scholarly journals Cellular localization of neuraminidases in cultured human fibroblasts

1981 ◽  
Vol 198 (3) ◽  
pp. 505-508 ◽  
Author(s):  
M Zeigler ◽  
G Bach

The cellular localization of glycoprotein and ganglioside sialidases in normal and I-cell-disease cultured fibroblasts has been investigated. Cellular organelles have been separated on a colloidal silica gradient. The subcellular distribution of these enzymes indicated that the glycoprotein sialidase is mainly a lysosomal hydrolase, whereas the ganglioside sialidase is primarily located in the plasma membranes. The latter isoenzymes is tightly bound to these membranes and thus could not be extracted by homogenization in the presence of Triton X-100. The interpretation of this finding and its relation to the pathochemistry of sialidase-deficient disorders is discussed.

1987 ◽  
Vol 248 (2) ◽  
pp. 345-350 ◽  
Author(s):  
G Lorkowski ◽  
J E Zijderhand-Bleekemolen ◽  
E G Erdös ◽  
K von Figura ◽  
A Hasilik

The biosynthesis, glycosylation and subcellular localization of the neutral endopeptidase-24.11 were studied in cultured human fibroblasts. The enzyme was synthesized as a precursor (Mr 88,000) containing four or five N-linked oligosaccharides. Within 1 h the synthesis-mature (Mr 94,000) endopeptidase-24.11 was formed and contained sialylated oligosaccharides. The half-life of endopeptidase-24.11 was 3.7 days and in the presence of 10 mM-NH4Cl it increased to 6 days. Mature endopeptidase-24.11 was solubilized with 0.2% saponin and partitioned into Triton X-114. In intact fibroblasts, endopeptidase-24.11 was accessible to antibodies and to neuraminidase even when the treatment was performed at 4 degrees C. The localization of endopeptidase-24.11 to the plasma membrane in cultured fibroblasts was further demonstrated by immunocytochemistry.


1981 ◽  
Vol 240 (6) ◽  
pp. E645-E648
Author(s):  
F. Ishibashi ◽  
P. H. Bennett ◽  
B. V. Howard

The site of action of alloxan on glucose metabolism has been investigated using cultured human fibroblasts. Analysis of cell extracts after cell monolayers were exposed to D-[U-14C]glucose indicated that the initial stimulation of glucose incorporation by alloxan was observed primarily in the nucleotide fraction (ribose) with inhibition of lactate production. The subsequent inhibition of glucose incorporation was observed in the nucleotide fraction. Assay of 14CO2 production indicated that alloxan enhanced 14CO2 formation from D-[U-14C]glucose for approximately 10 min, followed by inhibition. To probe the site of alloxan action, rates of 14CO2 formation from 1- and 6-position labeled [14C]glucose, and [U-14C]pyruvate were compared. The initial stimulation was observed mainly in D-[1–14C]glucose oxidation, whereas inhibition was measurable with the 6-position tracer and [14C]pyruvate. The results suggest that alloxan initially stimulates the pentose-monophosphate shunt and then subsequently inhibits both the pentose-monophosphate shunt and tricarboxylic acid pathways.


1988 ◽  
Vol 263 (26) ◽  
pp. 12886-12892 ◽  
Author(s):  
H Greve ◽  
Z Cully ◽  
P Blumberg ◽  
H Kresse

1987 ◽  
Vol 262 (36) ◽  
pp. 17412-17419 ◽  
Author(s):  
W B Rizzo ◽  
D A Craft ◽  
A L Dammann ◽  
M W Phillips

1971 ◽  
Vol 42 (2) ◽  
pp. 340-345 ◽  
Author(s):  
Reuben Matalon ◽  
J.A. Cifonelli ◽  
Albert Dorfman

1980 ◽  
Vol 255 (3) ◽  
pp. 929-936 ◽  
Author(s):  
G.C. Gazzola ◽  
V. Dall'Asta ◽  
G.G. Guidotti

1974 ◽  
Vol 249 (11) ◽  
pp. 3430-3435
Author(s):  
Richard E. Hillman ◽  
Elaine F. Otto

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