Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023418 (leukemia)
93,477 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The glycosidases, enzymes which participate in the degradation of glycoproteins and glycolipids inside the lysosomes are themselves glycoproteins and, for one enzyme, several forms may be isolated in tissues and in biological fluids, corresponding to variations in the composition or the structure of their glycanic moiety. We have previously studied the different forms of alpha-L-fucosidase in human serum, kidney and urine. Some modifications of the glycanic fraction of glycoproteins have been described in various forms of tumoral cells; therefore, we have attempted to verify if the alpha-L-fucosidase of blood cells might be a useful marker in the diagnosis of leukemias, using the enzymic pattern obtained by chromatographic or electrofocusing methods. Detergent extracts from normal lymphocytes, submitted to ion-exchange chromatography as well as to chromatofocusing, revealed the presence of two forms of alpha-L-fucosidase, A and B, with respective pIs of 5.7 and 6.2. After treatment by neuraminidase, these two forms remain distinct, showing that the degrees of sialylation is not the only difference. Moreover, after desialylation, the two forms have not the same affinity for concanavalin A, an argument for the heterogeneity of the glycanic structures. The determination of the total activity, and of enzymic patterns of alpha-L-fucosidase from leukemic cells led to the observation of three types of modifications, in comparison with normal lymphocytes: quantitative variations in the total activity; variations in the proportions of the two forms; variations due to the modification of pIs. We have studied the lymphocytes from four patients with a hairy-cell leukemia (HCL), four patients with chronic lymphoid leukemia (CLL) and the MO cell-line, proceeding from a HCL. In all cases, the total fucosidase activity is strongly decreased in comparison with normal lymphocytes activity. The chromatofocusing pattern for CLL cells reveals the presence of the A and B forms, without modification of their eluting pH. A characteristic pattern is obtained with hairy cells, presenting only the B form, eluted in more acidic conditions. The normal lymphocytes in peripheral blood are for 80 per cent of the T phenotype, and the CLL lymphocytes exhibit the phenotypic markers B, as well as the hairy cells, but the MO cell-line acquires in culture the T markers. As these last cells express both the A and B forms of enzyme, the absence of the A form of alpha-L-fucosidase seems to be a marker of the HCL.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:[Alpha-L-fucosidase of normal and pathological blood cells]. 186 62

alpha-L-Fucosidase isoenzymes pattern in hairy cell leukaemia (HCL) is characterized by the disappearance of the more acidic form when compared to normal lymphocytes. Our data seem to indicate that this profile could not be related to the T or B phenotype because in normal lymphocytes (mainly T), MO cells possessing T markers, as well as lymphocytes from chronic lymphoid leukaemia (CLL) known to exhibit normal-like B phenotypes two alpha-L-fucosidase forms are identified and especially the more acidic one.
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PMID:Alpha-L-fucosidase isoenzyme pattern in hairy cell leukaemia. 233 87

A new common region of virus integration, Evi11, has been identified in two retrovirally induced murine myeloid leukemia cell lines, NFS107 and NFS78. By interspecific backcross analysis, it was shown that Evi11 is located at the distal end of mouse chromosome 4, in a region that shows homology with human 1p36. The genes encoding the peripheral cannabinoid receptor (Cnr2) and alpha-L-fucosidase (Fuca1) were identified near the integration site by using a novel exon trapping system. Cnr2 is suggested to be the target gene for viral interference in Evi11, since proviruses are integrated in the first intron of Cnr2 and retroviral integrations alter mRNA expression of Cnr2 in NFS107 and NFS78. In addition, proviral integrations were demonstrated within the 3' untranslated region of Cnr2 in five independent newly derived CasBrM-MuLV (mouse murine leukemia virus) tumors, CSL13, CSL14, CSL16, CSL27, and CSL97. The Cnr2 gene encodes a seven-transmembrane G-protein-coupled receptor which is normally expressed in hematopoietic tissues. Our data suggest that the peripheral cannabinoid receptor gene might be involved in leukemogenesis as a result of aberrant expression of Cnr2 due to retroviral integration in Evi11.
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PMID:The genes encoding the peripheral cannabinoid receptor and alpha-L-fucosidase are located near a newly identified common virus integration site, Evi11. 926 4