Role of matrix metalloprotease-2 in oxidant activation of Ca2+ATPase by hydrogen peroxide in pulmonary vascular smooth muscle plasma membrane

2003 ◽  
Vol 28 (2) ◽  
pp. 205-213 ◽  
Author(s):  
Malay ManDal ◽  
Sudip Das ◽  
Tapati Chakraborti ◽  
Amritlal ManDal ◽  
Sajal Chakraborti
2002 ◽  
Vol 17 (3) ◽  
pp. 392-398 ◽  
Author(s):  
Francisco R. González‐Pacheco ◽  
Carlos Caramelo ◽  
Maria Ángeles Castilla ◽  
Juan J. P. Deudero ◽  
Javier Arias ◽  
...  

1989 ◽  
Vol 264 (2) ◽  
pp. 609-612 ◽  
Author(s):  
L Missiaen ◽  
L Raeymaekers ◽  
G Droogmans ◽  
F Wuytack ◽  
R Casteels

Negatively charged phospholipids strongly stimulate the purified plasma membrane Ca2+ pump of erythrocytes [Enyedi, Flura, Sarkadi, Gardos & Carafoli (1987) J. Biol. Chem. 262, 6425-6430] and of smooth muscle [Missiaen, Raeymaekers, Wuytack, Vrolix, De Smedt & Casteels, (1989) Biochem. J. 263, 687-694]. We have investigated the role of arginine residues in the interaction of these acidic phospholipids with the smooth-muscle Ca2+ transport ATPase. The arginine-modifying reagent phenylglyoxal inhiibited the ATPase activity in a time-dependent fashion by decreasing the Vmax. of the Ca2(+)-activation curve. Low concentrations of PtdIns, PtdIns4P, PtdIns(4,5) P2, phosphatidylserine and phosphatidic acid partially prevented this inactivation. This protective effect was however not apparent at higher concentrations of PtdIns4P, PtdIns(4,5) P2 and phosphatidic acid, which may be related to the previously observed inhibition of the enzyme at higher concentrations of these phospholipids. These findings indicate that the functionally important interaction of the acidic lipids with the protein occurs at least partially via arginine residue(s).


2019 ◽  
Vol 33 (9) ◽  
pp. 9785-9796 ◽  
Author(s):  
Takuro Numaga‐Tomita ◽  
Tsukasa Shimauchi ◽  
Sayaka Oda ◽  
Tomohiro Tanaka ◽  
Kazuhiro Nishiyama ◽  
...  

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