The distribution of glycosyl-phosphatidylinositol anchored proteins is differentially regulated by serum and insulin

Lisanti, Michael P.; Darnell, Jennifer C.; Chan, Betty; Rodríguez-Boulan, Enrique; Saltiel, Alan R.

doi:10.1016/0006-291x(89)91533-7

Cited by 46 publications

(22 citation statements)

References 23 publications

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“…A portion of at least one GPI-anchored protein, the ecto-receptor protein for cAMP, is released from the membrane through the activation of an endogenous PLC. This anchor cleavage following a nutritional upshift qualitatively resembles the lipolytic membrane release of some GPIanchored proteins (e.g., 5'-nucleotidase, alkaline phosphatase, lipoprotein lipase, and heparan sulfate proteoglycan) observed with cultured cells and tissues from vertebrates in response to glucose and insulin (Ishihara et al, 1987;Romero et al, 1988;Chan et al, 1988;Klip et al, 1988;Lisanti et al, 1989). In both cases, yeast as shown here andas far as is known-vertebrate cells, a phospholipase is activated in response to extrinsic signals.…”

Section: Discussionsupporting

confidence: 65%

“…Since cAMP plays an important role in the regulation of carbohydrate metabolism in both lower and higher eucaryotes, we examined if the cAMP-binding protein is involved in nutritional signaling. We tested if a change of the nutritional situation of yeast cells results in the cleavage of a GPI anchor in a similar fashion as the deprivation of vertebrate cells of serum factors (Lisanti et al, 1989). We found that, indeed, a change of media from non-fermentable carbon sources to glucose causes a rapid partial conversion of the photoaffinitylabeled amphiphilic cAMP-binding protein into its hydrophilic form (Fig.…”

Section: Glucose Effects Amphiphilic To Hydrophilic Conversion Of Thementioning

confidence: 99%

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Glucose induces lipolytic cleavage of a glycolipidic plasma membrane anchor in yeast

Müller

Bandlow

1993

The Journal of Cell Biology

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Abstract. In the yeast Saccharomyces cerevisiae an amphiphilic cAMP-binding protein has been found recently to be anchored to plasma membranes by virtue of a glycolipid structure Bandlow, 1991a, 1992). The cAMP-binding parameters of this protein are affected by the lipolytic removal of the glycosylphosphatidylinositol (GPI) membrane anchor by exogenous (G)PI-specific phospholipases C or D (PLC or PLD) (Miiller and Bandlow, 1993) suggesting a regulatory role of glycolipidic membrane anchorage. Here we report that transfer of yeast cells from lactate to glucose medium results in the conversion of the amphiphilic form of the cAMP receptor protein into a hydrophilic version accompanied by the rapid loss of fatty acids from the GPI anchor of the [14C]palmitic acid-labeled protein. Analysis of the cleavage site identifies [~4C]inositol phosphate as the major product after treatment of the soluble, [t4C]inositol-labeled protein with nitrous acid which destroys the glucosamine constituent of the anchor. Together with the observed cross-reactivity of the hydrophilic fragment with antibodies directed against the cross-reacting determinant of soluble trypanosomal variable surface glycoproteins (i.e., myo-inositol-l,2-cyclic phosphate) this demonstrates that, in membrane release, the initial cleavage event is catalyzed by an intrinsic GPI-PLC activated upon transfer of cells to glucose medium. Release from the plasma membrane in soluble form requires, in addition, the presence of high salt or or-methyl mannopyranoside, or the removal of the carbohydrate moieties, because otherwise the protein remains associated with the membrane presumably at least in part via its N-glycosidic carbohydrate side chains. The data point to the possibility that cleavage of the anchor could play a role in the transfer of the signal for the nutritional situation to the interior of the cell.

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Section: Discussionsupporting

confidence: 65%

Section: Glucose Effects Amphiphilic To Hydrophilic Conversion Of Thementioning

confidence: 99%

Glucose induces lipolytic cleavage of a glycolipidic plasma membrane anchor in yeast

Müller

Bandlow

1993

The Journal of Cell Biology

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“…It is possible that the sulphonylurea-and insulin-dependent releasing mechanisms share some common steps, since at submaximal concentrations the two agents act in a synergistic manner and at higher concentrations they do not exceed a maximal level of release. Up until now, insulin-regulated membrane release of GPI-proteins has been reported for 3T3-LI adipocytes [LPL (Eckel et al, 1978;Spooner et al, 1979;Chan et al, 1988); several unidentified proteins (Lisanti et al, 1989); 5'-nucleotidase and cAMP-binding ectoprotein (this study)], BC3H1 myocytes [alkaline phosphatase (Romero et al, 1988)] and HepG-2 cells [heparan sulphate proteoglycan (Ishihara et al, 1987)], for membranes prepared from rat hindquarter muscles after perifusion with insulin [5'-nucleotidase (Klip et al, 1988)] and for rat osteosarcoma cells after culture in the presence of insulin [alkaline phosphatase (Levy et al, 1984)]. …”

