Glycosyltransferase activities in leukemic cells from patients and human leukemic cell lines

Rossowski, W; Srivastava, B. I. Sahai

doi:10.1016/0277-5379(93)90013-u

Cited by 10 publications

(2 citation statements)

References 18 publications

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“…Since the α6-sialyltransferase (N) and sialyl-Le x occur in inversely related levels, the α6-sialyltransferase may prevent and control the synthesis of selectin ligands [Skacel et al, 1991]. The isotype and levels of sialyltransferases and other glycosyltransferases appear to be characteristic of the cell type, and enzyme profiles may be useful in determining the cell type or in distinguishing between normal and leukemia cells [Rossowsky and Srivastava, 1983;Suda et al, 1987].…”

Section: Glycoproteins Of Leukemia Cellsmentioning

confidence: 99%

Glycoproteins and Their Relationship to Human Disease

Brockhausen

Schutzbach

Kuhns

1998

Cells Tissues Organs

169

105

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Glycoproteins are proteins that carry N- and O-glycosidically-linked carbohydrate chains of complex structures and functions. N-glycan chains are assembled in the endoplasmic reticulum and the Golgi by a controlled sequence of glycosyltransferase and glycosidase processing reactions involving dolichol intermediates. The assembly of O-glycans occurs in the Golgi and does not involve dolichol. For most reactions, families of glycosyltransferases exist; the expression of the individual enzymes within a family is often subject to complex regulation. The biosynthesis of N- and O-glycan is controlled at the level of gene expression, mRNA, enzyme protein activity and localization, and through substrate and cofactor concentrations at the site of synthesis. This complex regulation results in many hundreds of structures, the range of which varies in different species, cell types, tissue types, states of development and differentiation. In diseased cells, the relative proportions of these structures are often characteristically different from normal, and may be useful for the assessment of the stage of the disease and for diagnosis. Knowledge of disease-specific glycoprotein structures and their functions may be used therapeutically, in immunotherapy, in blocking cell adhesion or interfering with other binding or biological processes. Recently, some of the mechanisms underlying glycoprotein alterations in disease have been elucidated. This opens the possibility of an active interference in the disease process. The functions of glycans in diseased cells will become more clear with the tools of molecular biology and transgenic animal models.

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Section: Glycoproteins Of Leukemia Cellsmentioning

confidence: 99%

Glycoproteins and Their Relationship to Human Disease

Brockhausen

Schutzbach

Kuhns

1998

Cells Tissues Organs

169

105

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“…While there are no other reports in the literature regarding protein fucosylation and canine lymphoma, increased fucosyltransferase activity and changes in fucosylated glycopeptides have been documented in leukaemic B‐cell lines and non‐Hodgkin’s lymphoma in humans. In these reports, plasma fucosyltransferases have been shown to be elevated in human leukaemic B‐cell lines 20 and in plasma from patients with non‐Hodgkin’s lymphoma 21 . Additionally, biosynthesis of fucosylated peptides in acute‐leukaemic lymphoblasts has been observed to be an inherent characteristic of that malignant cell type 22 …”

Section: Introductionmentioning

confidence: 98%

Glycoproteomic profiling of serum peptides in canine lymphoma and transitional cell carcinoma

Wilson

Regnier

Knapp

et al. 2008

Vet Comparative Oncology

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Differential expression of fucosylated glycoproteins has been correlated with malignancy and metastatic potential in various types of neoplasia. Utilizing glycoproteomics techniques, changes in fucosylated serum peptides associated with naturally occurring canine lymphoma and transitional cell carcinoma (TCC) have been evaluated. In both types of neoplasia, the majority of the fucosylated peptides that changed increased with the cancer. In one lymphoma case that was examined over the course of the disease, the same fucosylated peptides that increased during pre-chemotherapy decreased during post-chemotherapy, and then subsequently increased upon recurrence of the lymphoma. When comparing all the fucosylated peptides that increased in both types of cancer, there were only two peptides in common allowing discrimination between lymphoma and TCC based on their peptide profiles. These results emphasize the prospect of glycopeptide profiling in proteomics for use in discovering a panel of non-invasive, diagnostic or prognostic biomarkers of cancer.

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Glycosylation in Leukemia and Blood-Related Disorders

Brockhausen

Kuhns

1997

Glycoproteins and Human Disease

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Glycosyltransferase activities in leukemic cells from patients and human leukemic cell lines

Cited by 10 publications

References 18 publications

Glycoproteins and Their Relationship to Human Disease

Glycoproteins and Their Relationship to Human Disease

Glycoproteomic profiling of serum peptides in canine lymphoma and transitional cell carcinoma

Glycosylation in Leukemia and Blood-Related Disorders

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