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1.
Acute Med Surg ; 9(1): e772, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-35899244

RESUMO

Background: There are few reports of dextrose-associated hepatic steatosis during insulin overdose treatment. Reports in nondiabetic patients are extremely rare. There is inadequate knowledge about the clinical course and treatment. Case Presentation: A 37-year-old previously healthy, nondiabetic man self-administered 5,925 IU of insulin. On admission, his liver function tests were normal. However, following continued dextrose treatment, they increased, and he was diagnosed with hepatic steatosis. The liver function tests improved with decreasing dextrose dosage, and he was asymptomatic on discharge. Conclusion: Acute hepatic steatosis may occur in nondiabetic and diabetic patients during treatment requiring large doses of dextrose infusion, such as for an insulin overdose. In addition, the degree of liver damage might also be related to the dextrose dose. Therefore, careful glycemic control and minimization of the dextrose dosage are recommended for diabetic and nondiabetic patients.

2.
Trauma Case Rep ; 32: 100412, 2021 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-33665308

RESUMO

A 48-year-old man fell asleep while driving a 4-t truck, hit an 11-t truck from behind, and was injured. Contrast-enhanced computed tomography revealed retroperitoneal hematoma and extravasation of contrast medium in the left common iliac vein. No obvious pelvic fracture was observed. The patient showed no hemodynamic deterioration, so conservative management was selected. Computed tomography images obtained 2 days after injury showed that the hematoma around the left common iliac vein had shrunk and no clear vein thrombus was observed. No findings suggestive of deep vein thrombosis or pulmonary embolism were seen after the start of gait training. Iliac vein injury without pelvic fracture due to blunt trauma is particularly rare. This rare injury was attributed to sudden extension of the hip and force in the direction of the long axis of the common iliac vein. Conservative management is the recommended first choice for isolated iliac vein injury with stable hemodynamics.

3.
Acute Med Surg ; 6(3): 252-258, 2019 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-31304026

RESUMO

AIM: Intentional or unintentional acute drug poisoning occurs even in elderly people, but little is known about the factors influencing the intention to poisoning. A retrospective study was undertaken to describe the characteristics of acute drug poisoning in elderly people according to whether the poisoning was intentional or unintentional and the responsible agents. METHODS: The study was carried out in a single tertiary hospital in Japan. A total of 145 patients aged ≥65 years who were transferred by an ambulance service and were diagnosed with acute drug poisoning were included. Medical records were used to collect information on the intention behind poisoning and the responsible agents. Patients were divided into two groups according to whether they experienced intentional or unintentional poisoning and were further classified according to the responsible agent. Multivariable logistic regression models were used to estimate the association between hospitalization for acute drug poisoning and the use of benzodiazepine receptor agonists (BzRAs). RESULTS: Poisoning was unintentional in 102 (70.3%) patients and intentional in 43 (29.7%) patients. In total, 65 (44.8%) patients required hospitalization. Among patients in the unintentional poisoning group, those using non-BzRAs were more likely to be hospitalized than those using BzRAs (odds ratio, 6.64; 95% confidence interval, 2.56-17.22). The length of hospital stay was significantly longer in the unintentional poisoning group than in the intentional poisoning group (13.9 vs. 6.2 days; P = 0.013). CONCLUSIONS: The proportion of unintentional poisoning in the elderly is high, and particularly with respect to poisoning with non-BzRAs, the hospitalization rates are high.

5.
J Biol Chem ; 286(34): 29462-9, 2011 Aug 26.
Artigo em Inglês | MEDLINE | ID: mdl-21642437

RESUMO

Dentin matrix phosphoprotein 1 (DMP1) is a non-collagenous, acidic extracellular matrix protein expressed chiefly in bone and dentin. We examined the DMP1 ability to engage cell-surface receptors and subsequently activate intracellular signaling pathways. Our data indeed show that the presence of extracellular DMP1 triggers focal adhesion point formation in human mesenchymal stem cells and osteoblast-like cells. We determine that DMP1 acts via interaction with αvß3 integrin and stimulates phosphorylation of focal adhesion kinase. Further biochemical characterization confirms the activation of downstream effectors of the MAPK pathways, namely ERK and JNK, after DMP1 treatment. This activation is specifically inhibitable and can also be blocked by the addition of anti-αvß3 integrin antibody. Furthermore, we show that extracellular treatment with DMP1 stimulates the translocation of phosphorylated JNK to the nucleus and a concomitant up-regulation of transcriptional activation by phosphorylated c-Jun. The evidence presented here indicates that DMP1 is specifically involved in signaling via extracellular matrix-cell surface interaction. Combined with the published DMP1-null data (Feng, J. Q., Ward, L. M., Liu, S., Lu, Y., Xie, Y., Yuan, B., Yu, X., Rauch, F., Davis, S. I., Zhang, S., Rios, H., Drezner, M. K., Quarles, L. D., Bonewald, L. F., and White, K. E. (2006) Nat. Genet. 38, 1310-1315) it can be hypothesized that DMP1 could be a key effector of ECM-osteocyte signaling.


