Cell surface glycoconjugates as onco-differentiation markers in hematopoietic cells

Fukuda, Minoru

doi:10.1016/0304-419x(84)90002-7

Cited by 110 publications

(104 citation statements)

References 123 publications

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“…5A, lane 6), and this band became 41 kDa when treated further with endo-␤-galactosidase. The sensitivity to endo-␤-galactosidase strongly suggests the presence of polylactosaminoglycans (39). These findings indicate that the 37-kDa band is a nonglycosylated form and that the 41-kDa species contains a high mannose-type oligosaccharide.…”

Section: Fig 3 Northern Hybridization Analysis Of the Pap Isozymesmentioning

confidence: 78%

Cloning and Characterization of Two Human Isozymes of Mg2+-independent Phosphatidic Acid Phosphatase

Kai

Wada

Imai

et al. 1997

Journal of Biological Chemistry

175

211

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We obtained two human cDNA clones encoding phosphatidic acid phosphatase (PAP) isozymes named PAP-2a (M r ‫؍‬ 32,158) and -2b (M r ‫؍‬ 35, 119), both of which contained six putative transmembrane domains. Both enzymes were glycosylated and cleaved by N-glycanase and endo-␤-galactosidase, thus suggesting their post-Golgi localization. PAP-2a and -2b shared 47% identical sequence and were judged to be the human counterparts of the previously sequenced mouse 35-kDa PAP(83% identity) and rat Dri42 protein (94% identity), respectively. Furthermore, the sequences of both PAPs were 34 -39% identical to that of Drosophila Wunen protein. In view of the functions ascribed to Wunen and Dri42 in germ cell migration and epithelial differentiation, respectively, these findings unexpectedly suggest critical roles of PAP isoforms in cell growth and differentiation. Although the two PAPs hydrolyzed lysophosphatidate and ceramide-1-phosphate in addition to phosphatidate, the hydrolysis of sphingosine-1-phosphate was detected only for PAP-2b. PAP-2b was expressed almost ubiquitously in all human tissues examined, whereas the expression of PAP-2a was relatively variable, being extremely low in the placenta and thymus. In HeLa cells, the transcription of PAP-2a was not affected by different stimuli, whereas PAP-2b was induced (up to 3-fold) by epidermal growth factor. These findings indicate that despite structural similarities, the two PAP isozymes may play distinct functions through their different patterns of substrate utilization and transcriptional regulation.Phosphatidic acid phosphatase (PAP) 1 (EC 3.1.3.4) supplies diacylglycerol (DG) in glycerolipid biosynthesis by dephosphorylating phosphatidic acid (PA) (1). Since both DG (2) and PA (3) are potent signaling molecules, PAP plays an important role in cellular signal transduction in addition to lipid biosynthesis (4). In signaling systems mediated by phospholipase D (5), liberated PA is generally converted, albeit to different extents, to DG by the action of PAP (6 -8), thus suggesting that PAP contributes to the control of the relative balance of the two lipid second messengers.There exist two forms of mammalian PAP that can be distinguished with respect to subcellular localization and enzymologic properties (9). So far, distinct functions have been ascribed to the two forms of PAP. The type 1 PAP, a Mg 2ϩ -dependent and N-ethylmaleimide-sensitive enzyme, is considered to be primarily involved in lipid synthesis based on its translocation from the cytosol to microsomes upon stimulation of cellular triacylglycerol synthesis (10 -12). In this context, a recent work showed using a novel enzyme inhibitor that the type 1 PAP indeed participated in triacylglycerol synthesis in mouse macrophages (13). On the other hand, the type 2 PAP, a Mg 2ϩ -independent and N-ethylmaleimide-insensitive enzyme, has been postulated to participate in cellular signal transduction mediated by phospholipase D. The finding that the activities of the type 2 PAP and phospholipase D were decreased in a c...

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Section: Fig 3 Northern Hybridization Analysis Of the Pap Isozymesmentioning

confidence: 78%

Cloning and Characterization of Two Human Isozymes of Mg2+-independent Phosphatidic Acid Phosphatase

Kai

Wada

Imai

et al. 1997

Journal of Biological Chemistry

175

211

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“…Extension of polylactosamine chains requires the repeated sequential addition of only two oligosaccharides such that this glycosylation motif might be particularly sensitive to residence time in the Golgi apparatus. Such an influence of cellular and Golgi organization on polylactosamine glycosylation could explain the differential degree of LAMP polylactosamine glycosylation found during cellular differentiation and transformation (Fukuda, 1985;Heffernan et al, 1989;Youakim et al, 1989;Amos and Lotan, 1990;Lee et al, 1990;Saitoh et al, 1992).…”

Section: Discussionmentioning

confidence: 99%

“…cosylation sites (Carlsson and Fukuda, 1990). Changes in expression and structure of polylactosamine glycans are associated with cellular differentiation and oncogenesis (Fukuda, 1985). Extensive polylactosamine glycosylation is found on the LAMP-1 homologous P2B antigen of the highly metastatic cell line MDAY (Heffernan et al, 1989), and increased polylactosamine glycosylation of LAMP-1 and LAMP-2 are associated with increased metastatic ability in sublines of human colon carcinoma (Saitoh et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer.

