Transient versus permanent expression of cancer-related glycopeptides on normal versus leukemic myeloid cells coinciding with marrow egress

Beek, Wim Van; Tulp, A.; Bolscher, Jan G. M.; Blanken, G; Roozendaal, K. J.; Egbers, M

doi:10.1182/blood.v63.1.170.170

Cited by 30 publications

(3 citation statements)

References 38 publications

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“…Every 2 h, 5 mg of pronase per ml of lysate was added and this was repeated six times. Digested material was dialyzed (pore size of dialysis membranes 800 D) and samples were analyzed on a Mono Q column coupled to fast protein liquid chromatography (FPLC) equipment (LKB Instruments, Inc., Gaithersberg, MD) as described (28). The radioactivity in the samples was determined by liquid spectrometry.…”

Section: Labeling and A Nalysis Of Total N-linked Carbohydratesmentioning

confidence: 99%

“…Lysates were prepared and digested with pronase. Samples were analyzed through a Mono Q column as described (28), resulting in the separation of charged (complex) sialylated and noncharged (high-mannose) carbohydrates. 2-[3H]-D-mannose cannot be subjected to epimerization into other sugars without losing its label and mannose is only incorporated into N-linked carbohydrates.…”

Section: Recycling Of Bulk N-linked Glycoproteins Along the Er/cis-golgimentioning

confidence: 99%

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Recycling glycoproteins do not return to the cis-Golgi.

Neefjes

Verkerk

Broxterman

et al. 1988

The Journal of Cell Biology

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Abstract. Recycling of a number of glycoproteins along the site of action of mannosidase I (the distal endoplasmic reticulum/cis-Golgi) was followed in several different cell lines. Treatment of cells with 1-deoxymannojirimycin (dMM) produced high mannose oligosaccharides at positions otherwise occupied by complex-type oligosaccharides in these glycoproteins. Conversion of high-mannose-type oligosaccharides to complex oligosaccharides of proteins initially synthesized in the presence of dMM was used as a marker for recycling of glycoproteins along the site of action of dMM. In contrast to findings reported by Snider and Rogers (Snider, M. D., and O. C. Rogers. 1986. J. Cell Biol. 103:265-275), removal of dMM did not result in reconversion of high-mannose oligosaccharides to complex-type sugars, even after prolonged periods of culture. We conclude that surface glycoproteins do not recycle through the cis-medial Golgi elements.NDOCYTOSIS of surface receptors is one of the mechanisms by which the cell controls uptake of nutrients, and levels of surface receptors. Any stimulus delivered by hormones or growth factors may likewise be dependent on, or modulated by receptor-mediated endocytosis (7,8). The endocytotic pathway has been unraveled in considerable detail morphologically and biochemically (17,26). Far less is known about the route taken by recycling receptors on their way back to the cell surface, because it is difficult to discriminate between newly synthesized receptors that are on their way to the plasma membrane, and recycling receptors that were already resident at the cell surface.In principle, the exocytotic aspect of the recycling pathway can be studied, provided the following conditions can be fulfilled. Receptors resident at the cell surface need to be tagged specifically; the label used should not perturb the recycling process per se; traversing a particular subcellular compartment should produce a detectable change in the tagged receptor. Lactoperoxidase-catalyzed iodination of surface receptors in conjunction with neuraminidase digestion has been used to produce labeled, desialylated surface molecules that can report on traffic through the trans-Golgi (22). Under these circumstances, acquisition of sialic acid(s) is interpreted as indicative of traversal through the transGolgi network.A second approach is to use modifications of N-linked glycans as produced by oligosaccharide-trimming inhibitors (6). Use of the mannosidase I inhibitor 1-deoxymannojirimycin (dMM) ~ results in retention of high-mannose oligo-1. Abbreviations used in this paper: dMM, 1-deoxymannojirimycin; Endo H, endoglycosidase H; ER, endoplasmic reticulum; FPLC, fast protein liquid chromatography; NANAse, neuraminidase; Tf, transferrin; Tfr, transferrin receptor; Tfr ~mm, transferrin receptor synthesized in the presence of dMM.saccharides for those glycans normally converted to the complex type (5). In a pulse-chase experiment, surface receptors carrying high-mannose glycans as a consequence of treatment with dMM can be delivere...

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Section: Labeling and A Nalysis Of Total N-linked Carbohydratesmentioning

confidence: 99%

Section: Recycling Of Bulk N-linked Glycoproteins Along the Er/cis-golgimentioning

confidence: 99%

Recycling glycoproteins do not return to the cis-Golgi.

