Isolation of a soluble Ca2+ binding glycoprotein from ox liver mitochondria

Sottocasa, Gian Luigi; Sandri, Gabriella; Panfili, Enrico; Bernard, B. de; Gazzotti, Paolo; Vasington, Frank D.; Carafoli, Ernesto

doi:10.1016/0006-291x(72)90564-5

Cited by 121 publications

(42 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A soluble mitochondrial Ca 2+ -binding glycoprotein, whose Ca 2+ binding could be inhibited by La 3+ or ruthenium red, was isolated in 1972 (95), and antibodies against it inhibited Ca 2+ uptake (96). Later, Mironova and coworkers (97) also isolated a 40-kDa Ca 2+ -binding glycoprotein from beef heart mitochondria and found that a 2-kDa peptide fragment in the preparation could reconstitute a ruthenium red-sensitive Ca 2+ selective conductance in black-lipid membranes.…”

Section: The Mitochondrial Ca 2+ Uniportermentioning

confidence: 99%

Mitochondrial Ion Channels

O’Rourke

2007

Annu. Rev. Physiol.

279

153

View full text Add to dashboard Cite

In work spanning more than a century, mitochondria have been recognized for their multifunctional roles in metabolism, energy transduction, ion transport, inheritance, signaling, and cell death. Foremost among these tasks is the continuous production of ATP through oxidative phosphorylation, which requires a large electrochemical driving force for protons across the mitochondrial inner membrane. This process requires a membrane with relatively low permeability to ions to minimize energy dissipation. However, a wealth of evidence now indicates that both selective and nonselective ion channels are present in the mitochondrial inner membrane, along with several known channels on the outer membrane. Some of these channels are active under physiological conditions, and others may be activated under pathophysiological conditions to act as the major determinants of cell life and death. This review summarizes research on mitochondrial ion channels and efforts to identify their molecular correlates. Except in a few cases, our understanding of the structure of mitochondrial ion channels is limited, indicating the need for focused discovery in this area.

show abstract

Section: The Mitochondrial Ca 2+ Uniportermentioning

confidence: 99%

Mitochondrial Ion Channels

O’Rourke

2007

Annu. Rev. Physiol.

279

153

View full text Add to dashboard Cite

show abstract

“…The treatment with lithium di-jodosalycilate, used to extract additional glycoprotein, was applied to mitochondria from which the 'osmotic' glycoprotein had already been separated, and is described in [7]. The glycoprotein was purified from the 'osmotic' or 'LlS' extracts by preparative polyacrylamide gel electrophoresis, as described in [ 1,3] and in [2] for the case of beef liver mitochondria.…”

Section: Materials and Methomentioning

confidence: 99%

Interactions of a mitochondrial Ca²⁺‐binding glycoprotein with lipid bilayer membranes

et al. 1974

View full text Add to dashboard Cite

“…A soluble glycoprotein was identified as being located in the intermembrane space of rat-liver mitochondria [6]. The isolation of this protein is similar to that of a soluble Ca2+-binding glycoprotein of ox-liver mitochondria which contains sialic acid, phospholipid, and is sensitive to La3+ and ruthenium red [6].…”

Section: ~-mentioning

confidence: 68%

“…The isolation of this protein is similar to that of a soluble Ca2+-binding glycoprotein of ox-liver mitochondria which contains sialic acid, phospholipid, and is sensitive to La3+ and ruthenium red [6]. Another, insoluble, CaZ+-binding glycoprotein has been isolated from rat-liver mitochondria which also contains hexosamine, sialic acid, phospholipids, free fatty acids and chloroform -methanol-insoluble phosphorus [7].…”

Section: ~-mentioning

confidence: 72%

“…Another, insoluble, CaZ+-binding glycoprotein has been isolated from rat-liver mitochondria which also contains hexosamine, sialic acid, phospholipids, free fatty acids and chloroform -methanol-insoluble phosphorus [7]. This molecule is of higher molecular weight but shows similar CaZ+-binding kinetics and may actually be the molecule described by Sottocasa et al [6] plus some additional lipid material or membrane material.…”

Section: ~-mentioning

confidence: 99%

See 1 more Smart Citation

Transfer of Monosaccharide onto Exogenous Acceptors by Mitochondrial Glycosyl Transferases

Myers

Bosmann

1974

European Journal of Biochemistry

View full text Add to dashboard Cite

Mitochondrial glycosyl transferase have been studied by the transfer of labeled monosaccharide from nucleotide monosaccharide onto exogenous acceptor glycoproteins prepared by serial removal of carbohydrate from collagen, fetuin and immunoglobulin G. Triton X‐100 extracts of isolated mitochondria were used as enzyme source. Collagen minus glucose served as the best acceptor for the transfer of glucose from UDP‐glucose; immunoglobulin G minus sialic acid, galactose, N‐acetyl‐glucosamine and mannose served as the best acceptor for mannose from GDP‐mannose. The reaction has been studied for divalent cation requirement (glucosyl transfer is optimal with Mg2+; mannosyl transfer is optimal with Mn2+), temperature optima (30 °C) and pH optima (6.8). The data reveal some similarities and some differences between cytoplasmic and mitochondrial glycosyl transferases.

show abstract

Isolation of a soluble Ca2+ binding glycoprotein from ox liver mitochondria

Cited by 121 publications

References 18 publications

Mitochondrial Ion Channels

Mitochondrial Ion Channels

Interactions of a mitochondrial Ca²⁺‐binding glycoprotein with lipid bilayer membranes

Transfer of Monosaccharide onto Exogenous Acceptors by Mitochondrial Glycosyl Transferases

Contact Info

Product

Resources

About

Isolation of a soluble Ca2+ binding glycoprotein from ox liver mitochondria

Cited by 121 publications

References 18 publications

Mitochondrial Ion Channels

Mitochondrial Ion Channels

Interactions of a mitochondrial Ca2+‐binding glycoprotein with lipid bilayer membranes

Transfer of Monosaccharide onto Exogenous Acceptors by Mitochondrial Glycosyl Transferases

Contact Info

Product

Resources

About

Interactions of a mitochondrial Ca²⁺‐binding glycoprotein with lipid bilayer membranes