Nabi

Rodríguez-Boulan

1993

MBoC

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An endogenous Madin-Darby canine kidney (MDCK) lysosomal membrane glycoprotein that exhibits a basolateral targeting pathway to the lysosome is shown here to exhibit significant N-terminal amino acid sequence identity to lysosomal associated membrane proteins (LAMP-2) of other species. During establishment of the MDCK monolayer after only 1 d of culture, this canine LAMP-2 has a larger molecular size (110 kDa) than following formation of a confluent monolayer after 3 d of culture (100 kDa) due to the increased presence of N-linked polylactosamine oligosaccharide chains. Neither polylactosamine glycosylation of LAMP-2 in MDCK cells nor truncation of N-linked oligosaccharide chains of LAMP-2 in a ricin-resistant MDCK-RCAR cell line influenced the basolateral polarity of its targeting. However, the rate of basolateral delivery of LAMP-2 in MDCK cells plated for 3 d was significantly faster (tl/2 = 28 min) than in 1-d cells (tl/2 = 40 min); in MDCK-RCAR cells the rate of basolateral delivery at both 1 and 3 d of plating was similar (t1/2 = 40 min). The rate differential in MDCK cells occurred after arrival of LAMP-2 to the Golgi apparatus because the rate of acquisition of endoglycosidase H resistance was the same (t1/2 = 25 min) at both days of plating. The rate of transit of LAMP-2 through the Golgi apparatus to the basolateral domain was therefore far more rapid (-4-fold) in 3 d compared with 1-d MDCK cultures. The increased polylactosamine glycosylation of MDCK LAMP-2 at early times of plating during the establishment of a confluent epithelial monolayer may thus be related to its longer residence time in the Golgi apparatus.

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“…Increased expression of polylactosamine and the associated Lewis and blood group antigens are carcinoma markers (Fukuda, 1985;Hakamori, 1989). Modified expression of polylactosamine is also associated with cellular differentiation of various cell types (Spillmann and Finne, 1987;Youakim et al, 1989;Amos and Lotan, 1990;Lee et al, 1990;Tuo et al, 1992;Nabi and Rodriguez-Boulan, 1993).…”

Section: Expression Of Mlbs In Glcnac-tv-transfected Mv1lu Cellsmentioning

confidence: 99%

Biogenesis of Multilamellar Bodies via Autophagy

Hariri

Millane

Guimond

et al. 2000

MBoC

162

142

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Transfection of Mv1Lu mink lung type II alveolar cells with ␤1-6-N-acetylglucosaminyl transferase V is associated with the expression of large lysosomal vacuoles, which are immunofluorescently labeled for the lysosomal glycoprotein lysosomal-associated membrane protein-2 and the ␤1-6-branched N-glycan-specific lectin phaseolis vulgaris leucoagglutinin. By electron microscopy, the vacuoles present the morphology of multilamellar bodies (MLBs). Treatment of the cells with the lysosomal protease inhibitor leupeptin results in the progressive transformation of the MLBs into electron-dense autophagic vacuoles and eventual disappearance of MLBs after 4 d of treatment. Heterologous structures containing both membrane lamellae and peripheral electron-dense regions appear 15 h after leupeptin addition and are indicative of ongoing lysosome-MLB fusion. Leupeptin washout is associated with the formation after 24 and 48 h of single or multiple foci of lamellae within the autophagic vacuoles, which give rise to MLBs after 72 h. Treatment with 3-methyladenine, an inhibitor of autophagic sequestration, results in the significantly reduced expression of multilamellar bodies and the accumulation of inclusion bodies resembling nascent or immature autophagic vacuoles. Scrape-loaded cytoplasmic FITC-dextran is incorporated into lysosomal-associated membrane protein-2-positive MLBs, and this process is inhibited by 3-methyladenine, demonstrating that active autophagy is involved in MLB formation. Our results indicate that selective resistance to lysosomal degradation within the autophagic vacuole results in the formation of a microenvironment propicious for the formation of membrane lamella. INTRODUCTIONMultilamellar bodies (MLBs) are membrane-bound cellular organelles, which vary in size from 100-2400 nm, are composed of concentric membrane layers, and frequently exhibit an electron-dense core. MLBs are found in numerous cell types where they function in lipid storage and secretion (Schmitz and Mü ller, 1991). In lung type II alveolar cells, MLBs function as secretory granules whose exocytosis results in the deposition of the tubular myelin forms of surfactant on the surface of the alveolae (Hatasa and Nakamura, 1965;Ryan et al., 1975;Williams, 1977). The surfactant film over the alveolar epithelium regulates the surface tension at the air-cell interface and protects the alveola from collapse during respiration (Haagman and van Golde, 1991).Although the secretory function of MLBs in type II alveolar cells is well established, the precise mechanism of MLB biogenesis remains unclear. Autoradiographic studies of murine type II alveolar cells of mouse lungs showed that although phospholipids labeled with [ 3 H]choline are delivered directly from the Golgi to the MLB, proteins metabolically labeled with [ 3 H]leucine are visualized within multivesicular bodies before delivery to MLBs (Chevalier and Collet, 1972). Surfactant proteins A, B, and C are delivered via multivesicular bodies to MLBs, and multivesicular bodies are proposed as th...

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Cell surface glycoconjugates as onco-differentiation markers in hematopoietic cells

Cited by 110 publications

References 123 publications

Cloning and Characterization of Two Human Isozymes of Mg2+-independent Phosphatidic Acid Phosphatase

Cloning and Characterization of Two Human Isozymes of Mg2+-independent Phosphatidic Acid Phosphatase

Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer.

Biogenesis of Multilamellar Bodies via Autophagy

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