Granulocytic differentiation of HL-60 cells is associated with increase of poly-N-acetyllactosamine in Asn-linked oligosaccharides attached to human lysosomal membrane glycoproteins

Lee, N; Wang, W C; Fukuda, Minoru

doi:10.1016/s0021-9258(17)30529-x

Cited by 113 publications

(6 citation statements)

References 61 publications

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“…Third, HT-29 ceils, which also express sialyl Le x, do not interact at all with P-selectin (Zhou et al, 1991). Finally, several neutrophil membrane proteins known to carry the sialyl Le x structure (Lee et al, 1990;Picker et al, 1991b;Asada et al, 1991;Fukuda et al, 1984), are distinct from the major glycoprotein ligand we have identified and do not bind P-selectin in the assays described here. These observations suggest that the ligand we have identified contains structural features in addition to the sialyl Le x tetrasaccharide that enhance the affinity and/or specificity of its interaction with P-selectin.…”

Section: Discussionmentioning

confidence: 70%

“…The first two molecules, lamp-1 and lamp-2, are abundant neutrophil proteins that are predominantly localized in lysosomal membranes but are also expressed in small amounts on the cell surface. These proteins have a large number of complex N-linked glycan chains (Fukuda et al, 1988;Carlsson et al, 1988;Carlsson and Fukuda, 1990), many of which carry the sialyl Le x tetrasaccharide (Lee et al, 1990). Polyclonal antisera (1:5 dilution) and mAbs (40/zg/ml) to lamp-1 (CD3) and lamp-2 (BB6) had no effect on binding of P-selectin to neutrophils as assessed by flow cytometry (data not shown).…”

Section: Comparison Of the P-selectin Ligand With Known Neutrophil Membrane Proteinsmentioning

confidence: 94%

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Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells.

Moore

Stults

Díaz

et al. 1992

The Journal of Cell Biology

485

330

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Abstract. P-selectin (CD62, GMP-140, PADGEM), a Ca2+-dependent lectin on activated platelets and endothelium, functions as a receptor for myeloid cells by interacting with sialylated, fucosylated lactosaminoglycans. P-selectin binds to a limited number of proteasesensitive sites on myeloid cells, but the protein(s) that carry the glycans recognized by P-selectin are unknown. Blotting of neutrophil or HL-60 cell membrane extracts with [m25I]P-selectin and affinity chromatography of [3H]glucosamine-labeled HL-60 cell extracts were used to identify P-selectin ligands. A major ligand was identified with an =250,000 Mr under nonreducing conditions and =120,000 under reducing conditions. Binding of P-selectin to the ligand was Ca 2 § dependent and was blocked by mAbs to P-selectin. Brief sialidase digestion of the ligand increased its apparent molecular weight; however, prolonged digestion abolished binding of P-selectin. Peptide:N-glycosidase F treatment reduced the apparent molecular weight of the ligand by =3,000 but did not affect P-selectin binding. Western blot and immunodepletion experiments indicated that the ligand was not lamp-I, lamp-2, or L-selectin, which carry sialyl Le ~, nor was it leukosialin, a heavily sialylated glycoprotein of similar molecular weight. The preferential interaction of the ligand with P-selectin suggests that it may play a role in adhesion of myeloid cells to activated platelets and endothelial cells.

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Section: Discussionmentioning

confidence: 70%

Section: Comparison Of the P-selectin Ligand With Known Neutrophil Membrane Proteinsmentioning

confidence: 94%

Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells.

Moore

Stults

Díaz

et al. 1992

The Journal of Cell Biology

485

330

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“…We recently described a glycoprotein, ISG 100 [8], of the FP-endocytic pathway in T. brucei that appears to contain a single extensive N-linked glycan (~50% by weight). Many lysosomal membrane glycoproteins (LAMPs) from higher eukaryotes have N-linked glycans that contain linear repeats of N-acetyllactosamine (Galβ1 → 4GlcNAcβ1 → 3) n [9]. These can be identified either using tomato lectin (TL), which binds with high affinity only when three or more linear disaccharide repeats are present [10], or by digestion with endo-β-galactosidase [11].…”

