scholarly journals Permeability of lactating-rat mammary gland Golgi membranes to monosaccharides

1980 ◽  
Vol 190 (3) ◽  
pp. 621-624 ◽  
Author(s):  
M D White ◽  
N J Kuhn ◽  
S Ward
Keyword(s):  
Mammary Gland ◽  
Membrane Vesicles ◽  
Golgi Membrane ◽  
Temperature Dependent ◽  
Golgi Membranes ◽  
Rat Mammary Gland ◽  
Lactose Synthesis

The Golgi-membrane vesicles present in particulate preparations of lactating rat mammary gland were biosynthetically loaded with [14C]lactose. This lactose was effectively retained by particles sedimented after exposure to 0.25 M-disaccharide, but was partly lost after exposure to 0.25 M-glucose or other solutes of similar size. Loss of lactose was time-, concentration- and temperature-dependent and varied with the solute structure. This behaviour is ascribed to the presence of protein in the Golgi membrane, forming a specific carrier or channel that serves to supply glucose for lactose synthesis.

scholarly journals Mannitol and glucose movement across the Golgi membrane of lactating-rat mammary gland

1981 ◽  
Vol 194 (1) ◽  
pp. 173-177 ◽  
Author(s):  
M D White ◽  
N J Kuhn ◽  
S Ward
Keyword(s):  
Mammary Gland ◽  
Pore Size ◽  
Membrane Vesicles ◽  
Golgi Membrane ◽  
First Order ◽  
First Order Kinetics ◽  
Rat Mammary Gland ◽  
Lactose Synthesis ◽  
Kinetics Of ◽  
Uptake And Release

1. Purified Golgi-membrane vesicles of lactating-rat mammary gland were penetrated by glucose. 3-O-methylglucose, mannose, fructose, sorbitol and mannitol, but not by lactose or sucrose. 2. The kinetics of mannitol uptake and release were followed at 2-6 degrees C with the aid of fine filters (0.45 micrometers pore size) to separate the vesicles from the medium. 3. Mannitol efflux exhibited apparent first-order kinetics with k approximately 1 min-1. Neither saturability, nor inhibition by excess sorbitol or glucose, could be observed. 4. Mannitol efflux at 18 degrees C was about seven times faster than at 1 degrees C, and rates at higher temperatures were too fast to be measured. The rate of glucose efflux at 2-6 degrees C exceeded that of mannitol severalfold. 5. These findings imply a channel or carrier of definite, but limited, specificity straddling the Golgi membrane and able to supply glucose for lactose synthesis.

scholarly journals Effects of phlorrhizin and thiol reagents on the galactosyltransferase activity of Golgi membrane vesicles of lactating rat mammary gland

1980 ◽  
Vol 188 (2) ◽  
pp. 503-507 ◽  
Author(s):  
N J Kuhn ◽  
A White
Keyword(s):  
Mammary Gland ◽  
Membrane Vesicles ◽  
Golgi Membrane ◽  
No Inhibition ◽  
Glucose Analogues ◽  
Rat Mammary Gland

1. The ability of phlorrhizin to inhibit the galactosylation of glucose was re-examined with Golgi membrane vesicles purified from rat mammary gland, and extended to the galactosylation of several glucose analogues and N-acylglucosamines. 2. The inhibition is ascribed, contrary to previous conclusions, to a general annealing of leaky membranes comprising a minority of the vesicles. 3. Three thiol reagents were able to inhibit the galactosylation of N-acylglucosamines with less, or no, inhibition of galactosylation of glucose. This demonstrates the existence of a Golgi membrane carrier that distinguishes between glucose and N-acylglucosamines.

scholarly journals Evidence for specific transport of uridine diphosphate galactose across the Golgi membrane of rat mammary gland

1976 ◽  
Vol 154 (1) ◽  
pp. 243-244 ◽  
Author(s):  
N J Kuhn ◽  
A White
Keyword(s):  
Mammary Gland ◽  
Golgi Apparatus ◽  
Facilitated Transport ◽  
Uridine Diphosphate ◽  
Golgi Membrane ◽  
Specific Transport ◽  
Rat Mammary Gland ◽  
Lactose Synthesis ◽  
Uridine Diphosphate Galactose

The inhibition of lactose synthesis by UDP-glucose, UDP-glucuronate and, less so, by UDP-N-acetylglucosamine was markedly smaller in preparations of “intact” than of lysed vesicles derived from the Golgi apparatus of lactating rat mammary gland. This constitutes evidence for a specific, probably facilitated, transport of UDP-galactose across the Golgi membrane.

scholarly journals The topography of lactose synthesis

1975 ◽  
Vol 148 (1) ◽  
pp. 77-84 ◽  
Author(s):  
N J Kuhn ◽  
A White
Keyword(s):  
Mammary Gland ◽  
Transport System ◽  
Active Site ◽  
Golgi Membrane ◽  
Glucose Transport System ◽  
Lactose Synthase ◽  
Rat Mammary Gland ◽  
Lactose Synthesis ◽  
Relationship Of ◽  
The Relationship

1. At short incubation times, and under suitable osmotic conditions, the lactose synthesized by Golgi-derived vesicles of rat mammary gland is 85-90% particulate. Evidence is presented for its occlusion within the lumen of the vesicles. 2. Ovalbumin is used as a bulky active-site inhibitor to show that the active site of lactose synthase lies on the inner face of the Golgi membrane. 3. Phlorrhizin and phloretin inhibit lactose synthesis by such vesicles, indicating the presence of a glucose-transport system. 4. The relationship of this topography to the synthesis of N-acetylneuraminyl-lactose and to the secretion of milk sugars is discussed.

