Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.6.1 (
sulfatase
)
3,205
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Variable constitutional mosaicism, mos45,XY,-22/46,XY,-22,+mar/46,XY,-22,+r(22)/47,XY,-22,+r(22)+mar/ 47, XY,-22,+r(22)*2, was found in
PHA
-stimulated peripheral blood, in a lymphoblastoid cell line and in cultured skin fibroblasts from a mentally retarded patient with neurofibromatosis. Both the ring chromosome and the small extra marker chromosome stained positively by in situ hybridization with a chromosome 14/22-specific alphoid repeat probe. DNA dosage analysis showed constitutional loss of one copy of the
arylsulfatase A
gene (ARSA), consistent with its terminal location on 22q. There was no evidence of constitutional loss of D22S1 or D22S28 which flank the neurofibromatosis type 2 (NF2) locus. Analysis of two DNA samples from a skin neurofibroma indicated retainment of two copies of D22S1, whereas the results were ambiguous with respect to tumor-specific loss of one copy of D22S28. It is suggested that the development of neurofibromatosis of unclear type in two r(22) carriers might be associated with somatic mutation of the NF2 locus due to instability of the ring chromosome(s), and in analogy, that somatic mutation of either NF1 or NF2 may account for some cases of neurofibromatosis which do not meet the criteria of either NF1 or NF2. The occurrence of seminoma in the proband may be fortuitous, but could also be due to the presence of a seminoma-associated locus on chromosome 22.
...
PMID:Ring chromosome 22 and neurofibromatosis. 142 40
It has been shown that the concentration of
arylsulfatase A
increases in the body fluids of patients with some forms of cancer and the carbohydrate component of
arylsulfatase A
synthesized in tumor tissues and transformed cells undergoes increased sialylation, phosphorylation and sulfation. The specificity of changes in the glycosylation of glycoproteins in cancer is still unknown. To understand the significance of any changes in glycosylation of
arylsulfatase A
in cancer, it is important to know the structure of its carbohydrate component in normal tissue. Here, carbohydrate moieties of human placental
arylsulfatase A
were studied by sequential lectin affinity chromatography after enzymatic cleavage and labelling with tritiated sodium borohydride. Labelled oligosaccharides were subjected to ion exchange chromatography. The uncharged fraction and the neuraminidase treated charged fraction were further analysed using the lectins: Concanavalin A (Con A), Ricinus communis (RCA I), Triticum vulgaris (L-
PHA
) and Aleuria aurantia (AAL). The results indicated that 97% of the
arylsulfatase A
oligosaccharides were low molecular weight high mannose type glycans possessing up to 5 mannose residues. This was supported by the approximately 2.4 kDa decrease in the molecular weight of
arylsulfatase
. A subunits upon complete peptide N-glycosidase F deglycosylation, as shown using SDS-PAGE. The remaining 3% of the
arylsulfatase A
oligosaccharides were of the high mannose type, possessing more than 5 mannose residues. Most (97.5%) of the glycans were uncharged, while 2.5% were charged. Neuraminidase treatment of the latter did not remove the charge, suggesting the presence of phosphate or sulfate residues. This study, of
arylsulfatase A
oligosaccharides separated from the protein part, shows that all glycans of the enzyme from human placenta are of the high mannose type.
...
PMID:Arylsulfatase A from human placenta possesses only high mannose-type glycans. 920 26