Neefjes

Verkerk

Broxterman

et al. 1988

The Journal of Cell Biology

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“…Van Beek, Tulp and Bolscher (1984) reported that the increased adhesion of AML and endothelial cells was induced by the aberrant expression of adhesion molecules on the surface of AML and HUVECs. Our study showed that, after exposure to the supernatant of hyperleukocytic AML blasts for 24 h, endothelial cell surface ICAM‐1 expression was significantly increased compared with that of nonhyperleukocytic AML blast supernatant.…”

Section: Discussionmentioning

confidence: 99%

Effect of ICAM-1 and LFA-1 in hyperleukocytic acute myeloid leukaemia

Zhang

Fan

et al. 2006

Clin Lab Haematol

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Acute hyperleukocytic leukemia [AHL; WBC count >100 x 10(9)/l] is associated with a life-threatening complication. The mechanisms of hyperleukocytosis in acute myeloid leukaemia (AML) remain unclear. However, the interaction of intercellular adhesion molecule-1 (ICAM-1) and lymphocyte function-associated antigen-1 (LFA-1) plays an important role in the adhesion and migration of normal leukocytes and AML cells. Therefore, effects of ICAM-1 and LFA-1 were studied in hyperleukocytic AML. The adhesion of hyperleukocytic AML blasts and human umbilical vein endothelial cells (HUVECs) was significantly increased compared with that of blasts from non-hyperleukocytic AML (WBC < 100 x 10(9)/l). The adhesion of normal neutrophils and HUVECs treated with hyperleukocytic AML blast supernatant was increased significantly. Finally, we determined the ICAM-1 on the surface of HUVECs treated with the supernatant of hyperleukocytic AML blasts and LFA-1 on hyperleukocytic AML blasts by flow cytometry. It showed that the ICAM-1 expression on the surface of the HUVECs treated with hyperleukocytic AML blast supernatant for 24 h could be increased, and the expression of LFA-1 on hyperleukocytic AML was also increased significantly. Our data show that hyperleukocytic AML blasts stimulate the endothelium to secrete more ICAM-1 and promote their own adhesion to vascular endothelium, suggesting that ICAM-1 and LFA-1 may have a role in hyperleukocytic AML.

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Transfection by human oncogenes: Concomitant induction of tumorigenicity and tumor‐associated membrane alterations

Collard

Beek

Janssen

et al. 1985

Intl Journal of Cancer

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NIH 3T3 cells were transfected with DNA derived from human bladder carcinoma, colon carcinoma and HL60 promyelocytic leukemia cells. The transfectants were examined for the presence of human oncogenes in relation to tumorigenic potential and composition of surface-located fucosyl glycopeptides by gel filtration, Concanavalin-A-binding and high-performance liquid chromatography. All transfectants, harboring 3 different human cellular ras genes, appeared to be tumorigenic in nude mice and displayed characteristically altered glycopeptides. The surface glycopeptides were consistently changed to higher apparent molecular weight due to enrichment in higher-branched sialic-acid-containing glycopeptides. Similar alterations have been found previously in virally- and chemically-transformed cells in vitro and tumors raised in vivo, and were designated as cancer-related or tumor-associated glycopeptides. Revertants derived from HL60-DNA-induced transfectants, which had lost the transfected human N-ras oncogene, simultaneously lost their tumorigenic potential and expression of cancer-related membrane glycopeptides. In addition, spontaneous transformants, exhibiting morphology and growth patterns indistinguishable from those of tumor-DNA-induced transfectants, neither contained transferred human DNA sequences nor expressed cancer-related glycopeptides. Nevertheless these cells were capable, after prolonged latency periods, of inducing tumors in nude mice. Cells derived from such tumors constantly displayed cancer-related glycopeptides on their surface, suggesting selection of tumorigenic cells from spontaneous transformants during passage in nude mice. In one of these tumors at least, an endogenous mouse ras-gene appeared to be activated. The results indicate a close correlation between the presence of activated ras-oncogenes in the genome of the transfected cells, the tumorigenic potential of these cells and the expression of surface-located cancer-related glycopeptides. The data suggest that functions provided by human ras-oncogenes contribute to the alteration of membrane glycopeptides on tumor cells.

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Transient versus permanent expression of cancer-related glycopeptides on normal versus leukemic myeloid cells coinciding with marrow egress

Cited by 30 publications

References 38 publications

Recycling glycoproteins do not return to the cis-Golgi.

Recycling glycoproteins do not return to the cis-Golgi.

Effect of ICAM-1 and LFA-1 in hyperleukocytic acute myeloid leukaemia

Transfection by human oncogenes: Concomitant induction of tumorigenicity and tumor‐associated membrane alterations

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