Insulin binding to rat mammary-gland Golgi membranes

1981 ◽  
Vol 9 (5) ◽  
pp. 469-469
Author(s):  
DAVID J. FLINT ◽  
DAVID W. WEST
Keyword(s):  
Mammary Gland ◽  
Insulin Binding ◽  
Golgi Membranes ◽  
Rat Mammary Gland

scholarly journals Incorporation into phospholipid vesicles of pore-like properties from Golgi membranes of lactating-rat mammary gland

1986 ◽  
Vol 236 (1) ◽  
pp. 91-96 ◽  
Author(s):  
A V Wallace ◽  
N J Kuhn
Keyword(s):  
Mammary Gland ◽  
Gel Filtration ◽  
Egg Yolk ◽  
Phospholipid Vesicles ◽  
Selective Permeability ◽  
Golgi Membranes ◽  
Rat Mammary Gland ◽  
Acidic Phospholipids ◽  
Triton X ◽  
Sepharose 4B

The ability of rat mammary-gland Golgi membranes to produce monosaccharide-specific pores in phospholipid vesicles was investigated. The apparent ability of Triton X-100 extracts of Golgi membranes to form such pores was re-evaluated, since we have now found that an apparent pore is produced by the detergent alone. We therefore incorporated intact Golgi membranes (1 mg of protein) into egg-yolk phospholipid vesicles by direct sonication in the absence of any detergent. These vesicles retained about 0.6% of the total sucrose, but demonstrated selective permeability towards glucose compared with sucrose, with 19.8% of the glucose being lost during gel filtration on Sepharose 4B. This phenomenon seemed to be enhanced by the presence of acidic phospholipids and lysophosphatidylcholine, but was inhibited by inclusion of cholesterol in the vesicles. The best mixture of phospholipids comprised 6.5 mg of egg-yolk phospholipid, 1 mg of phosphatidylserine and 0.05 mg of lysophosphatidylcholine, where 32.9% of the glucose was lost. By using this optimum phospholipid mixture the pores were shown to be permeable to both glucose and mannitol, whereas sucrose and lactose were retained by the vesicles. Chaps (3- [(3-cholamidopropyl)dimethylammonio] propane-1-sulphonate)-solubilized membranes produced similar permeability in vesicles produced by dialysis of a solution of the phospholipids mixed with the membrane extract. This technique resulted in a greater loss of glucose, 33% loss requiring about 0.25 mg of protein. The pore-forming ability of both intact Golgi membranes and Chaps extracts was sensitive to boiling and proteolysis, indicating that a membrane protein was likely to be involved in pore formation.

scholarly journals The role of nucleoside diphosphatase in a uridine nucleotide cycle associated with lactose synthesis in rat mammary-gland Golgi apparatus

1977 ◽  
Vol 168 (3) ◽  
pp. 423-433 ◽  
Author(s):  
N J Kuhn ◽  
A White
Keyword(s):  
Mammary Gland ◽  
Uridine Nucleotide ◽  
Lactose Synthase ◽  
Bivalent Metal Ions ◽  
Ump Kinase ◽  
Rat Mammary Gland ◽  
Lactose Synthesis ◽  
Galactose Utilization ◽  
Nucleoside Diphosphatase

1. UDP-galactose utilization by isolated Golgi vesicles or rat mammary gland synthesizing lactose causes accumulation of UMP but not UDP, although UDP is the immediate product of lactose synthase (EC 2.4.1.22). 2. This can be ascribed to a nucleoside diphosphatase (EC 3.6.1.6), specific for UDP, GDP and IDP, activated by bivalent metal ions and apparently located on the luminal face of the Golgi membrane. 3. The uridine diphosphatase activity exceeds the total galactosyltransferase activity 5-fold, and is estimated to maintain UDP at about 14 micrometer within the Golgi lumen. 4. Evidence is given that UMP, but not UDP, penetrates the membrane and that UMP is rephosphorylated to UDP by a UMP kinase located in the cytosol. 5. Golgi-cytosol relationships with respect to lactose synthesis are formulated in terms of a uridine nucleotide cycle which throws new light on the energy cost and possible regulation of lactose synthesis.

Lactose Synthesis by a Golgi Apparatus Fraction from Rat Mammary Gland

Nature ◽  
1970 ◽  
Vol 228 (5276) ◽  
pp. 1105-1106 ◽  
Author(s):  
T. W. KEENAN ◽  
D. JAMES MORRÉ ◽  
R. D. CHEETHAM
Keyword(s):  
Mammary Gland ◽  
Golgi Apparatus ◽  
Rat Mammary Gland ◽  
Lactose Synthesis
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