A specific acid α-glucosidase in lamellar bodies of the human lung

Vries, A.C.J. de; Schram, A. W.; Tager, J. M.; Batenburg, Joseph J.; Golde, L.M.G. Van

doi:10.1016/0005-2760(85)90046-3

Cited by 22 publications

(14 citation statements)

References 33 publications

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“…Furthermore, the expression of LAMP-2 in the MLBs of GlcNAc-TV-transfected Mv1Lu cells is consistent with the previously described lysosomal nature of this organelle (Balis and Conen, 1964;Hatasa and Nakamura, 1965;Goldfischer et al, 1968;Hoffman, 1972;DiAugustine, 1974;Heath et al, 1976;Hook and Gilmore, 1982;de Vries et al, 1985;Voorhut et al, 1992). To assess the role of lysosomal degradation on MLB expression, M1 cells were treated with the lysosomal Figures 4E and 5A).…”

Section: Lysosomal Degradation Is Necessary For Mlb Biogenesissupporting

confidence: 83%

“…© 2000 by The American Society for Cell Biology 255 Heath et al, 1976;Hook and Gilmore, 1982;de Vries et al, 1985). It has been previously suggested based on morphological criteria that MLBs form via cellular autophagy (Balis and Conen, 1964;Sorokin, 1967;Flaks and Flaks, 1972;Stratton, 1978).…”

Section: Introductionmentioning

confidence: 99%

“…Surfactant proteins A, B, and C are delivered via multivesicular bodies to MLBs, and multivesicular bodies are proposed as the site of processing of surfactant precursor to mature forms; both multivesicular bodies and MLBs express the lysosomal marker CD63 and are therefore part of the lysosomal pathway (Voorhut et al, 1992(Voorhut et al, , 1993. The lysosomal nature of the MLB has been demonstrated by the localization of various lysosomal enzymes to this organelle (Balis and Conen, 1964;Hatasa and Nakamura, 1965;Goldfischer et al, 1968;Hoffman, 1972;DiAugustine, 1974;Heath et al, 1976;Hook and Gilmore, 1982;de Vries et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

“…E-mail address: ivan.robert.nabi@ umontreal.ca. Abbreviations used: AV d , degradative autophagic vacuole; AV i , nascent or immature autophagic vacuole; GlcNAc-TV, ␤1-6-Nacetylglucosaminyl transferase V; LAMP-2, lysosomal-associated membrane protein-2; 3-MA, 3-methyladenine; L-PHA, phaseolis vulgaris leucoagglutinin; MLB, multilamellar body; PBS/CM, PBS supplemented with 0.1 mM Ca 2ϩ and 1 mM Mg 2ϩ .© 2000 by The American Society for Cell Biology 255 Heath et al, 1976;Hook and Gilmore, 1982;de Vries et al, 1985). It has been previously suggested based on morphological criteria that MLBs form via cellular autophagy (Balis and Conen, 1964;Sorokin, 1967;Flaks and Flaks, 1972;Stratton, 1978).…”

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Biogenesis of Multilamellar Bodies via Autophagy

Hariri

Millane

Guimond

et al. 2000

MBoC

162

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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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Section: Lysosomal Degradation Is Necessary For Mlb Biogenesissupporting

confidence: 83%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Biogenesis of Multilamellar Bodies via Autophagy

Hariri

Millane

Guimond

et al. 2000

MBoC

162

142

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show abstract

“…Surfactant is released to the alveolar space by exocytosis from intracellular storage organelles termed lamellar bodies which contain the majority of the components of the surfactant. During active secretion of contents from the lamellar bodies to the alveoli and during the surfactant recycling process, a variety of hydrolases have been related to these organelles (de Vries et al, 1985;DiAugustine, 1974;Edelson et al, 1988;Gilder et al, 1981;Hook & Gilmore, 1982;S.L. Young et al, 1993), many of which have lysosomal-type degradative functions.…”

Section: Alveolar Epithelial Cellsmentioning

confidence: 99%