Isolation of tryptic fragment of antigen from mitochondrial inner membrane proteins reacting with antimitochondrial antibody in sera of patients with primary biliary cirrhosis

Hepatology ◽  
1990 ◽  
Vol 11 (1) ◽  
pp. 16-23 ◽  
Author(s):  
Daisaku Muno ◽  
Eiki Kominami ◽  
Hideo Ishii ◽  
Koh Usui ◽  
Koji Saifuku ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Primary Biliary Cirrhosis ◽  
Biliary Cirrhosis ◽  
Inner Membrane ◽  
Tryptic Fragment ◽  
Antimitochondrial Antibody ◽  
Mitochondrial Inner Membrane

scholarly journals Fmp30, Mdm31, and Mdm32 Function in Ups1-Independent Cardiolipin Accumulation Under Low Phosphatidylethanolamine Conditions

Contact ◽  
2018 ◽  
Vol 1 ◽  
pp. 251525641876404
Author(s):  
Non Miyata ◽  
Osamu Kuge
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Membrane Proteins ◽  
Phosphatidic Acid ◽  
Yeast Saccharomyces Cerevisiae ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane ◽  
Per Se

Maintenance of the cardiolipin (CL) level largely depends on Ups1-Mdm35 complex-mediated intramitochondrial phosphatidic acid transfer. In addition, the presence of an alternative CL accumulation pathway has been suggested in the yeast Saccharomyces cerevisiae. This pathway is independent of the Ups1-Mdm35 complex and stimulated by loss of Ups2, which forms a complex with Mdm35 and mediates intramitochondrial transfer of phosphatidylserine for phosphatidylethanolamine synthesis. Recently, we found that the alternative CL accumulation pathway is enhanced by a lowered phosphatidylethanolamine level, not by loss of Ups2 per se, and depends on three mitochondrial inner membrane proteins, Fmp30, Mdm31, and Mdm32.

Antimitochondrial antibody-negative primary biliary cirrhosis: a subset of primary biliary cirrhosis

2008 ◽  
Vol 28 (2) ◽  
pp. 233-239 ◽  
Author(s):  
Bin Liu ◽  
Xu Hua Shi ◽  
Feng Chun Zhang ◽  
Wen Zhang ◽  
Li Xia Gao
Keyword(s):  
Primary Biliary Cirrhosis ◽  
Biliary Cirrhosis ◽  
Antimitochondrial Antibody

Translocation of mitochondrial inner-membrane proteins: conformation matters

2006 ◽  
Vol 31 (5) ◽  
pp. 259-267 ◽  
Author(s):  
Carine de Marcos-Lousa ◽  
Dionisia P Sideris ◽  
Kostas Tokatlidis
Keyword(s):  
Membrane Proteins ◽  
Inner Membrane ◽  
Mitochondrial Inner Membrane

Antimitochondrial antibody profiles: are they valid prognostic indicators in primary biliary cirrhosis?

2002 ◽  
Vol 97 (4) ◽  
pp. 999-1002 ◽  
Author(s):  
Supriya Joshi ◽  
Karen Cauch-Dudek ◽  
E. Jenny Heathcote ◽  
Keith Lindor ◽  
Roberta Jorgensen ◽  
...  
Keyword(s):  
Primary Biliary Cirrhosis ◽  
Prognostic Indicators ◽  
Biliary Cirrhosis ◽  
Antimitochondrial Antibody

AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis

2001 ◽  
Vol 29 (4) ◽  
pp. 431-436 ◽  
Author(s):  
T. Langer ◽  
M. Käser ◽  
C. Klanner ◽  
K. Leonhard
Keyword(s):  
Quality Control ◽  
Membrane Proteins ◽  
Matrix Space ◽  
Inner Membrane ◽  
Membrane Surfaces ◽  
Mitochondrial Inner Membrane ◽  
Catalytic Sites ◽  
The Matrix ◽  
The Stability ◽  
Regulatory Functions

An ubiquitous and conserved proteolytic system regulates the stability of mitochondrial inner membrane proteins. Two AAA proteases with catalytic sites at opposite membrane surfaces form a membrane-integrated quality control system and exert crucial functions during the biogenesis of mitochondria. Their activity is modulated by another membrane-protein complex that is composed of prohibitins. Peptides generated upon proteolysis in the matrix space are transported across the inner membrane by an ATP-binding cassette transporter. The function of these conserved components is discussed in the present review.

Sign in / Sign up

Export Citation Format

Share Document