Partial structure of an insulin-sensitive glycophospholipid

Mato, José M.; Kelly, Kathleen; Abler, Andrew S.; Jarett, Leonard; Corkey, Barbara E.; Cashel, Jo Anne; Zopf, David

doi:10.1016/0006-291x(87)90595-x

Cited by 145 publications

(137 citation statements)

References 11 publications

Supporting

Mentioning

122

Contrasting

Unclassified

Order By: Relevance

“…Considerable progress has been made in the last two years regarding the identification of water-soluble mediators [l-3] that stimulate glycogen synthase phosphatase [4] and mimic several other actions of insulin [ 1,5,6] even in intact cells [5]. These purported insulin mediators are inositol-containing phosphoglycans (IPG) produced by phospholipase C (PL-C) hydrolysis of phospholipid-glycans present in B&H1 myocytes [ 11, liver membranes [2] or H35 hepatoma cells [3]. They have been equated to the 'polar head groups' isolated from insulin-treated BCsH 1 myocytes [l] or H35 hepatoma cells [3], which are generated roughly in a 1: 1 ratio to diacylglycerol [ 11. In cell membranes, IPGs are found in phosphatidylinositol-glycans (phospholipid-glycans) and in phosphatidylinositol-glycan-ethanolamine-proteins (henceforth referred to as phospholipid-glycan-proteins) (review [7]).…”

Section: Introductionmentioning

confidence: 99%

“…These purported insulin mediators are inositol-containing phosphoglycans (IPG) produced by phospholipase C (PL-C) hydrolysis of phospholipid-glycans present in B&H1 myocytes [ 11, liver membranes [2] or H35 hepatoma cells [3]. They have been equated to the 'polar head groups' isolated from insulin-treated BCsH 1 myocytes [l] or H35 hepatoma cells [3], which are generated roughly in a 1: 1 ratio to diacylglycerol [ 11. In cell membranes, IPGs are found in phosphatidylinositol-glycans (phospholipid-glycans) and in phosphatidylinositol-glycan-ethanolamine-proteins (henceforth referred to as phospholipid-glycan-proteins) (review [7]). Membrane proteins anchored to the membrane through phospholipid-glycans include 5 ' -nucleotidase and alkaline phosphatase (reviews [8,17]).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Insulin‐induced decrease in 5′‐nucleotidase activity in skeletal muscle membranes

et al. 1988

View full text Add to dashboard Cite

Insulin releases inositol phosphoglycansfrom myocytes in culture [(1986) Science 233,967-9721, which display insulinomimetic activity. Because S'nucleotidase is anchored to the membrane through inositol-containing phospholipid glycans, we investigated whether insulin could release the enzyme from the membrane. Membranes prepared from hindquarter muscles of rats perfused with insulin showed a 23% decrease in S-nucleotidase activity. Isolated membranes from muscle exposed to insulin in vitro also showed a small but reproducible decrease (9%) in S-nucleotidase activity relative to unexposed controls. Phospholipase C from Staphylococcus aureus released m of the membrane-bound S-nucleotidase. We propose that insulin may activate an endogenous phospholipase C that cleaves phospholipid-glycan-anchored proteins.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Insulin‐induced decrease in 5′‐nucleotidase activity in skeletal muscle membranes

et al. 1988

View full text Add to dashboard Cite

show abstract

“…In a variety of cells including murine myocytes BC3H1 [l], H35 hepatoma cells [2], T lymphocytes [3] and rat hepatocytes [4], insulin promotes the phosphodiesteratic hydrolysis of a glycosyl-phosphatidylinositol (glycosyl-PtdIns) and thus releases and increases the intracellular levels of the polar headgroup of this lipid. This polar headgroup, a phosphooligosaccharide containing inositol, glucosamine, galactose and phosphate [I, 2, 5, 61, mimics insulin-directed effects on protein phosphorylation/dephosphorylation [7], as well as a variety of the biological effects of this hormone, including lipolysis [8], lipogenesis [9] and the effects of the hormone on pyruvate kinase, glycogen phosphorylase and cyclic AMP levels [lo].…”

mentioning

confidence: 99%

Asymmetric distribution of the phosphatidylinositol‐linked phospho‐oligosaccharide that mimics insulin action in the plasma membrane

