Poly-arginine-fused calpastatin peptide, a living cell membrane-permeable and specific inhibitor for calpain

Hai Yan Wu; Kazuhito Tomizawa; Masayuki Matsushita; Yun Fei Lu; Sheng Tian Li; Hideki Matsui

doi:10.1016/S0168-0102(03)00195-0

Poly-arginine-fused calpastatin peptide, a living cell membrane-permeable and specific inhibitor for calpain

Hai Yan Wu, Kazuhito Tomizawa, Masayuki Matsushita, Yun Fei Lu, Sheng Tian Li, Hideki Matsui

Research output: Contribution to journal › Article › peer-review

31 Citations (Scopus)

Abstract

Calpain, a Ca²⁺-dependent neutral protease, is highly related to the pathogenesis of a variety of disorders and its inhibitors offer potential for therapeutic intervention. General calpain inhibitors, however, have the disadvantage of a lack of specificity or poor cellular permeability or oxidization under physiological conditions. Here, we developed a membrane-permeable specific calpain inhibitor by fusing calpastatin peptide (CS) and 11 poly-arginine peptides (11R). The 11R-fused CS (11R-CS) effectively penetrated across the plasma membrane of living neurons and significantly inhibited calpain activity in the cells.

Original language	English
Pages (from-to)	131-135
Number of pages	5
Journal	Neuroscience Research
Volume	47
Issue number	1
DOIs	https://doi.org/10.1016/S0168-0102(03)00195-0
Publication status	Published - Sep 1 2003
Externally published	Yes

Keywords

Apoptosis
Calpain
Calpastatin
Neuronal cell death
Poly-arginine peptides
Tat

ASJC Scopus subject areas

Neuroscience(all)

Access to Document

10.1016/S0168-0102(03)00195-0

Fingerprint Dive into the research topics of 'Poly-arginine-fused calpastatin peptide, a living cell membrane-permeable and specific inhibitor for calpain'. Together they form a unique fingerprint.

Cite this

@article{51855ffadc6c4815b159baf973a63800,

title = "Poly-arginine-fused calpastatin peptide, a living cell membrane-permeable and specific inhibitor for calpain",

abstract = "Calpain, a Ca2+-dependent neutral protease, is highly related to the pathogenesis of a variety of disorders and its inhibitors offer potential for therapeutic intervention. General calpain inhibitors, however, have the disadvantage of a lack of specificity or poor cellular permeability or oxidization under physiological conditions. Here, we developed a membrane-permeable specific calpain inhibitor by fusing calpastatin peptide (CS) and 11 poly-arginine peptides (11R). The 11R-fused CS (11R-CS) effectively penetrated across the plasma membrane of living neurons and significantly inhibited calpain activity in the cells.",

keywords = "Apoptosis, Calpain, Calpastatin, Neuronal cell death, Poly-arginine peptides, Tat",

author = "Wu, {Hai Yan} and Kazuhito Tomizawa and Masayuki Matsushita and Lu, {Yun Fei} and Li, {Sheng Tian} and Hideki Matsui",

note = "Funding Information: This work was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan (K.T., M.M. and H.M.). and by the Industrial Technology Research Grant Program in 2001 from New Energy and Industrial Technology Development Organization, Japan (K.T.).",

year = "2003",

month = sep,

day = "1",

doi = "10.1016/S0168-0102(03)00195-0",

language = "English",

volume = "47",

pages = "131--135",

journal = "Neuroscience Research",

issn = "0168-0102",

publisher = "Elsevier Ireland Ltd",

number = "1",

}

TY - JOUR

T1 - Poly-arginine-fused calpastatin peptide, a living cell membrane-permeable and specific inhibitor for calpain

AU - Wu, Hai Yan

AU - Tomizawa, Kazuhito

AU - Matsushita, Masayuki

AU - Lu, Yun Fei

AU - Li, Sheng Tian

AU - Matsui, Hideki

N1 - Funding Information: This work was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan (K.T., M.M. and H.M.). and by the Industrial Technology Research Grant Program in 2001 from New Energy and Industrial Technology Development Organization, Japan (K.T.).

PY - 2003/9/1

Y1 - 2003/9/1

N2 - Calpain, a Ca2+-dependent neutral protease, is highly related to the pathogenesis of a variety of disorders and its inhibitors offer potential for therapeutic intervention. General calpain inhibitors, however, have the disadvantage of a lack of specificity or poor cellular permeability or oxidization under physiological conditions. Here, we developed a membrane-permeable specific calpain inhibitor by fusing calpastatin peptide (CS) and 11 poly-arginine peptides (11R). The 11R-fused CS (11R-CS) effectively penetrated across the plasma membrane of living neurons and significantly inhibited calpain activity in the cells.

AB - Calpain, a Ca2+-dependent neutral protease, is highly related to the pathogenesis of a variety of disorders and its inhibitors offer potential for therapeutic intervention. General calpain inhibitors, however, have the disadvantage of a lack of specificity or poor cellular permeability or oxidization under physiological conditions. Here, we developed a membrane-permeable specific calpain inhibitor by fusing calpastatin peptide (CS) and 11 poly-arginine peptides (11R). The 11R-fused CS (11R-CS) effectively penetrated across the plasma membrane of living neurons and significantly inhibited calpain activity in the cells.

KW - Apoptosis

KW - Calpain

KW - Calpastatin

KW - Neuronal cell death

KW - Poly-arginine peptides

KW - Tat

UR - http://www.scopus.com/inward/record.url?scp=0041660920&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0041660920&partnerID=8YFLogxK

U2 - 10.1016/S0168-0102(03)00195-0

DO - 10.1016/S0168-0102(03)00195-0

M3 - Article

C2 - 12941454

AN - SCOPUS:0041660920

VL - 47

SP - 131

EP - 135

JO - Neuroscience Research

JF - Neuroscience Research

SN - 0168-0102

IS - 1

ER -

Poly-arginine-fused calpastatin peptide, a living cell membrane-permeable and specific inhibitor for calpain

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this