Calpain inhibitor entrapped in liposome rescues ischemic neuronal damage

Yokota, Masayuki; Tani, Eiichi; Tsubuki, Satoshi; Yamaura, Ikuya; Nakagaki, Ikuko; Hori, Seiki; Saido, Takaomi C.

doi:10.1016/s0006-8993(98)01334-1

Cited by 59 publications

(25 citation statements)

References 31 publications

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“…Proteases, such as calpain (31) and caspases (32), have been found to be increased in activity and have been implicated in the pathophysiology of ischemic injury to the kidney and other organs. In the brain, for example, inhibition of calpainmediated proteolysis protects hippocampal neurons against ischemic injury (33). We are proposing, however, that Omi may act similarly to heat shock proteins, which have been implicated in the protection of the kidney and other organs against ischemic injury (34).…”

Section: Isolation Of Omi a Human Htra Homologuementioning

confidence: 98%

Characterization of a Novel Human Serine Protease That Has Extensive Homology to Bacterial Heat Shock Endoprotease HtrA and Is Regulated by Kidney Ischemia

Faccio¹,

Fusco²,

Chen³

et al. 2000

Journal of Biological Chemistry

207

177

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We report the isolation and characterization of a cDNA encoding the novel mammalian serine protease Omi. Omi protein consists of 458 amino acids and has homology to bacterial HtrA endoprotease, which acts as a chaperone at low temperatures and as a proteolytic enzyme that removes denatured or damaged substrates at elevated temperatures. The carboxyl terminus of Omi has extensive homology to a mammalian protein called L56 (human HtrA), but unlike L56, which is secreted, Omi is localized in the endoplasmic reticulum. Omi has several novel putative protein-protein interaction motifs, as well as a PDZ domain and a Src homology 3-binding domain. Omi mRNA is expressed ubiquitously, and the gene is localized on human chromosome 2p12. Omi interacts with Mxi2, an alternatively spliced form of the p38 stress-activated kinase. Omi protein, when made in a heterologous system, shows proteolytic activity against a nonspecific substrate ␤-casein. The proteolytic activity of Omi is markedly up-regulated in the mouse kidney following ischemia/reperfusion.

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Section: Isolation Of Omi a Human Htra Homologuementioning

confidence: 98%

Characterization of a Novel Human Serine Protease That Has Extensive Homology to Bacterial Heat Shock Endoprotease HtrA and Is Regulated by Kidney Ischemia

Faccio¹,

Fusco²,

Chen³

et al. 2000

Journal of Biological Chemistry

207

177

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“…Moreover, when liposomes were associated with contrast agents, researchers observed that they quickly accumulated in the ischemic zone. 134,143,148,152,190 Some formulations have demonstrated their ability to improve in vivo activity of drugs, such as chrysophanol, 133 dexamethasone phosphate, 154 nerve growth factor, 170 Xe, 150,158 FK506, 149 isopropylidene-shikimic acid, 151 asialo-erythropoietin, 153 antisense oligonucleotides, 165 plasmids, 174 quercetin, 166,168 fasudil, 176 nitric oxide, 146 N-acetylleucyl-leucyl-norleucine amide, 178 and a combination of synergistic drugs. 156,175 Very recently, a promising uncoupling new drug -ZL006 (5-(3, 5-dichloro-2-hydroxybenzylamino)-2-hydroxybenzoic acid) -was developed for stroke treatment.…”

Section: Stroke or Cerebral Ischemiamentioning

confidence: 99%

Getting into the brain: liposome-based strategies for effective drug delivery across the blood–brain barrier

Vieira

Gamarra

2016

IJN

349

238

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This review summarizes articles that have been reported in literature on liposome-based strategies for effective drug delivery across the blood–brain barrier. Due to their unique physicochemical characteristics, liposomes have been widely investigated for their application in drug delivery and in vivo bioimaging for the treatment and/or diagnosis of neurological diseases, such as Alzheimer’s, Parkinson’s, stroke, and glioma. Several strategies have been used to deliver drug and/or imaging agents to the brain. Covalent ligation of such macromolecules as peptides, antibodies, and RNA aptamers is an effective method for receptor-targeting liposomes, which allows their blood–brain barrier penetration and/or the delivery of their therapeutic molecule specifically to the disease site. Additionally, methods have been employed for the development of liposomes that can respond to external stimuli. It can be concluded that the development of liposomes for brain delivery is still in its infancy, although these systems have the potential to revolutionize the ways in which medicine is administered.

