Degranulation and sex‐specific regranulation of reticular membranes from rat liver as studied using a spectrophotometric assay of protein disulphide isomerase

Dani, H. M.; Fielder, John A.; Rabin, B. R.

doi:10.1016/0014-5793(76)80151-2

Cited by 6 publications

(7 citation statements)

References 16 publications

(17 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Comparison with previous studies on PDI Previous work on liver microsomal PDI has shown that various treatments activate the enzyme to some extent. The treatments include lipid extraction with acetone followed by buffer solubilization from the acetone-dried power (Givol et al, 1964;De Lorenzo et al, 1966;Hawkins & Freedman, 1976;Ohba et al, 1981), solubilization by detergents (Ohba et al, 1977(Ohba et al, , 1981Freedman et al, 1978), centrifugation and resuspension (Drazic & Cottrell, 1977;Ohba et al, 1977) and treatments leading to displacement of ribosomes (Williams et al, 1968;Dani et al, 1976). In all these studies some PDI activity was detected in pellet as a percentage of that retained in microsomes treated comparably but in the absence of detergent.…”

Section: Solubilization Ofmicrosomal Enzymes By Detergentsmentioning

confidence: 99%

The latency of rat liver microsomal protein disulphide-isomerase

Lambert¹,

Freedman²

1985

Biochemical Journal

View full text Add to dashboard Cite

Protein disulphide-isomerase (PDI) activity was not detectable in freshly prepared rat liver microsomes (microsomal fraction), but became detectable after treatments that damage membrane integrity, e.g. sonication, detergent treatment or freezing and thawing. Maximum activity was detectable after sonication. Identical latency was observed in microsomes prepared by gel filtration and in those prepared by high-speed centrifugation. PDI activity was latent in all particulate subcellular fractions, but not latent in the high-speed supernatant. When all fractions were sonicated to expose total PDI activity, PDI was found at highest specific activity in the microsomal fraction and co-distributed with marker enzymes of the endoplasmic reticulum. Washing of microsomes under various conditions that removed peripheral proteins and, in some cases, bound ribosomes did not remove significant quantities of PDI, nor did it affect the latency of PDI activity. Treatment of microsomes with proteinases, under conditions where the permeability barrier of the microsomal vesicles was maintained intact, did not inactivate PDI significantly or affect its latency. PDI was very readily solubilized from microsomal vesicles by low concentrations of detergents, which removed only a fraction of the total microsomal protein. In all these respects, PDI resembled nucleoside diphosphatase, a marker peripheral protein of the luminal surface of the endoplasmic reticulum, and differed from NADPH: cytochrome c reductase, a marker integral protein exposed at the cytoplasmic surface of the membrane. The data are compatible with a model in which PDI is loosely associated with the luminal surface of the endoplasmic reticulum, a location consistent with the proposed physiological role of the enzyme as catalyst of formation of native disulphide bonds in nascent and newly synthesized secretory proteins.

show abstract

Section: Solubilization Ofmicrosomal Enzymes By Detergentsmentioning

confidence: 99%

The latency of rat liver microsomal protein disulphide-isomerase

Lambert¹,

Freedman²

1985

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…1 An enzyme from liver, called disulfide interchange enzyme, reshufflace, or rearrangease, 2 was identified as facilitating the refolding of ribonuclease by forming the disulfide bonds to obtain the lowest energy structure. 3 This enzyme came to be known as protein disulfide isomerase (PDI; EC.5.3.4.1) and was established as a critical component of the biosynthetic pathway for proteins.…”

Section: Introduction To Thiol Isomerasesmentioning

confidence: 99%

Vascular thiol isomerases

Flaumenhaft

Furie

2016

Blood

View full text Add to dashboard Cite

Thiol isomerases are multifunctional enzymes that influence protein structure via their oxidoreductase, isomerase, and chaperone activities. These enzymes localize at high concentrations in the endoplasmic reticulum of all eukaryotic cells where they serve an essential function in folding nascent proteins. However, thiol isomerases can escape endoplasmic retention and be secreted and localized on plasma membranes. Several thiol isomerases including protein disulfide isomerase, ERp57, and ERp5 are secreted by and localize to the membranes of platelets and endothelial cells. These vascular thiol isomerases are released following vessel injury and participate in thrombus formation. Although most of the activities of vascular thiol isomerases that contribute to thrombus formation are yet to be defined at the molecular level, allosteric disulfide bonds that are modified by thiol isomerases have been described in substrates such as αIIbβ3, αvβ3, GPIbα, tissue factor, and thrombospondin. Vascular thiol isomerases also act as redox sensors. They respond to the local redox environment and influence S-nitrosylation of surface proteins on platelets and endothelial cells. Despite our rudimentary understanding of the mechanisms by which thiol isomerases control vascular function, the clinical utility of targeting them in thrombotic disorders is already being explored in clinical trials.

show abstract

“…In the present paper we follow our previous studies (Dani et al, 1976) with some new observations on the binding of 60S ribosomal subunits, monoribosomes, oligoribosomes and unfractionated polyribosomes (all prepared without high-salt treatment) to reticular membranes, by using a methodology based on the enzyme protein disulphide-isomerase, the activity of which is masked by ribosome-membrane interaction.…”

mentioning

confidence: 94%

“…The high-salt treatments often used in the preparation of degranulated membranes and ribosomal fractions may drastically alter the binding properties of both entities. High-salt treatment causes partial degranulation of rough membranes (Adelman et al, 1973;Dani et al, 1976) and destroys membrane-bound protein disulphide-isomerase activity (Dani et al, 1976). High-salt treatment also solubilizes some initiation factors for protein synthesis (Schreier & Staehelin, 1973) and is believed to remove from polyribosomes a factor that appears to mediate detachment of monoribosomes from rough microsomal fractions (Blobel, 1976).…”

mentioning

confidence: 99%

The binding of monoribosomes, oligoribosomes and polyribosomes to reticular membranes from rat liver

Fielder¹,

Dani²,

Ridge³

et al. 1978

Biochemical Journal

View full text Add to dashboard Cite

1. The activity of the enzyme protein disulphide-isomerase (EC 5.3.4.1) was used to measure the binding of ribosomal fractions to reticular membranes from the liver of unstarved male rats. 2. Membranes degranulated by treatment with KCl plus puromycin and washed by centrifugation through 0.5 M-KCl bound oligoribosomes but not monoribosomes. 3. Substitution of 0.25 M-KCl for 0.5 M-KCl in the wash solution produced membranes that bound monoribosomes and 60 S subunits in addition to oligoribosomes. 4. The binding of all classes of ribosomes to smooth and 'lightly granulated' rough membranes was activated by oestradiol. The hormone activation was much greater with polyribosomes from fed rats than for monoribosomes or oligoribosomes from starved rats. 5. Exposure of rough membranes to centrifugal forces caused them to undergo partial degranulation, as demonstrated by unmasking of protein disulphide-isomerase activity.

show abstract

Degranulation and sex‐specific regranulation of reticular membranes from rat liver as studied using a spectrophotometric assay of protein disulphide isomerase

Cited by 6 publications

References 16 publications

The latency of rat liver microsomal protein disulphide-isomerase

The latency of rat liver microsomal protein disulphide-isomerase

Vascular thiol isomerases

The binding of monoribosomes, oligoribosomes and polyribosomes to reticular membranes from rat liver

Contact Info

Product

Resources

About