Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 4 de 4
Filter
1.
Int J Law Psychiatry ; 76: 101695, 2021.
Article in English | MEDLINE | ID: mdl-33761439

ABSTRACT

The practice of involuntary psychiatric commitment is central to the acute treatment of persons with severe mental illness and others in psychiatric crisis. Deciding whether a patient should be admitted involuntarily requires weighing respect for autonomy against beneficence, considering the clinical needs of the patient, and navigating ambiguous legal standards. The relative dearth of information about the impact of involuntary commitment on objective patient outcomes complicates matters ethically, legally, and clinically. To address this gap in the literature, we sought to determine the association between temporary psychiatric holds and length of stay and readmission rates among a retrospective sample of adult patients admitted to a large psychiatric hospital with diagnoses of schizophrenia, schizoaffective disorder, mania, and other psychotic disorders. In total, we identified 460 patients and 559 unique encounters meeting our inclusion criteria; 90 of the encounters were voluntary (involving a temporary psychiatric hold) and 469 were involuntary. Univariable and multivariable analyses suggested that temporary psychiatric holds were not significantly associated with either length of stay or readmission rate. These findings are relevant to clinicians who must decide whether to admit a patient involuntarily, as they suggest that making a patient involuntary is not associated with differences in length of stay or readmission risk.


Subject(s)
Mental Disorders , Psychotic Disorders , Adult , Commitment of Mentally Ill , Hospitalization , Humans , Length of Stay , Patient Readmission , Retrospective Studies
2.
Acad Psychiatry ; 41(5): 582-586, 2017 Oct.
Article in English | MEDLINE | ID: mdl-28707231

ABSTRACT

OBJECTIVE: This report examines the experience of one institution's development of the first student-run psychiatry clinic that serves both adult and pediatric populations. METHODS: The clinic is held weekly with pre-clinical and clinical medical student volunteers under the supervision of board-certified adult and child psychiatrists. The development and evolution of the clinic over time are evaluated with particular attention to obstacles overcome. Medical student volunteers were surveyed retrospectively to evaluate their experience with patients with psychiatric illness, skill development, and interest in psychiatry. RESULTS: Since January 2016, the clinic has scheduled 90 patients, 32% of which were pediatric patients. Ninety-six medical students have volunteered, with roughly equal parts from all four medical school classes. Respondents to the experience survey showed marked improvement in their comfort working with patients with mental illness. Additionally, 40% "strongly agreed" or "agreed" that their experience influenced their interest in pursuing psychiatry as a career. CONCLUSION: This report describes a student-run psychiatry clinic with a dual mission of education and service, and the challenges associated with these sometimes competing goals. This clinic serves a vital need within our community and may be an example of the role that student-run clinics can have in fostering interdisciplinary care, psychiatric recruitment, and training for medical students.


Subject(s)
Adolescent Psychiatry/organization & administration , Ambulatory Care Facilities/organization & administration , Child Psychiatry/organization & administration , Mental Disorders/therapy , Schools, Medical/organization & administration , Students, Medical , Adult , Female , Humans , Male , Young Adult
3.
PLoS One ; 8(2): e56780, 2013.
Article in English | MEDLINE | ID: mdl-23418601

ABSTRACT

Mucolipidosis type IV is a lysosomal storage disorder resulting from mutations in the MCOLN1 gene, which encodes the endosomal/lysosomal Transient Receptor Potential channel protein mucolipin-1/TRPML1. Cells isolated from Mucolipidosis type IV patients and grown in vitro and in in vivo models of this disease both show several lysosome-associated defects. However, it is still unclear how TRPML1 regulates the transport steps implicated by these defects. Identifying proteins that associate with TRPML1 will facilitate the elucidation of its cellular and biochemical functions. We report here two saturation screens for proteins that interact with TRPML1: one that is based on immunoprecipitation/mass spectrometry and the other using a genetic yeast two-hybrid approach. From these screens, we identified largely non-overlapping proteins, which represent potential TRPML1-interactors., Using additional interaction assays on some of the potential interactors from each screen, we validated some proteins as candidate TRPML1 interactors In addition, our analysis indicates that each of the two screens not only identified some false-positive interactors, as expected from any screen, but also failed to uncover potential TRPML1 interactors. Future studies on the true interactors, first identified in these screens, will help elucidate the structure and function of protein complexes containing TRPML1.


Subject(s)
Mucolipidoses/metabolism , Protein Interaction Mapping/methods , Proteins/metabolism , Transient Receptor Potential Channels/metabolism , Animals , Blotting, Western , Cell Line , Green Fluorescent Proteins/genetics , Green Fluorescent Proteins/metabolism , HeLa Cells , Humans , Immunoprecipitation/methods , Mass Spectrometry/methods , Mice , Microscopy, Confocal , Mucolipidoses/genetics , Mutation , Protein Binding , Proteins/genetics , Transient Receptor Potential Channels/genetics , Two-Hybrid System Techniques
4.
Traffic ; 12(10): 1417-31, 2011 Oct.
Article in English | MEDLINE | ID: mdl-21722281

ABSTRACT

Cells have to maintain stable plasma membrane protein and lipid compositions under normal conditions and to remodel their plasma membranes in response to stimuli. This maintenance and remodeling require that integral membrane proteins at the plasma membrane that become misfolded, because of the relatively harsher extracellular milieu or carbohydrate and amino acid sequence changes, are degraded. We had previously shown that Derlin proteins, required for quality control mechanisms in the endoplasmic reticulum, also localize to endosomes and function in the degradation of misfolded integral membrane proteins at the plasma membrane. In this study, we show that Derlin proteins physically associate with sorting nexins that function in retrograde membrane transport from endosomes to the Golgi apparatus. Using genetic studies in Caenorhabditis elegans and ricin pulse-chase analyses in murine RAW264.7 macrophages, we show that the Derlin-sorting nexin interaction is physiologically relevant. Our studies suggest that at least some integral membrane proteins that are misfolded at the plasma membrane are retrogradely transported to the Golgi apparatus and ultimately to the endoplasmic reticulum for degradation via resident quality control mechanisms.


Subject(s)
Caenorhabditis elegans Proteins/metabolism , Endosomes/metabolism , Golgi Apparatus/metabolism , Membrane Proteins/metabolism , Animals , Blotting, Western , Caenorhabditis elegans/genetics , Caenorhabditis elegans/metabolism , Endocytosis/physiology , HeLa Cells , Humans , Immunoprecipitation , Macrophages/metabolism , Macrophages/physiology , Mice , Protein Folding , Protein Transport , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sorting Nexins/metabolism , Two-Hybrid System Techniques
SELECTION OF CITATIONS
SEARCH DETAIL
...