Glycoproteins and glycolipids of oxyntic cell microsomes I. Glycoproteins: Carbohydrate composition, analytical and preparative fractionation

Beesley, Robert C.; Forte, John G.

doi:10.1016/0005-2736(73)90103-x

Cited by 22 publications

(7 citation statements)

References 42 publications

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“…Incubation of s.a. vesicles at pH 1.9 for 4 min resulted in a 77% loss of non-latent activity, but only 22% loss of latent activity. The role of the apical coat of glycosubstances (Forte & Forte, 1970;Beesley & Forte, 1973) as a putative protective mechanism is of particular interest, and the rso vesicles are an attractive model for the study of such mechanisms.…”

Section: Discussionmentioning

confidence: 99%

Redistribution and characterization of (H+ + K+)-ATPase membranes from resting and stimulated gastric parietal cells

Hirst¹,

Forte²

1985

Biochemical Journal

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When isolated from resting parietal cells, the majority of the (H+ + K+)-ATPase activity was recovered in the microsomal fraction. These microsomal vesicles demonstrated a low K+ permeability, such that the addition of valinomycin resulted in marked stimulation of (H+ + K+)-ATPase activity, and proton accumulation. When isolated from stimulated parietal cells, the (H+ + K+)-ATPase was redistributed to larger, denser vesicles: stimulation-associated (s.a.) vesicles. S.a. vesicles showed an increased K+ permeability, such that maximal (H+ + K+)-ATPase and proton accumulation activities were observed in low K+ concentrations and no enhancement of activities occurred on the addition of valinomycin. The change in subcellular distribution of (H+ + K+)-ATPase correlated with morphological changes observed with stimulation of parietal cells, the microsomes and s.a. vesicles derived from the intracellular tubulovesicles and the apical plasma membrane, respectively. Total (H+ + K+)-ATPase activity recoverable from stimulated gastric mucosa was 64% of that from resting tissue. Therefore, we tested for latent activity in s.a. vesicles. Permeabilization of s.a. vesicles with octyl glucoside increased (H+ + K+)-ATPase activity by greater than 2-fold. Latent (H+ + K+)-ATPase activity was resistant to highly tryptic conditions (which inactivated all activity in gastric microsomes). About 20% of the non-latent (H+ + K+)-ATPase activity was also resistant to trypsin digestion. We interpret these results as indicating that, of the s.a. vesicles, approx. 55% have a right-side-out orientation and are impermeable to ATP, 10% right-side-out and permeable to ATP, and 35% have an inside-out orientation.

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Section: Discussionmentioning

confidence: 99%

Redistribution and characterization of (H+ + K+)-ATPase membranes from resting and stimulated gastric parietal cells

Hirst¹,

Forte²

1985

Biochemical Journal

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“…The glycoproteins of the extracellular space have been carefully investigated, since they are easily available and occur in large amounts (I). Studies performed in recent years have also demonstrated that a large number of intracellular structures in various animal tissues, such as the gastric mucosa (2), small intestine (3), brain (4), kidney (5)+ platelets (6), fibroblasts (7), many solid tumors, and ascites tumor cells (8,9), contain glycoproteins. The nature of the association between the glycoproteins and these structures is not yet established; the main glycoprotein of the erythrocyte membrane appears to be an integral protein and bridges the membrane.…”

mentioning

confidence: 99%

Biogenesis of microsomal membrane glycoproteins in rat liver. I. Presence of glycoproteins in microsomes and cytosol.

Autuori¹,

Svensson²,

Dallner³

1975

The Journal of Cell Biology

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The glycoproteins of microsomes and cytosol were studied. Various washing procedures did not release the proteins from the microsomes, and immunological tests demonstrated that the sialoproteins are not serum components. Low concentrations of deoxycholate and incubation in 0.25 M sucrose solution liberated a small amount of microsomal sialoprotein and this fraction exhibited a high degree of labeling of protein-bound N-acetylneuraminic acid. A part of the glycoprotein fraction could not be solubilized, even with a high concentration of the detergent. Thoroughly perfused rat liver contained sialoproteins in the particle-free supernate. The level of sialoprotein present could not be due to contamination with serum or broken organelles. The high in vivo incorporation of [SH]glucosamine into protein-bound sialic acid of Golgi membranes and cytosol was paralleled by a delayed and lesser rate of incorporation into the rough and smooth microsomal membranes. This incorporation pattern suggests the possibility that the glycoproteins of cytosol and Golgi may later be incorporated into the membrane of the endoplasmic reticulum.

