VASOACTIVE INTESTINAL PEPTIDE (VIP): TISSUE DISTRIBUTION IN THE RAT AS MEASURED BY RADIOIMMUNOASSAY AND BY RADIORECEPTORASSAY

1978 ◽  
Vol 87 (4) ◽  
pp. 799-810 ◽  
Author(s):  
J. Besson ◽  
M. Laburthe ◽  
D. Bataille ◽  
C. Dupont ◽  
G. Rosselin
Keyword(s):  
Digestive Tract ◽  
Plasma Membranes ◽  
Biologically Active ◽  
Muscular Tissue ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes ◽  
Brain Extracts ◽  
High Concentrations ◽  
Almost All ◽  
The Brain

ABSTRACT This work was undertaken to study the distribution of VIP in the digestive tract. VIP was measured both by radioimmunoassay and by radioreceptorassay in order to determine whether immunoreactive VIP is related to a biologically active component. The effect of digestive extracts in inhibiting the binding of porcine [125I]VIP to the antibody (RIA) and to the rat liver plasma membranes (RRA) paralleled that of porcine VIP used as the standard. VIP was found throughout the digestive tract with especially high concentrations between the duodenum (1676 ± 186 ng/g) and the colon (1214 ± 214 ng/g); the maximal quantity occurred in the jejuno-ileum (11 698 ± 687 ng/g). Less than 1 % of VIP was found in the epithelium whereas almost all VIP (> 99%) was localized in the mucosal muscular tissue of the jejunoileum. VIP concentration in the pancreas was 180 ± 26 ng/g of tissue. The VIP contents of the digestive tract were similar when measured either by radioimmunoassay or by radioreceptorassay. Immunoreactive VIP was found in the brain (155 ± 7 ng/g of tissue) and brain extracts competitively inhibited the binding of [125I]VIP (purified from gut) to liver plasma membranes. These results show that: 1) VIP from the overall gastrointestinal tract is a biological active molecule: 2) VIP from brain binds to receptors for intestinal VIP in liver.

scholarly journals Lysophosphatidylcholines can modulate the activity of the glucagon-stimulated adenylate cyclase from rat liver plasma membranes

1979 ◽  
Vol 178 (1) ◽  
pp. 217-221 ◽  
Author(s):  
M D Houslay ◽  
R W Palmer
Keyword(s):  
Adenylate Cyclase ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Hormone Receptors ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes ◽  
Increased Sensitivity

1. Synthetic lysophosphatidylcholines inhibit the glucagon-stimulated adenylate cyclase activity of rat liver plasma membranes at concentrations two to five times lower than those needed to inhibit the fluoride-stimulated activity. 2. Specific 125I-labelled glucagon binding to hormone receptors is inhibited at concentrations similar to those inhibiting the fluoride-stimulated activity. 3. At concentrations of lysophosphatidylcholines immediately below those causing inhibition, an activation of adenylate cyclase activity or hormone binding was observed. 4 These effects are essentially reversible. 5. We conclude that the increased sensitivity of glucagon-stimulated adenylate cyclase to inhibition may be due to the lysophosphatidylcholines interfering with the physical coupling between the hormone receptor and catalytic unit of adenylate cyclase. 6. We suggest that, in vivo, it is possible that lysophosphatidylcholines may modulate the activity of adenylate cyclase only when it is in the hormone-stimulated state.

scholarly journals The roles of phospholipase D and a GTP-binding protein in guanosine 5′-[γ-thio]triphosphate-stimulated hydrolysis of phosphatidylcholine in rat liver plasma membranes

1990 ◽  
Vol 272 (3) ◽  
pp. 749-753 ◽  
Author(s):  
K M Hurst ◽  
B P Hughes ◽  
G J Barritt
Keyword(s):  
Rat Liver ◽  
Phospholipase D ◽  
Plasma Membranes ◽  
Regulatory Protein ◽  
Gtp Binding ◽  
Liver Plasma Membranes ◽  
Low Concentrations ◽  
Rat Liver Plasma Membranes ◽  
Triton X ◽  
Hydrolysis Of

