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2.
J Vet Med Educ ; 41(4): 400-5, 2014.
Article in English | MEDLINE | ID: mdl-25172106

ABSTRACT

The purpose of this study was to describe the average client transaction (ACT) of fourth-year veterinary students in a university community practice setting at the University of Georgia (UGA) and to investigate variables that may affect the students' ACT. The revenue generated by each student was assessed to determine whether gender, ethnicity, academic class rank, area of emphasis, and UGA versus non-UGA student could affect the ACT of the students. Two hundred one students were evaluated over 19 continuous 3-week-long clinical rotations. For all students, the M±SD gross revenue was $2,836±$1,051, the total number of client transactions was 18±6, and the ACT was $154±$35 per student. During the study, hospital fees (price class) increased four times. No student-related factors were significantly associated with the ACT in the univariate analyses. No factors except price class were found to be significant in the two-factor analyses. Generating an ACT equivalent to the national average demonstrates that the typical student at the community practice clinic should provide a level of productivity to the practice owners who hire these students. The factors measured demonstrated little influence on the student's revenue-generating ability at the community practice clinic. Mentorship provided to students for each appointment might have affected the study outcome. Other variables, such as communication style, may affect the ACT more than those investigated in this study and warrant further study.


Subject(s)
Clinical Competence , Education, Veterinary , Primary Health Care , Students , Veterinary Medicine , Ambulatory Care Facilities , Animals , Georgia , Primary Health Care/economics , Veterinary Medicine/economics
3.
Mol Cell Neurosci ; 42(3): 219-25, 2009 Nov.
Article in English | MEDLINE | ID: mdl-19607921

ABSTRACT

The voltage-gated sodium channel Na(V)1.8 is expressed exclusively in nociceptive sensory neurons and plays an important role in pain pathways. Na(V)1.8 cannot be functionally expressed in non-neuronal cells even in the presence of beta-subunits. We have previously identified Pdzd2, a multi PDZ-domain protein, as a potential interactor for Na(V)1.8. Here we report that Pdzd2 binds directly to the intracellular loops of Na(V)1.8 and Na(V)1.7. The endogenous Na(V)1.8 current in sensory neurons is inhibited by antisense- and siRNA-mediated downregulation of Pdzd2. However, no marked change in pain behaviours is observed in Pdzd2-decificent mice. This may be due to compensatory upregulation of p11, another regulatory factor for Na(V)1.8, in dorsal root ganglia of Pdzd2-deficient mice. These findings reveal that Pdzd2 and p11 play collaborative roles in regulation of Na(V)1.8 expression in sensory neurons.


Subject(s)
Adaptor Proteins, Signal Transducing/metabolism , Nerve Tissue Proteins/metabolism , PDZ Domains , Sensory Receptor Cells/metabolism , Sodium Channels/metabolism , Adaptor Proteins, Signal Transducing/genetics , Amino Acid Sequence , Animals , Cell Adhesion Molecules , Cells, Cultured , Ganglia, Spinal/cytology , Mice , Mice, Knockout , Molecular Sequence Data , NAV1.7 Voltage-Gated Sodium Channel , NAV1.8 Voltage-Gated Sodium Channel , Nerve Tissue Proteins/genetics , Pain/metabolism , Pain Measurement , Protein Binding , RNA, Small Interfering/genetics , RNA, Small Interfering/metabolism , Rats , Rats, Wistar , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sensory Receptor Cells/cytology , Sequence Alignment , Sodium Channels/genetics , Two-Hybrid System Techniques
4.
FEBS Lett ; 558(1-3): 114-8, 2004 Jan 30.
Article in English | MEDLINE | ID: mdl-14759526

ABSTRACT

The interaction of p11 (annexin II light chain) with the N-terminal domain of Na(V)1.8, a tetrodotoxin-resistant sodium channel, is essential for the functional expression of the channel. Here we show that p11 binds to Na(V)1.8 but not to sodium channel isoforms Na(V)1.2, 1.5, 1.7 or Na(V)1.9. The binding of amino acids 74-103 of Na(V)1.8 to p11 residues 33-78 occurs in a random coiled region flanked by two EF hand motifs whose crystal structure has been established. As Na(V)1.8 channel expression is associated with pain pathways, drugs that disrupt the Na(V)1.8-p11 interaction and down-regulate channel expression may have analgesic activity.


