retina.

A new non-alpha (n alpha) member of the nicotinic acetylcholine receptor (nAChR) gene family designated GFn alpha-2 has been identified in goldfish retina by cDNA cloning. This cDNA clone encodes a protein with structural features common to all nAChR subunits sequenced to date; however, unlike all known alpha-subunits of the receptor, it lacks the cysteine residues believed to be involved in acetylcholine binding. Northern blot analysis shows multiple transcripts hybridizing to the GFn alpha-2 cDNA in goldfish retina but undetectable levels of hybridizable RNA in brain, muscle, or liver. S1 nuclease protection experiments indicate that multiple mRNAs are expressed in retina with regions identical or very similar to the GFn alpha-2 sequence. In situ hybridization shows that the gene encoding GFn alpha-2 is expressed predominantly in the ganglion cell layer of the retina.

Amino Acid Sequence↗