1. Guanosine 5′-[gamma-thio]triphosphate (GTP[S]) stimulated by 50% the rate of release of [3H]choline and [3H]phosphorylcholine in rat liver plasma membranes labelled with [3H]choline. About 70% of the radioactivity released in the presence of GTP[S] was [3H]choline and 30% was [3H]phosphorylcholine. 2. The hydrolysis of phosphorylcholine to choline and the conversion of choline to phosphorylcholine did not contribute to the formation of [3H]choline and [3H]phosphorylcholine respectively. 3. The release of [3H]choline from membranes was inhibited by low concentrations of SDS or Triton X-100. Considerably higher concentrations of the detergents were required to inhibit the release of [3H]phosphorylcholine. 4. Guanosine 5′-[beta gamma-imido]triphosphate and guanosine 5′-[alpha beta-methylene]triphosphate, but not adenosine 5′-[gamma-thio]-triphosphate, stimulated [3H]choline release to the same extent as did GTP[S]. The GTP[S]-stimulated [3H]choline release was inhibited by guanosine 5′-[beta-thio]diphosphate, GDP and GTP but not by GMP. 5. It is concluded that, in rat liver plasma membranes, (a) GTP[S]-stimulated hydrolysis of phosphatidylcholine is catalysed predominantly by phospholipase D with some contribution from phospholipase C, and (b) the stimulation of phosphatidylcholine hydrolysis by GTP[s] occurs via a GTP-binding regulatory protein.

Receptors for calcitonin gene-related peptide on the rat liver plasma membranes

1988 ◽  
Vol 152 (1) ◽  
pp. 383-391 ◽  
Author(s):  
Akinori Yamaguchi ◽  
Tsutomu Chiba ◽  
Yasuhiko Okimura ◽  
Toshiyuki Yamatani ◽  
Tomoyuki Morishita ◽  
...  
Keyword(s):  
Rat Liver ◽  
Plasma Membranes ◽  
Calcitonin Gene Related Peptide ◽  
Related Peptide ◽  
Liver Plasma Membranes ◽  
Calcitonin Gene ◽  
Rat Liver Plasma Membranes

Purification of NADH-cytochromeb 5 reductase from rat liver plasma membranes

PROTOPLASMA ◽  
1995 ◽  
Vol 184 (1-4) ◽  
pp. 111-117 ◽  
Author(s):  
C. Kim ◽  
F. L. Crane ◽  
G. W. Becker ◽  
D. J. Morr�
Keyword(s):  
Rat Liver ◽  
Plasma Membranes ◽  
Liver Plasma Membranes ◽  
Rat Liver Plasma Membranes

scholarly journals ISOLATION OF RAT LIVER PLASMA MEMBRANES

1970 ◽  
Vol 47 (3) ◽  
pp. 604-618 ◽  
Author(s):  
Oscar Touster ◽  
N. N. Aronson ◽  
John T. Dulaney ◽  
Herman Hendrickson
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Plasma Membranes ◽  
Preparative Method ◽  
Membrane Localization ◽  
Plasma Membrane Localization ◽  
Liver Plasma Membranes ◽  
Nucleotide Pyrophosphatase ◽  
Rat Liver Plasma Membranes

Nucleotide pyrophosphatase and phosphodiesterase I of rat liver have been found to be localized primarily in cell particulates highly enriched with respect to the most commonly accepted plasma membrane marker, 5'-nucleotidase, and therefore should themselves be assigned a plasma membrane localization. The observation that plasma membranes sediment in isotonic sucrose with both nuclear and microsomal fractions was exploited to obtain plasma membrane preparations from each fraction. Both preparations are similar in chemical and enzymic composition. Moreover, the preparative method developed in this study appears to give the best combination of yield, purity, and reproducibility available. The question of the possible identity of nucleotide pyrophosphatase and phosphodiesterase I is considered, and evidence is presented suggesting that these activities may be manifestations of the same enzyme.

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