Section: Discussionmentioning

confidence: 99%

“…RESULTS 3T3-Ll adipocytes contain a number of GPI-anchored plasmamembrane proteins (Chan et al, 1988;Lisanti et al, 1989). Release of these ectoproteins from the plasma membrane into the culture medium by removal of their GPI membrane anchor has been observed after short-term incubation with insulin (see the Discussion).…”

Section: Miscellaneous Proceduresmentioning

confidence: 97%

“…(1 993) 289,[509][510][511][512][513][514][515][516][517][518][519][520][521] insulin accompanied by release of the protein moiety from the cell surface of adipocytes and myocytes has been observed (Chan et al, 1988;Romero et al, 1988;Lisanti et al, 1989) and correlated with stimulation of glucose metabolism (Romero et al, 1988). Furthermore, the cleavage products of structurally related free GPI lipids, diacylglycerol and polar phosphoinositolglycan headgroups, activate glucose transport in isolated rat adipocytes presumably by a two-step mechanism (ObermaierKusser et al, 1989;Vogt et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

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The sulphonylurea drug, glimepiride, stimulates release of glycosylphosphatidylinositol-anchored plasma-membrane proteins from 3T3 adipocytes

Müller

Dearey

Pünter

1993

Biochemical Journal

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Sulphonylurea drugs stimulate glucose transport and metabolism in muscle and fat cells in vitro. The molecular basis for the insulin-mimetic extrapancreatic effects of these oral antidiabetic therapeutic agents is unknown at present. Here we demonstrate that incubation of 3T3 adipocytes with the novel sulphonylurea, glimepiride, causes a time- and concentration-dependent release of the glycosylphosphatidylinositol (GPI)-anchored ecto-proteins, 5′-nucleotidase, lipoprotein lipase and a 62 kDa cyclic AMP (cAMP)-binding protein from the plasma membrane into the culture medium. The change in the localization is accompanied by conversion of the membrane-anchored amphiphilic proteins into their soluble hydrophilic versions, as judged by pulse-chase experiments and Triton X-114 partitioning, and by appearance of anti-cross-reacting determinant (CRD) immunoreactivity of the released proteins as shown by Western blotting. Metabolic labelling of cells with myo-[14C]inositol demonstrates that inositol is retained in the major portion of released lipoprotein lipase and cAMP-binding ectoprotein. The identification of inositol phosphate after deamination of these proteins with nitrous acid suggests cleavage of their GPI membrane anchor by a GPI-specific phospholipase C. However, after longer incubation with glimepiride the amount of soluble versions of the GPI-proteins lacking inositol and anti-CRD immunoreactivity increases, which may be caused by additional drug-stimulated hydrolytic events within their GPI structure or C-termini. Since insulin also stimulates membrane release of these GPI-modified proteins, and in combination with glimepiride in a synergistic manner, sulphonylurea drugs may exert their peripheral actions in adipose tissue by using (part of) the insulin postreceptor signalling cascade at the step of activation of a GPI-specific phospholipase C.

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Control of alkaline phosphatase activity in C3H10T1/2 cells: Role of retinoic acid and cell density

Reese

Larsen

Hornicek

1992

Journal Cellular Physiology

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The enzyme alkaline phosphatase (AP) has been shown to be lost or inappropriately expressed during carcinogenesis in some tissues. Because retinoic acid (RA) appears to play a role in the normal regulation of the enzyme (RA up-regulates AP in a variety of cell types) we have suggested that altered AP expression in some cancers may be caused by a defect in the ability of the cells to respond normally to retinoid. We have begun to use the chemically transformable mouse embryo fibroblast cell, C3H10T1/2, to investigate this possibility. In this initial study we characterized AP regulation in normal C3H10T1/2 cells and show that: (1) 10(-7) M RA increases AP activity within 3-4 h in serum-free medium; (2) serum inhibits short-term induction (0-8 h) in a concentration-dependent manner (10% serum causes complete inhibition); (3) during long-term RA exposure (24 h and 48 h), induction can be detected in serum-containing medium; (4) AP induction is dose related at RA concentrations from 10(-10) M to 10(-6) M in serum-free medium; (5) 10(-5) M RA is ineffective at inducing AP in serum-free medium during 8 h but is the most effective concentration in serum-containing medium during 24 h and 48 h exposures; (6) AP inducibility by RA requires near-confluent cell densities; and (7) when cultures become confluent, cells become constitutive for AP and no longer require RA for enzyme expression. The effects of serum and cell density on AP inducibility by RA and implications of the RA up-regulation of AP for teratogenesis are discussed.

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The distribution of glycosyl-phosphatidylinositol anchored proteins is differentially regulated by serum and insulin

Cited by 46 publications

References 23 publications

Glucose induces lipolytic cleavage of a glycolipidic plasma membrane anchor in yeast

Glucose induces lipolytic cleavage of a glycolipidic plasma membrane anchor in yeast

The sulphonylurea drug, glimepiride, stimulates release of glycosylphosphatidylinositol-anchored plasma-membrane proteins from 3T3 adipocytes

Control of alkaline phosphatase activity in C3H10T1/2 cells: Role of retinoic acid and cell density

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