scholarly journals Arylsulphatase A activity and sulphatide concentration in placenta, membranes and cord after delivery

2009 ◽  
Vol 37 (5) ◽  
Author(s):  
Ugo Indraccolo ◽  
Enea Traini ◽  
Emilia Baldoni ◽  
Salvatore Renato Indraccolo ◽  
Lucia Vitaioli
Keyword(s):  
Arylsulphatase A

ENZYMIC CHANGES IN THE CERVIX OF THE RAT AND HAMSTER DURING THE OESTROUS CYCLE AND THE EFFECT OF STEROIDS

1977 ◽  
Vol 72 (2) ◽  
pp. 153-161 ◽  
Author(s):  
ELIZABETH ZACHARIAH ◽  
N. R. MOUDGAL
Keyword(s):  
Alkaline Phosphatase ◽  
Specific Activity ◽  
Protein Biosynthesis ◽  
Hydrolytic Enzymes ◽  
Maximal Activity ◽  
Inhibitory Effect ◽  
Oestrous Cycle ◽  
Single Subcutaneous Injection ◽  
Arylsulphatase A ◽  
Phosphatase Alkaline

SUMMARY Changes in four hydrolytic enzymes, namely acid phosphatase, alkaline phosphatase, arylsulphatase A and B, of the cervix of the rat and hamster have been studied during the 4-day oestrous cycle. All four enzymes showed maximal activity on the day of oestrus and least activity on day 2 of dioestrus. All the enzymes showed significant reduction of activity after ovariectomy, arylsulphatase A and B showing the earliest changes in specific activity. A single subcutaneous injection of 0·02 μg oestradiol-17β/rat increased the specific activity of arylsulphatase A and B from the low ovariectomized level to that observed in control oestrous animals within 18 and 6 h respectively. A higher concentration of oestradiol-17β (2·0 μg) had an inhibitory effect. Progesterone was without effect on arylsulphatase B activity, but when given (2·0 mg) with 0·02 μg oestradiol-17β, it inhibited the response to oestrogen. Cycloheximide prevented the rise in arylsulphatase B activity occurring after oestrogen injection, suggesting a regulation of cervical arylsulphatase B at the level of protein biosynthesis. These results suggest that arylsulphatase B activity may be induced by oestrogen in the cervix of the rat.

Metachromatic leukodystrophy: a nonsense mutation (Q486X) in the arylsulphatase A (ARSA) gene

1994 ◽  
Vol 3 (1) ◽  
pp. 207-207 ◽  
Author(s):  
J. S. Harvey ◽  
W. F. Carey ◽  
P. V. Nelson ◽  
C. P. Morris
Keyword(s):  
Nonsense Mutation ◽  
Metachromatic Leukodystrophy ◽  
Arylsulphatase A

A Diagnostic Pointer to Adult Metachromatic Leucodystrophy

1980 ◽  
Vol 137 (2) ◽  
pp. 186-187 ◽  
Author(s):  
John A. O. Besson
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Autosomal Recessive ◽  
Demyelinating Disease ◽  
Initial Manifestation ◽  
The Central Nervous System ◽  
Metachromatic Leucodystrophy ◽  
Arylsulphatase A ◽  
Recessive Defect

Adult metachromatic leucodystrophy (MLD) is a rare demyelinating disease of the central nervous system caused by a genetic autosomal recessive defect and mediated through a deficiency in the enzyme arylsulphatase A (Peiffer, 1970). The initial manifestation may take the form of symptoms suggestive of schizophrenia or dementia (Sourander et al, 1962; Austin et al, 1968).

Searching for mutations in the arylsulphatase A gene

1994 ◽  
Vol 17 (3) ◽  
pp. 311-314 ◽  
Author(s):  
M. B. Salamon ◽  
E. Christensen ◽  
M. Schwartz
Keyword(s):  
Arylsulphatase A

scholarly journals The structural basis for the electrophoretic isoforms of normal and variant human platelet arylsulphatase A

1992 ◽  
Vol 287 (3) ◽  
pp. 979-983 ◽  
Author(s):  
R D Poretz ◽  
R S Yang ◽  
B Canas ◽  
H Lackland ◽  
S Stein ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Human Platelet ◽  
Normal Subjects ◽  
Exchange Chromatography ◽  
Structural Basis ◽  
Glycan Structure ◽  
Lectin Affinity Chromatography ◽  
Charge Heterogeneity ◽  
Arylsulphatase A ◽  
Polypeptide Structure

Human platelet arylsulphatase A (ASA) exhibits a multiple banding pattern when examined by PAGE. The isoform pattern (IVa) of the enzyme obtained from normal subjects differs from variants (IIIa, IIIb, IVb) which are primarily found in alcoholic patients. Alkaline phosphatase and endo-N-acetylglucosaminidase H treatments, as well as ion-exchange chromatography, demonstrate that the isoforms of ASA arise because of charge heterogeneity caused by phosphoglycan moieties. The isoform with the slowest mobility in PAGE lacks phosphate substituents. Based upon mannose-6-phosphate-receptor affinity chromatography it can be concluded that most, if not all, of the enzyme-linked phosphate is in the form of 6-O-phospho-D-mannosyl units. Lectin affinity chromatography and peptide-N-glycosidase F treatment followed by SDS/PAGE and Western-blot analysis indicate that normal platelet ASA contains two oligomannose and/or hybrid glycan moieties of which one, or both, possess a 6-O-L-fucosyl substituent on the asparagine-linked N-acetylglucosamine residue. Comparative analysis indicates that the variant IIIa and IIIb types of ASA differ from the IVa ASA with regard to the level of glycan phosphorylation and glycan structure, as well as the polypeptide structure.

scholarly journals Arylsulphatase A Pseudodeficiency (ARSA-PD), hypertension and chronic renal disease in Aboriginal Australians

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Dave Tang ◽  
Michaela Fakiola ◽  
Genevieve Syn ◽  
Denise Anderson ◽  
Heather J. Cordell ◽  
...  
Keyword(s):  
Renal Disease ◽  
Chronic Renal Disease ◽  
Aboriginal Australians ◽  
Arylsulphatase A

Arylsulphatase a and b in juvenile metachromatic leukodystrophy

1979 ◽  
Vol 95 (2) ◽  
pp. 255-261 ◽  
Author(s):  
Tuula Haltia ◽  
A. Icén ◽  
J. Palo
Keyword(s):  
Metachromatic Leukodystrophy ◽  
Arylsulphatase A

Presymptomatic diagnosis: Metachromatic eukodystrophy or pseudo arylsulphatase a deficiency?

1982 ◽  
Vol 5 (4) ◽  
pp. 215-217 ◽  
Author(s):  
H. Kihara ◽  
A. L. Fluharty ◽  
W. G. Ng ◽  
W. Leider
Keyword(s):  
Arylsulphatase A ◽  
Presymptomatic Diagnosis
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