Phospholipid synthesis in rat liver mitochondria

Zborowski, Józef; Wojtczak, Lech

doi:10.1016/0005-2760(69)90134-9

Cited by 80 publications

(23 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Cardiolipin was synthesized on the inner membrane exclusively (16). Phosphatidic acid synthesis was localized primarily on the outer membrane of mitochondria from rat liver (35,36,43). The single related work with plants indicated that CDP-diglyceride was synthesized only on the inner membrane of mitochondria from mung bean hypocotyls (13).…”

Section: Discussionmentioning

confidence: 99%

“…Kaiser and Bygrave (17) showed that "C-labeled choline was incorporated into phosphatidylcholine in the outer membranes of intact rat liver mitochondria. Finally, Zborowski and Wojtczak (43) and Shephard and Hubscher (36) both determined that phosphatidic acid was synthesized primarily on the outer membrane of rat liver mitochondria. Only Douce et al (13) examined the inner and outer membranes of plant mitochondria for their capacities to synthesize a phospholipid.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Phospholipid Metabolism in Plant Mitochondria

Sparace¹,

Moore²

1979

Plant Physiol.

View full text Add to dashboard Cite

Intact mitochondria from the endosperm of castor bean were isolated on linear sucrose gradients. These mitochondria were ruptured and the membranes separated on discontinuous sucrose gradients into outer membrane, intact inner membrane, and ruptured inner membrane fractions. Each membrane fraction was examined for its capacity to synthesize phosphatidyl4ycerol, CDP-diglyceride, phosphatidylcholine via methylation, and phosphatidic acid. The syntheses of phosphatidylglycerol, CDPdiglyceride, and phosphatidylcholine were localized exclusively in the inner mitochondrial membrane fractions while phosphatidic acid synthesis occurred in both the inner and outer mitochondrial membranes.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Phospholipid Metabolism in Plant Mitochondria

Sparace¹,

Moore²

1979

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…However, whether these studied LPATs are located in the ER is unknown. In plants and other organisms, LPAT activities have been found in the microsomes, plasma membrane (Bursten et al, 1991), and mitochondria (Zborowski and Wojtczak, 1969). It is also unknown whether redundant LPATs encoded by different genes exist in an individual plant to perform the same or different physiological functions.…”

Section: Introductionmentioning

confidence: 99%

Ubiquitous and Endoplasmic Reticulum–Located Lysophosphatidyl Acyltransferase, LPAT2, Is Essential for Female but Not Male Gametophyte Development in Arabidopsis

2005

View full text Add to dashboard Cite

Lysophosphatidyl acyltransferase (LPAT) is a pivotal enzyme controlling the metabolic flow of lysophosphatidic acid into different phosphatidic acids in diverse tissues. We examined putative LPAT genes in Arabidopsis thaliana and characterized two related genes that encode the cytoplasmic LPAT. LPAT2 is the lone gene that encodes the ubiquitous and endoplasmic reticulum (ER)-located LPAT. It could functionally complement a bacterial mutant with defective LPAT. LPAT2 and 3 synthesized in recombinant bacteria and yeast possessed in vitro enzyme activity higher on 18:1-CoA than on 16:0-CoA. LPAT2 was expressed ubiquitously in diverse tissues as revealed by RT-PCR, profiling with massively parallel signature sequencing, and promoter-driven b-glucuronidase gene expression. LPAT2 was colocalized with calreticulin in the ER by immunofluorescence microscopy and subcellular fractionation. LPAT3 was expressed predominately but more actively than LPAT2 in pollen. A null allele (lpat2) having a T-DNA inserted into LPAT2 was identified. The heterozygous mutant (LPAT2/lpat2) had minimal altered vegetative phenotype but produced shorter siliques that contained normal seeds and remnants of aborted ovules in a 1:1 ratio. Results from selfing and crossing it with the wild type revealed that lpat2 caused lethality in the female gametophyte but not the male gametophyte, which had the redundant LPAT3. LPAT2-cDNA driven by an LPAT2 promoter functionally complemented lpat2 in transformed heterozygous mutants to produce the lpat2/lpat2 genotype. LPAT3-cDNA driven by the LPAT2 promoter could rescue the lpat2 female gametophytes to allow fertilization to occur but not to full embryo maturation. Two other related genes, putative LPAT4 and 5, were expressed ubiquitously albeit at low levels in diverse organs. When they were expressed in bacteria or yeast, the microbial extract did not contain LPAT activity higher than the endogenous LPAT activity. Whether LPAT4 and 5 encode LPATs remains to be elucidated.