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“…Previous studies have shown that a rapid (within 30 min) and sustained activation of calpain occurs following focal neocortical ischemia and global ischemia (6 -10, 12-14) and following glutamate treatment of cultured hippocampal and cerebellar neurons (11). Direct inhibition of calpain reduces calpain-mediated proteolysis of spectrins and decreases brain infarction in ischemic rats and gerbils (13)(14)(15)(16)(17) and protects cultured hippocampal and cerebellar neurons against glutamate-induced toxicity (18 -20).…”

mentioning

confidence: 99%

Chlortetracycline and Demeclocycline Inhibit Calpains and Protect Mouse Neurons against Glutamate Toxicity and Cerebral Ischemia

Jiang

Lertvorachon

Hou

et al. 2005

Journal of Biological Chemistry

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Minocycline is a potent neuroprotective tetracycline in animal models of cerebral ischemia. We examined the protective properties of chlortetracycline (CTC) and demeclocycline (DMC) and showed that these two tetracyclines were also potent neuroprotective against glutamate-induced neuronal death in vitro and cerebral ischemia in vivo. However, CTC and DMC appeared to confer neuroprotection through a unique mechanism compared with minocycline. Rather than inhibiting microglial activation and caspase, CTC and DMC suppressed calpain activities. In addition, CTC and DMC only weakly antagonized N-methyl-D-aspartate (NMDA) receptor activities causing 16 and 14%, respectively, inhibition of NMDAinduced whole cell currents and partially blocked NMDA-induced Ca 2؉ influx, commonly regarded as the major trigger of neuronal death. In vitro and in vivo experiments demonstrated that the two compounds selectively inhibited the activities of calpain I and II activated following glutamate treatment and cerebral ischemia. In contrast, minocycline did not significantly inhibit calpain activity. Taken together, these results suggested that CTC and DMC provide neuroprotection through suppression of a rise in intracellular Ca 2؉

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Calpain inhibitor entrapped in liposome rescues ischemic neuronal damage

Cited by 59 publications

References 31 publications

Characterization of a Novel Human Serine Protease That Has Extensive Homology to Bacterial Heat Shock Endoprotease HtrA and Is Regulated by Kidney Ischemia

Characterization of a Novel Human Serine Protease That Has Extensive Homology to Bacterial Heat Shock Endoprotease HtrA and Is Regulated by Kidney Ischemia

Getting into the brain: liposome-based strategies for effective drug delivery across the blood–brain barrier

Chlortetracycline and Demeclocycline Inhibit Calpains and Protect Mouse Neurons against Glutamate Toxicity and Cerebral Ischemia

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Calpain inhibitor entrapped in liposome rescues ischemic neuronal damage

Cited by 59 publications

References 31 publications

Characterization of a Novel Human Serine Protease That Has Extensive Homology to Bacterial Heat Shock Endoprotease HtrA and Is Regulated by Kidney Ischemia

Characterization of a Novel Human Serine Protease That Has Extensive Homology to Bacterial Heat Shock Endoprotease HtrA and Is Regulated by Kidney Ischemia

Getting into the brain: liposome-based strategies for effective drug delivery across the blood&ndash;brain barrier

Chlortetracycline and Demeclocycline Inhibit Calpains and Protect Mouse Neurons against Glutamate Toxicity and Cerebral Ischemia

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Getting into the brain: liposome-based strategies for effective drug delivery across the blood–brain barrier