Subject(s)
Annexin A2/chemistry , Annexin A2/metabolism , S100 Proteins/chemistry , S100 Proteins/metabolism , Sodium Channels/chemistry , Sodium Channels/metabolism , Amino Acid Sequence , Animals , Annexin A2/genetics , COS Cells , Chlorocebus aethiops , Computer Simulation , Dimerization , EF Hand Motifs , Glutathione Transferase/metabolism , Green Fluorescent Proteins , Luminescent Proteins/metabolism , Models, Molecular , Models, Theoretical , Protein Isoforms/chemistry , Protein Isoforms/metabolism , Protein Structure, Tertiary , Rats , Recombinant Fusion Proteins/metabolism , S100 Proteins/genetics , Sequence Homology, Amino Acid , Sodium Channels/genetics
5.
Brain Res Mol Brain Res ; 110(2): 298-304, 2003 Feb 20.
Article in English | MEDLINE | ID: mdl-12591166

ABSTRACT

Voltage-gated sodium channels initiate and propagate action potentials in excitable cells. The tetrodotoxin-resistant Na(+) channel (Na(V)1.8/SNS) is expressed in damage-sensing neurons (nociceptors) and plays an important role in pain pathways. Expression of high levels of functional Na(V)1.8 in heterologous cells has proved problematic, even in the presence of known sodium channel accessory beta-subunits. This suggests that other regulatory proteins are required for normal levels of Na(V)1.8 expression. Here we report the use of a yeast two-hybrid system and a rat dorsal root ganglion cDNA library to identify 28 different clones encoding proteins which interact with intracellular domains of Na(V)1.8. Many clones are expressed at high levels in small diameter DRG neurons as judged by in situ hybridization. Interacting proteins include cytoplasmic elements and linker proteins (e.g. beta-actin and moesin), enzymes (e.g. inositol polyphosphate 5-phosphatase and TAO2 thousand and one protein kinase), channels and membrane-associated proteins (voltage-dependent anion channel VDAC3V and tetraspanin), as well as motor proteins (dynein intermediate and light chain) and transcripts encoding previously undescribed proteins. Immunoprecipitation (pull-down) assays confirm that some of the proteins interact with, and may hence regulate, Na(V)1.8 in vivo.


Subject(s)
Cell Membrane/metabolism , Cytosol/metabolism , Ganglia, Spinal/metabolism , Nerve Tissue Proteins/metabolism , Neurons, Afferent/metabolism , Neuropeptides/metabolism , Sodium Channels/metabolism , Animals , NAV1.8 Voltage-Gated Sodium Channel , Neuropeptides/genetics , Nociceptors/metabolism , Pain/genetics , Pain/metabolism , Protein Structure, Tertiary/genetics , Protein Transport/genetics , RNA, Messenger/metabolism , Rats , Sodium Channels/genetics , Two-Hybrid System Techniques , Voltage-Dependent Anion Channels
6.
Nature ; 417(6889): 653-6, 2002 Jun 06.
Article in English | MEDLINE | ID: mdl-12050667

ABSTRACT

The tetrodotoxin-resistant sodium channel Na(V)1.8/SNS is expressed exclusively in sensory neurons and appears to have an important role in pain pathways. Unlike other sodium channels, Na(V)1.8 is poorly expressed in cell lines even in the presence of accessory beta-subunits. Here we identify annexin II light chain (p11) as a regulatory factor that facilitates the expression of Na(V)1.8. p11 binds directly to the amino terminus of Na(V)1.8 and promotes the translocation of Na(V)1.8 to the plasma membrane, producing functional channels. The endogenous Na(V)1.8 current in sensory neurons is inhibited by antisense downregulation of p11 expression. Because direct association with p11 is required for functional expression of Na(V)1.8, disrupting this interaction may be a useful new approach to downregulating Na(V)1.8 and effecting analgesia.


Subject(s)
Annexin A2/chemistry , Annexin A2/metabolism , Gene Expression Regulation , Neurons, Afferent/metabolism , Neuropeptides/genetics , Neuropeptides/metabolism , Sodium Channels/genetics , Sodium Channels/metabolism , Animals , Annexin A2/genetics , CHO Cells , Cell Membrane/metabolism , Cells, Cultured , Cricetinae , Fluorescent Antibody Technique , Ganglia, Spinal/cytology , Gene Expression Profiling , Gene Expression Regulation/drug effects , In Situ Hybridization , Molecular Weight , NAV1.8 Voltage-Gated Sodium Channel , Nerve Growth Factor/pharmacology , Neurons, Afferent/drug effects , Organ Specificity , Patch-Clamp Techniques , Protein Binding , Protein Subunits , Protein Transport , RNA, Antisense/genetics , RNA, Messenger/genetics , RNA, Messenger/metabolism , Rats , Two-Hybrid System Techniques
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