Varela

Alvarez

Clemente

et al. 1990

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

We have investigated the topography of a glycosyl-phosphatidylinositol implicated in insulin action by a combination of two complementary methods : (a) chemical labelling with a non-permeable (isethionyl acetimidate) and a permeable (ethyl acetimidate) probe; and (b) enzymatic modifications with P-galactosidase (EC 3.2.1.23) or phosphatidylinositol-specific phospholipase C (EC 3.1.4.3). Using the first approach the majority of the glycosyl-phosphatidylinositol is found in the outer surface of intact hepatocytes, adipocytes, fibroblasts and lymphocytes, but not in erythrocytes which presented only a 20% of the total labelled glycosyl-phosphatidylinositol to the exterior. Upon insulin addition ( 3 0 nM), about 60% of the total glycosyl-phosphatidylinositol was hydrolysed in both hepatocytes and adipocytes but not in erythrocytes. In agreement with the extracellular localization in hepatocytes and with the proposed role of this glycolipid in insulin action, treatment of rat hepatocytes with fl-galactosidase from Escherichia coli, an enzyme that hydrolyses the oligosaccharide moiety of the glycosylphosphatidylinositol, cleaved 65% of the total glycophospholipid and blocked the effect of insulin (but not of glucagon) on pyruvate kinase (EC 2.7.1.40). Similar treatment with phosphatidylinositol-specific phospholipase C from Bacillus cereus hydrolysed 62% of the total glycosyl-phosphatidylinositol. From the various approaches used it is concluded that the majority of this glycophospholipid is at the outer surface in a variety of insulinsensitive cells. In a variety of cells including murine myocytes BC3H1 [l], H35 hepatoma cells [2], T lymphocytes [3] and rat hepatocytes[4], insulin promotes the phosphodiesteratic hydrolysis of a glycosyl-phosphatidylinositol (glycosyl-PtdIns) and thus releases and increases the intracellular levels of the polar headgroup of this lipid. This polar headgroup, a phosphooligosaccharide containing inositol, glucosamine, galactose and phosphate [I, 2, 5, 61, mimics insulin-directed effects on protein phosphorylation/dephosphorylation [7], as well as a variety of the biological effects of this hormone, including lipolysis [8], lipogenesis [9] and the effects of the hormone on pyruvate kinase, glycogen phosphorylase and cyclic AMP levels [lo]. These studies suggest that this glycosyl-Ptdlns is implicated in insulin action. This glycosyl-PtdIns has features in common with the glycosyl-PtdIns anchor of a number of cell membrane proteins (for recent reviews see [I 1 -131). These similarities include : (a) the observation that the insulin-sensitive glycosyl-PtdIns is hydrolysed by the phosphatidyl-inositol-specific phospholipase C (PtdIns-specific phospholiCorrespondence to I. Varela, Metabolismo, Nutricion y Hormonas, Fundacion Jimenez Diaz and C.S.I.C

show abstract

“…Saltiel et al [9,10] and Mato et al [11] demonstrated the possibility that insulin generated chemical mediators by activating an insulinsensitive phospholipase C acting on a novel glycophospholipid.…”

Section: When Fat Cells Were Incubated With D-myo-mentioning

confidence: 99%

“…It has been suggested that one or more chemical mediators are generated subsequent to this interaction and alter the activities of some insulin sensitive enzymes [7,8]. Several investigators suggest the possibility that insulin generated chemical mediators by activating an insulin-sensitive phospholipase C acting as a novel glycophospholipid [9][10][11].…”

Section: Introductionmentioning

confidence: 99%

A significant increase of lysophosphatidylinositol 4‐phosphate with insulin in isolated rat fat cells

et al. 1987

View full text Add to dashboard Cite

We studied the effects of insulin on the incorporation of 32P i into phospholipids in rat fat cells. When the cells were treated with insulin, a new radioactive phospholipid was detected on thin layer chromatography. The substance migrated slower than phosphatidylinositol 4,5-bisphosphate and was hardly detectable in the absence of insulin. This effect of insulin was both time-and dose-dependent with half-maximal stimulation at 120 #U/ml. Pretreatment of insulin with anti-insulin antibody or the cells with anti-insulin receptor antibody inhibited the effect of insulin. The product of phosphatidylinositol 4-phosphate hydrolyzed by phospholipase A z was coincided with the substance on thin layer chromatography. Quinacrine inhibited the formation of the substance in a dose-dependent manner. These results suggested that insulin stimulates the generation of lysophosphatidylinositol 4-phosphate through the insulin-receptor interaction.

show abstract

Partial structure of an insulin-sensitive glycophospholipid

Cited by 145 publications

References 11 publications

Insulin‐induced decrease in 5′‐nucleotidase activity in skeletal muscle membranes

Insulin‐induced decrease in 5′‐nucleotidase activity in skeletal muscle membranes

Asymmetric distribution of the phosphatidylinositol‐linked phospho‐oligosaccharide that mimics insulin action in the plasma membrane

A significant increase of lysophosphatidylinositol 4‐phosphate with insulin in isolated rat fat cells

Contact Info

Product

Resources

About