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“…Some of the structural features of the rabbit β-subunit oligosaccharides are present in other species. The complete absence of sialylation on the gastric β-subunit in rabbit, frog, and pig have previously been demonstrated (Beesley & Forte, 1973;Weitzhandler et al, 1993;Goldkorn et al, 1989). More recently, we have found that the Griffonia simplicifolia (GSI) lectins bind not only to the β-subunit from rabbit but also to that from frog and cow .…”

Section: Discussionmentioning

confidence: 78%

“…Digestion with Fucosidases. The presence of Fuc on the β-subunit has previously been shown by composition analysis (Beesley & Forte, 1973;Weitzhandler et al, 1993). We digested β-subunit oligosaccharides with the fucosidase from chicken liver which was found to be linkage nonspecific (Tyagarajan et al, 1996).…”

Section: Analysis Of the Oligosaccharides Of The Rabbit β-Subunitmentioning

confidence: 89%

“…Because the protein did not react with concanavalin A and was insensitive to Endo H, it was previously concluded that the β-subunit did not contain oligomannosidic chains (Okamoto et al, 1990;Hall et al, 1990). Monosaccharide analysis has demonstrated the presence of Man, Gal, GlcNAc, GalNAc, and Fuc but no NeuAc or NeuOGc (Beesley & Forte, 1973;Weitzhandler et al, 1993). It has been suggested that the oligosaccharides of the β-subunit may be sialylated during biosynthesis but lose sialic acid in the acidic environment of the stomach (Goldkorn et al, 1989).…”

mentioning

confidence: 99%

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The β-Subunit of the Rabbit H,K-ATPase: A Glycoprotein with All Terminal Lactosamine Units Capped with α-Linked Galactose Residues

1996

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The beta-subunit of the gastric H,K-ATPase is the most abundant glycoprotein in the tubulovesicular compartment of the acid-secreting parietal cells. The oligosaccharides of the beta-subunit have been shown to contain fucose, N-acetylglucosamine, mannose, galactose, and N-acetylgalactosamine. Previous studies have shown that the rabbit beta-subunit is devoid of N-acetylneuraminic acid. Here we report the structural features of the N-linked oligosaccharides of the beta-subunit from rabbit H,K-ATPase. We used glycosidase digestions and analysis by high-pH anion-exchange chromatography with pulsed amperometric detection and matrix-assisted laser desorption/ionization mass spectrometry to analyze the peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase (PNGase F)- and endo-beta-N-acetylglucosaminidase H (Endo H)-released oligosaccharides. The studies showed that the oligosaccharides of the beta-subunit are a mixture of both oligomannosidic and lactosamine-type structures. The high-mannose structures were identified as Man5Man8GlcNAc2 species. A striking finding was that all the branches of the lactosamine-type structures were terminated with Galalpha-->Galbeta-->GlcNAc extensions. All of the lactosamine-type structures were found to be core fucosylated and some of them contained one to three lactosamine repeats. We propose that a part of the adaptation of the gastric beta-subunit to the acidic environment of the stomach is through providing acid-stable terminal residues on the oligosaccharides.

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Glycoproteins and glycolipids of oxyntic cell microsomes I. Glycoproteins: Carbohydrate composition, analytical and preparative fractionation

Cited by 22 publications

References 42 publications

Redistribution and characterization of (H+ + K+)-ATPase membranes from resting and stimulated gastric parietal cells

Redistribution and characterization of (H+ + K+)-ATPase membranes from resting and stimulated gastric parietal cells

Biogenesis of microsomal membrane glycoproteins in rat liver. I. Presence of glycoproteins in microsomes and cytosol.

The β-Subunit of the Rabbit H,K-ATPase: A Glycoprotein with All Terminal Lactosamine Units Capped with α-Linked Galactose Residues

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