0000000000277375
AUTHOR
P. Vaith
Aggregation of sponge cells. Isolation and characterization of an inhibitor of aggregation receptor from the cell surface.
From the cell membranes of the sponge Geodia cydonium a component was isolated and purified which inhibits the aggregation factor isolated from the same source; the component was termed anti-aggregation receptor. This molecule was characterized as a glycoprotein (54% neutral carbohydrate) and its molecular weight is in the range of 180,000 One biological site of the anti-aggregation receptor was determined to be D-galactose. Indirect evidence presented seems to indicate that this molecule is present in an active form in aggregation-deficient cells and absent in aggregation-susceptible cells.
On the role of D-glucuronic acid in the aggregation of cells from the marine sponge Geodia cydonium.
Abstract The aggregation receptor (AR) from the marine sponge GEODIA CYDONIUM was analyzed with respect to its monosaccharide composition. Three major sugars ( D -galactose, D -glucose and D -glucuronic acid) accounted for about 85 % of the total carbohydrate. Negative results with different lectins directed against D -galactosyl, N -acetyl- D -galactosaminyl and N -acetyl- D -glucosaminyl groups, respectively, showed that these sugars are serologically unreactive in AR. Positive serological reactions were obtained with CONCANAVALIN A and LIMULUS POLYPHEMUS agglutinin. AR also reacted strongly with the basic polymer poly- L -lysine. Reaggregation experiments performed on the basis of these …
Sponge aggregation factor and sponge hemagglutinin: possible relationships between two different molecules.
Abstract A lectin from the marine sponge GEODIA CYDONIUM was isolated and characterized. GEODIA lectin (GL) agglutinates human red blood cells irrespective of the ABO blood group and precipitates with a variety of D -galactose containing glycosubstances, i.e. certain snail galactans, bovine erythrocyte glycoprotein and PNEUMOCOCCUS type XIV polysaccharide. The only simple sugars inhibiting the GL-mediated hemagglutination were lactose and n -acetyl- D -galactosamine. GL was purified by affinity chromatography on Sepharose 4B almost to homogeneity as tested by polyacrylamide disc gel electrophoresis. Positive staining of the lectin band with Coomassie brilliant blue and PAS suggest that GL i…
Identification and properties of the cell membrane bound leucine aminopeptidase interacting with the potential immunostimulant and chemotherapeutic agent bestatin.
Bestatin was found to be a competitive inhibitor (with respect to the Leu-NA substrate) not only of the isolated microsomal and cytosolic leucine aminopeptidases (Leu-APm and Leu-APc) but also of the aminopeptidases (APs) present in membrane preparations (from mouse liver) and on the cell surface of L5178Y cells. Kinetic parameters indicate that cellular AP is identical to Leu-APm. To rule out the possibility that AP-B is involved in the inhibition reactions, comparable studies with amastatin were performed. Electrophoretical studies revealed the solubilized cell membrane bound AP to co-migrate with Leu-APm in polyacrylamide gels. The activity of the separated membrane AP was inhibited by b…