Monophosphoryl Lipid A Protects Adult Rat Cardiac Myocytes With Induction of the 72-kD Heat Shock Protein: A Cellular Model of Pharmacologic Preconditioning

1997 ◽  
Vol 29 (8) ◽  
pp. 2305-2310 ◽  
Author(s):  
Mohammed A Nayeem ◽  
Gary T Elliott ◽  
Maulik R Shah ◽  
Samantha L Hastillo-Hess ◽  
Rakesh C Kukreja
1996 ◽  
Vol 156 (1) ◽  
Author(s):  
Kazu-ichi Yoshida ◽  
MohammedM. Maaieh ◽  
JoshuaB. Shipley ◽  
Mark Doloresco ◽  
NelsonL. Bernardo ◽  
...  

1996 ◽  
Vol 159 (1) ◽  
Author(s):  
Kazu-ichi Yoshida ◽  
MohammedM. Maaieh ◽  
JoshuaB. Shipley ◽  
Mark Doloresco ◽  
NelsonL. Bernardo ◽  
...  

1997 ◽  
Vol 273 (2) ◽  
pp. H861-H868 ◽  
Author(s):  
M. A. Nayeem ◽  
M. L. Hess ◽  
Y. Z. Qian ◽  
K. E. Loesser ◽  
R. C. Kukreja

We investigated the protective effect of heat stress and metabolic preconditioning in cultured adult rat cardiac myocytes and correlated this effect with induction of heat shock proteins (HSP). Myocytes were preconditioned with sublethal heat shock or metabolic preconditioning for 30 min. Twenty hours later, preconditioned myocytes were subjected to lethal heat shock (46 degrees C for 2 h) or ischemia by incubation in ischemic buffer for 2 h. Cellular injury index was reduced from 69 +/- 4.0% in lethally heat-shocked cells to 27.0 +/- 1.6% with heat shock preconditioning (mean +/- SE; P < 0.01) and 19.0 +/- 3.0% with metabolic preconditioning (P < 0.01). Cellular injury index was 81.0 +/- 1.0% in ischemic myocytes and was reduced to 25.9 +/- 2.7 and 21.4 +/- 2.6% in heat shock- and metabolic-preconditioned myocytes, respectively (P < 0.01). A significant cross-tolerance of myocytes against lethal injury was observed with the two preconditioning methods. Western blot analysis revealed 3.3- and 2.5-fold increases in HSP 90 and 500- and 15-fold increases in HSP 70 with heat shock and metabolic preconditioning, respectively. HSP 27 expression remained unaltered relative to control cells. We conclude that heat shock and metabolic preconditioning induce delayed tolerance against lethal injuries in adult cardiac myocytes with elevated levels of HSP 70 and HSP 90.


Vaccines ◽  
2020 ◽  
Vol 8 (3) ◽  
pp. 494 ◽  
Author(s):  
Teerasit Techawiwattanaboon ◽  
Christophe Barnier-Quer ◽  
Tanapat Palaga ◽  
Alain Jacquet ◽  
Nicolas Collin ◽  
...  

Leptospirosis vaccines with higher potency and reduced adverse effects are needed for human use. The carboxyl terminal domain of leptospiral immunoglobulin like protein A (LigAc) is currently the most promising candidate antigen for leptospirosis subunit vaccine. However, LigAc-based vaccines were unable to confer sterilizing immunity against Leptospira infection in animal models. Several factors including antigen properties, adjuvant, delivery system, and administration route need optimization to maximize vaccine efficacy. Our previous report demonstrated protective effects of the recombinant LigAc (rLigAc) formulated with liposome-based adjuvant, called LMQ (neutral liposome combined with monophosphoryl lipid A and Quillaja saponaria fraction 21) in hamsters. This study aimed to evaluate the impact of two commonly used administration routes, intramuscular (IM) and subcutaneous (SC), on immunogenicity and protective efficacy of rLigAc-LMQ administrated three times at 2-week interval. Two IM vaccinations triggered significantly higher levels of total anti-rLigAc IgG than two SC injections. However, comparable IgG titers and IgG2/IgG1 ratio was observed for both routes after the third immunization. The route of vaccine administration did not influence the survival rate (60%) and renal colonization against lethal Leptospira challenge. Importantly, the kidneys of IM group showed no pathological lesions while the SC group showed mild damage. In conclusion, IM vaccination with rLigAc-LMQ not only elicited faster antibody production but also protected from kidney damage following leptospiral infection better than SC immunization. However, both tested routes did not influence protective efficacy in terms of survival rate and the level of renal colonization.


1989 ◽  
Vol 67 (11-12) ◽  
pp. 749-750 ◽  
Author(s):  
Boyd Hardesty ◽  
Gisela Kramer

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e39009 ◽  
Author(s):  
Hirotaka Ata ◽  
Deepa Shrestha ◽  
Masahiko Oka ◽  
Rikuo Ochi ◽  
Chian Ju Jong ◽  
...  

2003 ◽  
Vol 285 (4) ◽  
pp. L957-L963 ◽  
Author(s):  
Hiroshi Ishii ◽  
Hiroshi Mukae ◽  
Tomoyuki Kakugawa ◽  
Tetsuji Iwashita ◽  
Hideyuki Kaida ◽  
...  

The 47-kDa heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that has been shown to play a major role during the processing and/or secretion of procollagen. Expression of HSP47 has been reported to increase in parallel with expression of collagens during the progression of various fibrosis models. The aim of the present study was to investigate the association between HSP47 expression and collagen accumulation in bleomycin (BLM)-induced murine fibrosis. We investigated the expression of HSP47 protein and mRNA using immunohistochemical analysis and semi-quantitative RT-PCR in murine BLM-induced pulmonary fibrosis. Immunohistochemical analysis showed that higher expression of HSP47 protein was present in BLM-induced pulmonary fibrosis compared with controls. HSP47 was localized predominantly in α-smooth muscle actin-positive myofibroblasts, F4/80 negative, surfactant protein-A-positive type II pneumocytes, and F4/80-positive macrophages. RT-PCR also demonstrated an increase of HSP47 mRNA expression in BLM-treated lungs. Moreover, the relative amounts of HSP47 mRNA correlated significantly with the lung hydroxyproline content as an indicator of pulmonary fibrosis in BLM-treated lungs ( r = 0.406, P <0.05). Our results suggest that these cells may play a role in the fibrotic process of BLM-treated lungs through upregulation of HSP47.


1999 ◽  
Vol 5 (3) ◽  
pp. 181-182 ◽  
Author(s):  
Suzanne M. Michalek ◽  
Noel K. Childers ◽  
Terry Greenway ◽  
George Hajishengallis ◽  
J. Terry Ulrich

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