Section: Resultsmentioning

confidence: 99%

N-linked glycans containing linear poly-N-acetyllactosamine as sorting signals in endocytosis in Trypanosoma brucei

1999

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African trypanosomes, such as Trypanosoma brucei, are protozoan parasites that are transmitted by the tsetse fly and cause sleeping sickness in humans and Nagana in cattle. Trypanosomes evade the immune responses of their hosts by varying their surface coat protein (VSG) and restricting exocytosis and endocytosis to an invagination of the plasma membrane called the flagellar pocket (FP). The FP represents only 0.5% of the cellular surface but membrane turnover here occurs at high rates [1] [2] [3]. No model has yet been proposed to account for the sequestration of membrane proteins and the rate of membrane turnover that occur in the FP. Recent data have suggested that glycans are involved in the sorting of membrane proteins in polarized cells [4] [5] [6] [7]. Here, we show that N-linked glycans containing linear poly-N-acetyllactosamine (pNAL) are only associated with proteins of the FP/endocytic pathway in T. brucei and are present only in bloodstream forms of the parasite. These glycoproteins bind to tomato lectin (TL), a property that allowed their single-step isolation. Chito-oligosaccharides that compete specifically for pNAL binding to TL also inhibited receptor-mediated uptake of several ligands. These results suggest a model in which N-linked linear pNAL acts as a sorting signal for endocytosis in trypanosomes.

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“…Many recent reports on the biogenesis of lysosomes have suggested a wide variety of functions of lysosomal integral membrane proteins, such as maintenance of the acidic milieu, transport of amino acids, fatty acids, and carbohydrates, and protection from lysosomal enzymes (55) . The presence of a highly glycosylated region of these molecules at the luminal side of the lysosome can possibly protect the delimiting membrane against degradation by lysosomal enzymes (57). Granule exocytosis would result in the exposure of lamp-1,-2 and CD63 at the CTL plasma membrane and, therefore, may also serve to protect the effector cell from released soluble granule proteins.…”

mentioning

confidence: 99%

Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes.

Peters

Borst

Oorschot

et al. 1991

The Journal of Experimental Medicine

Self Cite

616

439

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SummaryCytotoxic T lymphocytes (CTL) contain granules that are exocytosed during specific interaction with target cells (TC). In this process, the granule contents, including the lethal protein perforin, as well as granzymes, a family of serine esterases, are delivered to the TC . Information regarding the routing of these proteins towards the granule and their exact localization within the granule is of primary importance to resolve the mechanism of granule-mediated TC killing . In this study, the subcellular localization of perforin, granzymes, and known endosomal and lysosomal marker proteins was determined in human and murine CTL, by immunogold labeling of ultrathin cryosections followed by electron microscopy. Perforin and granzymes can be detected in rough endoplasmic reticulum, Golgi complex, trans-Golgi reticulum, and in all cytotoxic granules . Within the granules, they have a similar distribution and are localized not only in the so-called dense core but also over the region containing small internal vesicles. This finding implies that perforin and granzymes can be released in membrane-enveloped and/or -associated form into the intercellular cleft formed upon CTUTC interaction . On the basis of the present evidence, additional release of these molecules in soluble form cannot be excluded . The lysosomal membrane glycoproteins lamp-1, lamp-2, and CD63, are abundantly present on the granule-delimiting outer membrane, which becomes incorporated into the CTL plasma membrane during lethal hit delivery. In contrast, the cation-independent mannose 6-phosphate receptor, known to be present in endosomes and absent from lysosomes, is found only in a minority of the granules. Together with our previous findings that the granules are acidic and connected to the endocytic pathway, these observations define CTL granules as secretory lysosomes.

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Granulocytic differentiation of HL-60 cells is associated with increase of poly-N-acetyllactosamine in Asn-linked oligosaccharides attached to human lysosomal membrane glycoproteins

Cited by 113 publications

References 61 publications

Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells.

Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells.

N-linked glycans containing linear poly-N-acetyllactosamine as sorting signals in endocytosis in Trypanosoma brucei

Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes.

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