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1.
Community Ment Health J ; 58(8): 1544-1553, 2022 11.
Artículo en Inglés | MEDLINE | ID: mdl-35524906

RESUMEN

Increasing social connection and access to care has been found to decrease the rate of suicide in U.S. veterans. The Veteran Outreach Into the Community to Expand Social Support (VOICES) is an intervention developed by Department Veteran Affairs (VA) staff to improve social connection and provide information about services by implementing community-based Veterans Socials. Seventy veterans at eight locations completed an anonymous cross-sectional survey. This evaluation examined three domains, acceptability (i.e., perceived value), demand (i.e., estimated or actual use), and expansion (i.e., sustainability and increase of Veterans Socials across time and locations). Findings indicated considerable levels of acceptability, demand for, and expansion of this intervention. Additionally, data suggested this intervention may increase social connection and utilization of VA services among attendees.


Asunto(s)
Veteranos , Estados Unidos , Humanos , United States Department of Veterans Affairs , Estudios Transversales , Estudios de Factibilidad , Apoyo Social
2.
Biochemistry ; 58(13): 1705-1708, 2019 04 02.
Artículo en Inglés | MEDLINE | ID: mdl-30874431

RESUMEN

The human (h) zinc transporter ZIP4 is expressed on the plasma membrane and functions to increase cytosolic zinc levels. Mutations in hZIP4 cause the disease acrodermatitis enteropathica. Dysfunction in the regulation of hZIP4 has also been indicated in solid tissue cancers, including pancreatic and prostate cancer. Although structural studies of the extracellular domain and computational modeling of the membrane domain suggest hZIP4 exists as a dimer, the oligomerization status of hZIP4 in the plasma membrane of mammalian cells has not been directly quantified in vivo. Here, the oligomeric state of hZIP4 expressed in HEK293 cells was quantified using fluorescence correlation spectroscopy. hZIP4 was tagged with eGFP, and by comparing brightness values (ε) of monomer and tandem eGFP constructs to that of an hZIP4/eGFP, we show that hZIP4 is a dimer. Determining that hZIP4 is a dimer is an important step toward understanding the function and processing of the protein, which can provide more insight into how diseases affected by hZIP4 occur and can be managed.


Asunto(s)
Proteínas de Transporte de Catión/química , Membrana Celular/química , Células HEK293 , Humanos , Modelos Moleculares , Dominios Proteicos , Multimerización de Proteína , Espectrometría de Fluorescencia
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