scholarly journals Antifibrotic effects of 2-carba cyclic phosphatidic acid (2ccPA) in systemic sclerosis: contribution to the novel treatment

2019 ◽  
Vol 21 (1) ◽  
Author(s):  
Tomoaki Higuchi ◽  
Kae Takagi ◽  
Akiko Tochimoto ◽  
Yuki Ichimura ◽  
Takanari Norose ◽  
...  
Keyword(s):  
Systemic Sclerosis ◽  
Phosphatidic Acid ◽  
The Novel ◽  
Novel Treatment ◽  
Cyclic Phosphatidic Acid

scholarly journals Physiological Role for Phosphatidic Acid in the Translocation of the Novel Protein Kinase C Apl II in Aplysia Neurons

2008 ◽  
Vol 28 (15) ◽  
pp. 4719-4733 ◽  
Author(s):  
Carole A. Farah ◽  
Ikue Nagakura ◽  
Daniel Weatherill ◽  
Xiaotang Fan ◽  
Wayne S. Sossin
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phosphatidic Acid ◽  
Physiological Role ◽  
C2 Domain ◽  
The Novel ◽  
Physiological Conditions ◽  
Kinase C ◽  
Neuronal Membranes ◽  
Novel Protein

ABSTRACT In Aplysia californica, the serotonin-mediated translocation of protein kinase C (PKC) Apl II to neuronal membranes is important for synaptic plasticity. The orthologue of PKC Apl II, PKCε, has been reported to require phosphatidic acid (PA) in conjunction with diacylglycerol (DAG) for translocation. We find that PKC Apl II can be synergistically translocated to membranes by the combination of DAG and PA. We identify a mutation in the C1b domain (arginine 273 to histidine; PKC Apl II-R273H) that removes the effects of exogenous PA. In Aplysia neurons, the inhibition of endogenous PA production by 1-butanol inhibited the physiological translocation of PKC Apl II by serotonin in the cell body and at the synapse but not the translocation of PKC Apl II-R273H. The translocation of PKC Apl II-R273H in the absence of PA was explained by two additional effects of this mutation: (i) the mutation removed C2 domain-mediated inhibition, and (ii) the mutation decreased the concentration of DAG required for PKC Apl II translocation. We present a model in which, under physiological conditions, PA is important to activate the novel PKC Apl II both by synergizing with DAG and removing C2 domain-mediated inhibition.

scholarly journals Development of Immunopathogenesis Strategies to Treat Behçet’s Disease

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
Osman Köse
Keyword(s):  
Molecular Structure ◽  
Biologic Agents ◽  
Treatment Modalities ◽  
The Novel ◽  
Therapeutic Modalities ◽  
Novel Treatment ◽  
Unclear Etiology ◽  
Antigen Presenting ◽  
Disease Understanding ◽  
Novel Therapeutic

Behçet disease is a chronic relapsing vasculitis with unclear etiology and immunopathogenesis. Antigenic stimuli, antigen presenting cells, T cells, monocyte, and neutrophil and endothelial cells are major parts of the pathology of the disease. Understanding of the new pathogenic mechanisms based on molecular structure of the disease helps us in improving the novel therapeutic modalities. These drugs target specific and nonspecific inhibition of the immun system. These therapies include biologic agents, new topical and systemic immunosuppressants, tolerizing agents, and immunoablation. Novel treatment will be promising to treat the especially recalcitrant cases to conventional therapy. In this paper, new aspect of the immunopathogenesis of Behçet’s diseases and novel treatment modalities will be discussed.

2- O -Carba-oleoyl cyclic phosphatidic acid induces glial proliferation through the activation of lysophosphatidic acid receptor

2018 ◽  
Vol 1681 ◽  
pp. 44-51 ◽  
Author(s):  
Shingo Nakajima ◽  
Mari Gotoh ◽  
Keiko Fukasawa ◽  
Hiromu Murofushi ◽  
Kimiko Murakami-Murofushi
Keyword(s):  
Phosphatidic Acid ◽  
Lysophosphatidic Acid ◽  
Acid Receptor ◽  
Lysophosphatidic Acid Receptor ◽  
Glial Proliferation ◽  
Cyclic Phosphatidic Acid
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