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1.  The Symptom Frequency Characteristics of the Hamilton Depression Rating Scale and Possible Symptom Clusters of Depressive Disorders in Korea: The CRESCEND Study 
Psychiatry Investigation  2011;8(4):312-319.
Objective
This study analyzed the symptom frequencies of 17-item Hamilton Depression Rating Scale (HDRS-17) to understand the characteristics of each item and to propose the possible symptoms clusters.
Methods
From psychiatric clinics of 18 Hospitals in Korea, 1,183 patients, diagnosed with major depressive disorder (psychotic or non-psychotic), dysthymia or depressive disorder not otherwise specified. according to DSM-IV criteria, participated in this study from January 2006 to August 2008. The frequencies of each item of HDRS-17 were analyzed according to sex and severity. In addition, we compared this study with a previous study performed in England by Hamilton and with two studies performed in Korea by Kim et al.
Results
The frequencies of HDRS-17 items varied widely in this study, ranging from 95.8% in work and activities to 37.4% in loss of weight. But, depressed mood, psychic anxiety and work and activities items exhibited constant and higher frequency or rank regardless of study, the severity of depression or sex. Insomnia early, somatic gastrointestinal, genital symptoms and insight showed relatively constant but lower frequency or rank in disregard of studies or the clinical variables. Other symptoms had variable frequencies or ranks according to the variable clinical situations (culture, time, sex, severity of depression).
Conclusion
We propose three clusters of symptoms in depressive disorders: core symptoms cluster, an associated symptoms, and a situation-specific symptoms. We can use these possible symptom clusters of depression in simplifying diagnosis of depression, increasing diagnostic specificity in special situation and indexing disease severity.
doi:10.4306/pi.2011.8.4.312
PMCID: PMC3246138  PMID: 22216040
Symptom frequency; Variation; HDRS-17; Core symptoms cluster; Associate symptoms cluster; Situation-specific symptoms cluster
2.  Molecular characterization of Korean rabies virus isolates 
Journal of Veterinary Science  2011;12(1):57-63.
The nucleoprotein (N) and glycoprotein (G) of 11 Korean rabies virus (RABV) isolates collected from animals diagnosed with rabies between 2008 and 2009 were subjected to molecular and phylogenetic analyses. Six isolates originated from domestic animals (cattle and dogs) and five were obtained from wild free-ranging raccoon dogs. The similarities in the nucleotide sequences of the N gene among all Korean isolates ranged from 98.1 to 99.8%, while those of the G gene ranged from 97.9 to 99.3%. Based on the nucleotide analysis of the N and G genes, the Korean RABV isolates were confirmed as genotype I of Lyssavirus and classified into four distinct subgroups with high similarity. Phylogenetic analysis showed that the Korean isolates were most closely related to the non-Korean NeiMeng1025B and 857r strains, which were isolated from rabid raccoon dogs in Eastern China and Russia, respectively. These findings suggest that the Korean RABV isolates originated from a rabid raccoon dog in Northeastern Asia. Genetic analysis of the Korean RABV isolates revealed no substitutions at several antigenic sites, indicating that the isolates circulating in Korea may be pathogenic in several hosts.
doi:10.4142/jvs.2011.12.1.57
PMCID: PMC3053468  PMID: 21368564
characterization; genotype I; molecular epidemiology; rabies virus
3.  Deficiency of ATP2C1, a Golgi Ion Pump, Induces Secretory Pathway Defects in Endoplasmic Reticulum (ER)-associated Degradation and Sensitivity to ER Stress* 
The Journal of biological chemistry  2004;280(10):9467-9473.
Relatively few clues have been uncovered to elucidate the cell biological role(s) of mammalian ATP2C1 encoding an inwardly directed secretory pathway Ca2+/Mn2+ pump that is ubiquitously expressed. Deficiency of ATP2C1 results in a human disease (Hailey-Hailey), which primarily affects keratinocytes. ATP2C1-encoded protein is detected in the Golgi complex in a calcium-dependent manner. A small interfering RNA causes knockdown of ATP2C1 expression, resulting in defects in both post-translational processing of wild-type thyroglobulin (a secretory glycoprotein) as well as endoplasmic reticulum-associated protein degradation of mutant thyroglobulin, whereas degradation of a nonglycosylated misfolded secretory protein substrate appears unaffected. Knockdown of ATP2C1 is not associated with elevated steady state levels of ER chaperone proteins, nor does it block cellular activation of either the PERK, ATF6, or Ire1/XBP1 portions of the ER stress response. However, deficiency of ATP2C1 renders cells hypersensitive to ER stress. These data point to the important contributions of the Golgi-localized ATP2C1 protein in homeostatic maintenance throughout the secretory pathway.
doi:10.1074/jbc.M413243200
PMCID: PMC2527542  PMID: 15623514
4.  Protein disulfide isomerase–like proteins play opposing roles during retrotranslocation 
The Journal of Cell Biology  2006;173(6):853-859.
Misfolded proteins in the endoplasmic reticulum (ER) are retained in the organelle or retrotranslocated to the cytosol for proteasomal degradation. ER chaperones that guide these opposing processes are largely unknown. We developed a semipermeabilized cell system to study the retrotranslocation of cholera toxin (CT), a toxic agent that crosses the ER membrane to reach the cytosol during intoxication. We found that protein disulfide isomerase (PDI) facilitates CT retrotranslocation, whereas ERp72, a PDI-like protein, mediates its ER retention. In vitro analysis revealed that PDI and ERp72 alter CT's conformation in a manner consistent with their roles in retrotranslocation and ER retention. Moreover, we found that PDI's and ERp72's opposing functions operate on endogenous ER misfolded proteins. Thus, our data identify PDI family proteins that play opposing roles in ER quality control and establish an assay to further delineate the mechanism of CT retrotranslocation.
doi:10.1083/jcb.200602046
PMCID: PMC2063911  PMID: 16785320
5.  Mixed-Disulfide Folding Intermediates between Thyroglobulin and Endoplasmic Reticulum Resident Oxidoreductases ERp57 and Protein Disulfide Isomerase 
Molecular and Cellular Biology  2005;25(22):9793-9805.
We present the first identification of transient folding intermediates of endogenous thyroglobulin (Tg; a large homodimeric secretory glycoprotein of thyrocytes), which include mixed disulfides with endogenous oxidoreductases servicing Tg folding needs. Formation of disulfide-linked Tg adducts with endoplasmic reticulum (ER) oxidoreductases begins cotranslationally. Inhibition of ER glucosidase activity blocked formation of a subgroup of Tg adducts containing ERp57 while causing increased Tg adduct formation with protein disulfide isomerase (PDI), delayed adduct resolution, perturbed oxidative folding of Tg monomers, impaired Tg dimerization, increased Tg association with BiP/GRP78 and GRP94, activation of the unfolded protein response, increased ER-associated degradation of a subpopulation of Tg, partial Tg escape from ER quality control with increased secretion of free monomers, and decreased overall Tg secretion. These data point towards mixed disulfides with the ERp57 oxidoreductase in conjunction with calreticulin/calnexin chaperones acting as normal early Tg folding intermediates that can be “substituted” by PDI adducts only at the expense of lower folding efficiency with resultant ER stress.
doi:10.1128/MCB.25.22.9793-9805.2005
PMCID: PMC1280251  PMID: 16260597

Results 1-5 (5)