Assuntos
Núcleo Celular/metabolismo , Proteínas da Matriz Extracelular/metabolismo , Adesões Focais/metabolismo , Integrina alfaVbeta3/metabolismo , Células-Tronco Mesenquimais/metabolismo , Osteoblastos/metabolismo , Fosfoproteínas/metabolismo , Transdução de Sinais/fisiologia , Transporte Ativo do Núcleo Celular/fisiologia , Linhagem Celular , Núcleo Celular/genética , Matriz Extracelular/genética , Matriz Extracelular/metabolismo , Proteínas da Matriz Extracelular/genética , Quinase 1 de Adesão Focal/genética , Quinase 1 de Adesão Focal/metabolismo , Adesões Focais/genética , Humanos , Proteínas Quinases JNK Ativadas por Mitógeno/genética , Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo , MAP Quinase Quinase 4/genética , MAP Quinase Quinase 4/metabolismo , Células-Tronco Mesenquimais/citologia , Osteoblastos/citologia , Fosfoproteínas/genética , Fosforilação/fisiologia , Estrutura Terciária de Proteína
6.
Infect Immun ; 76(1): 198-205, 2008 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-17967853

RESUMO

Tannerella forsythia is a gram-negative anaerobe strongly associated with chronic human periodontitis. This bacterium expresses a cell surface-associated and secreted protein, designated BspA, which has been recognized as an important virulence factor. The BspA protein belongs to the leucine-rich repeat (LRR) and bacterial immunoglobulin-like protein families. BspA is, moreover, a multifunctional protein which interacts with a variety of host cells, including monocytes which appear to respond to BspA through Toll-like receptor (TLR) signaling. Since gingival epithelium forms a barrier against periodontal pathogens, this study was undertaken to determine if gingival epithelial cells respond to BspA challenge and if TLRs play any role in BspA recognition. This study was also directed towards identifying the BspA domains responsible for cellular activation. We provide direct evidence for BspA binding to TLR2 and demonstrate that the release of the chemokine interleukin-8 from human gingival epithelial cells by BspA is TLR2 dependent. Furthermore, the LRR domain of BspA is involved in activation of TLR2, while TLR1 serves as a signaling partner. Thus, our findings suggest that BspA is an important modulator of host innate immune responses through activation of TLR2 in cooperation with TLR1.


Assuntos
Proteínas de Bactérias/farmacologia , Células Epiteliais/efeitos dos fármacos , Células Epiteliais/metabolismo , Gengiva/citologia , Interleucina-8/genética , Proteínas de Membrana/farmacologia , Receptor 2 Toll-Like/metabolismo , Linhagem Celular , Bactérias Anaeróbias Gram-Negativas/metabolismo , Humanos , Interleucina-8/metabolismo , Ligação Proteica , Estrutura Terciária de Proteína , Receptor 1 Toll-Like/metabolismo , Receptor 6 Toll-Like/metabolismo
7.
Infect Immun ; 74(9): 5023-8, 2006 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-16926393

RESUMO

The human oral cavity harbors more than 500 species of bacteria. Periodontitis, a bacterially induced inflammatory disease that leads to tooth loss, is believed to result from infection by a select group of gram-negative periodontopathogens that includes Porphyromonas gingivalis, Treponema denticola, and "Tannerella forsythia" (opinion on name change from Tannerella forsythensis pending; formerly Bacteroides forsythus). Epithelial cell invasion by periodontopathogens is considered to be an important virulence mechanism for evasion of the host defense responses. Further, the epithelial cells with invading bacteria also serve as reservoirs important in recurrent infections. The present study was therefore undertaken to address the epithelial cell adherence and invasion properties of T. forsythia and the role of the cell surface-associated protein BspA in these processes. Further, we were interested in determining if P. gingivalis, one of the pathogens frequently found associated in disease, or its outer membrane vesicles (OMVs) could modulate the epithelial cell adherence and invasion abilities of T. forsythia. Here we show that epithelial cell attachment and invasion by T. forsythia are dependent on the BspA protein. In addition, P. gingivalis or its OMVs enhance the attachment and invasion of T. forsythia to epithelial cells. Thus, interactions between these two bacteria may play important roles in virulence by promoting host cell attachment and invasion.


Assuntos
Antígenos de Bactérias/fisiologia , Aderência Bacteriana , Proteínas de Bactérias/fisiologia , Bacteroides/patogenicidade , Mucosa Bucal/microbiologia , Porphyromonas gingivalis/patogenicidade , Proteínas/fisiologia , Antígenos de Bactérias/genética , Aderência Bacteriana/genética , Proteínas de Bactérias/genética , Bacteroides/genética , Membrana Celular , Células Epiteliais/microbiologia , Humanos , Proteínas de Repetições Ricas em Leucina , Mutação , Proteínas/genética , Virulência/genética
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