show abstract

“…This effect cannot be due to a direct influence on the activity of acyl-GoA:L-glycerol-3-phosphate acyltransferase which does not require ATP. Mitochondrial acyl-GoA:L-glycerol-3-phosphate acyltransferase is located on the outer membrane (Bygrave, 1969;Zborowski and Wojtczak, 1969) and therefore is readily accessible to exogenous ATP. It is possible that the added ATP acts in copper-deficient mitochondria by protecting palmitoyl-GoA from transformation by either palmitoyl-GoA hydrolase or palmitoyl-GoA: carnitine palmitoyltransferase present in liver mitochondrial preparations, or by providing energy for regeneration of ["G]palmitoyI-GoA split during the incubation, thus favouring optimal incorporation into phospholipids.…”

Section: Disgussionmentioning

confidence: 99%

“…The situation could well be analogous to that of the influence of the glycoside, atractyloside, on phospholipid synthesis by mitochondria. Atractyloside inhibits the transport of adenine nucleotides through the mitochondrial membrane and thus inhibits phospholipid synthesis by mitochondria unless exogenous ATP is added (Zborowski and Wojtczak, 1969). Alternatively, as it is known that mitochondrial permeability is increased in certain respects by copper deficiency (Gallagher et al, 1956a) it is possible that ATP is produced in nonnal amounts but lost excessively from mitochondria into the cell sap thus limiting ATP-dependent reactions of mitochondrial enzyme systems.…”

Section: Disgussionmentioning

confidence: 99%

Copper Deficiency in the Rat Effect on Synthesis of Phospholipids

Gallagher

Reeve

1971

Aust J Exp Biol Med

View full text Add to dashboard Cite

Summary Copper deficiency depresses phospholipid synthesis by liver mitochondria, but not by liver microsomes. The effect of copper deficiency on mitochondrial phospholipid synthesis is eliminated by adding 1 mM ATP. Phospholipid synthesis by liver mitochondria from normal rats is inhibited by 0·1–1 mM CN− and restored to normal by 1mM ATP. Mitochondria do not synthesise phospholipids significantly under anaerobic conditions with or without added electron transfer systems unless ATP is added. There appears to be a direct causal relationship between the two major biochemical disturbances in copper deficiency. One, the loss of cytochrome oxidase activity, leading to the other, depressed synthesis of phospholipids by liver mitochondria, by interfering with the provision of endogenous ATP to maintain an optimal rate of synthesis under the experimental conditions. Copper deficiency does not deplete acyl‐CoA:L‐glycerol‐3‐phosphate acyltransferase (E.C.2.3.1.15.) from either microsomes or mitochondria. The activies of palmitoyl‐CoA hydrolase (E.C.3.1.2.2.) in liver microsomes or liver mitochondria and of palmitoyl‐CoA:carnitine palmitoyl‐transferase in liver mitochondria are not affected by copper deficiency.

show abstract

Phospholipid synthesis in rat liver mitochondria

Cited by 80 publications

References 48 publications

Phospholipid Metabolism in Plant Mitochondria

Phospholipid Metabolism in Plant Mitochondria

Ubiquitous and Endoplasmic Reticulum–Located Lysophosphatidyl Acyltransferase, LPAT2, Is Essential for Female but Not Male Gametophyte Development in Arabidopsis

Copper Deficiency in the Rat Effect on Synthesis of Phospholipids

Contact Info

Product

Resources

About