Reversible histochemical modifications of endoplasmic reticulum following arginine vasopressin stimulation of granular cells of toad bladder

1995 ◽  
Vol 280 (2) ◽  
pp. 365-370
Author(s):  
Kaveh Danechi ◽  
Tina Hoang ◽  
Michel Bergeron
Keyword(s):  
Endoplasmic Reticulum ◽  
Arginine Vasopressin ◽  
Toad Bladder ◽  
Granular Cells ◽  
Stimulation Of

Reversible histochemical modifications of endoplasmic reticulum following arginine vasopressin stimulation of granular cells of toad bladder

1995 ◽  
Vol 280 (2) ◽  
pp. 365-370
Author(s):  
Kaveh Danechi ◽  
Tina Hoang ◽  
Michel Bergeron
Keyword(s):  
Endoplasmic Reticulum ◽  
Arginine Vasopressin ◽  
Toad Bladder ◽  
Granular Cells ◽  
Stimulation Of

INHIBITION BY MANGANESE OF THE ACTION OF ANTIDIURETIC HORMONE ON ADENYL CYCLASE IN TOAD BLADDER

1971 ◽  
Vol 50 (2) ◽  
pp. 231-235 ◽  
Author(s):  
S. HYNIE ◽  
G. W. G. SHARP
Keyword(s):  
Epithelial Cells ◽  
Water Flow ◽  
Arginine Vasopressin ◽  
Sodium Transport ◽  
Adenyl Cyclase ◽  
Toad Bladder ◽  
Inhibitory Effects ◽  
Marked Contrast ◽  
Hormonal Activation ◽  
Stimulation Of

SUMMARY In view of the report that Mn2+ stimulates sodium transport in the toad bladder but inhibits the effect of vasopressin on both water flow and sodium transport, the effects of this ion on adenyl cyclase from mucosal epithelial cells of toad bladder were investigated. Mn2+ was found to inhibit activation of adenyl cyclase by arginine vasopressin in the presence of Mg2+ and had no effect on activation of the enzyme by sodium fluoride. This is in marked contrast to the effects of Mn2+ on hormonal activation of adenyl cyclase from other tissues in which no inhibitory effects are seen and in which Mn2+ can replace Mg2+ in the reaction mixture. It is concluded that stimulation of sodium transport by Mn2+ is unlikely to be explainable by adenyl cyclase activation and that Mn2+ is not useful in the differentiation of the two forms of adenyl cyclase which are thought to be required for mediation of water flow and sodium transport stimulation by vasopressin.

Interaction of Vasopressin with Human Blood Platelets: Dependency on Mg2+

1986 ◽  
Vol 56 (03) ◽  
pp. 260-262 ◽  
Author(s):  
Isabella Roos ◽  
Fabrizia Ferracin ◽  
Alfred Pletscher
Keyword(s):  
Phosphatidic Acid ◽  
Human Blood ◽  
Arginine Vasopressin ◽  
Specific Binding ◽  
Blood Platelets ◽  
Bivalent Cations ◽  
Platelet Membranes ◽  
Maximal Rise ◽  
Human Blood Platelets ◽  
Stimulation Of

SummaryArginine-vasopressin (AVP) in the presence of Mg2+ but not in the absence of bivalent cations led to accumulation of [32P]-phosphatidic acid ([32P]-PA) in human blood platelets. Mg2+ also enhanced the specific binding of [3H]-AVP to intact platelets. The concentrations of the cation which enabled AVP to cause half maximal rise of [32P]-PA and those inducing half maximal [3H]-AVP-binding were of the same order. It is concluded that the stimulation of phosphatidyl inositide breakdown by AVP in presence of Mg2+ is at least partially due to a Mg2+-induced enhancement of specific AVP-binding to the platelet membranes.

scholarly journals The endosomal transcriptional regulator RNF11 integrates degradation and transport of EGFR

2016 ◽  
Vol 215 (4) ◽  
pp. 543-558 ◽  
Author(s):  
Sandra Scharaw ◽  
Murat Iskar ◽  
Alessandro Ori ◽  
Gaelle Boncompain ◽  
Vibor Laketa ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Egf Receptor ◽  
Regulatory Mechanism ◽  
Transcriptional Regulator ◽  
Transport Efficiency ◽  
Early Endosomes ◽  
Epidermal Growth ◽  
Partial Degradation ◽  
Stimulation Of

Stimulation of cells with epidermal growth factor (EGF) induces internalization and partial degradation of the EGF receptor (EGFR) by the endo-lysosomal pathway. For continuous cell functioning, EGFR plasma membrane levels are maintained by transporting newly synthesized EGFRs to the cell surface. The regulation of this process is largely unknown. In this study, we find that EGF stimulation specifically increases the transport efficiency of newly synthesized EGFRs from the endoplasmic reticulum to the plasma membrane. This coincides with an up-regulation of the inner coat protein complex II (COPII) components SEC23B, SEC24B, and SEC24D, which we show to be specifically required for EGFR transport. Up-regulation of these COPII components requires the transcriptional regulator RNF11, which localizes to early endosomes and appears additionally in the cell nucleus upon continuous EGF stimulation. Collectively, our work identifies a new regulatory mechanism that integrates the degradation and transport of EGFR in order to maintain its physiological levels at the plasma membrane.

scholarly journals Sodium Transport in the Toad Bladder

1971 ◽  
Vol 28 (5_suppl_2) ◽  
Author(s):  
HOWARD S. FRAZIER
Keyword(s):  
Urinary Bladder ◽  
Sodium Transport ◽  
Mode Of Action ◽  
Renal Tubule ◽  
Alternative Hypothesis ◽  
Toad Bladder ◽  
Second Step ◽  
Epithelial Layer ◽  
Granular Cells ◽  
Simple Alternative

The isolated urinary bladder of the toad transports sodium actively across its epithelial layer and responds to the hormones vasopressin and aldosterone, properties which make it a useful model for the study of certain functions of the renal tubule. Sodium transport in the granular cells of the bladder is thought to involve first an energetically passive but selective entry step at the mucosal surface, the rate of which is increased after vasopressin administration. The second step in transport is considered to be active extrusion of the ion across the serosal boundary of the cell. Recent evidence concerning the cellular pool of sodium and the site and mode of action of vasopressin suggests that this description is at best incomplete. No equally simple alternative hypothesis for the organization of sodium transport in this system is available at present.

scholarly journals The formation, distribution and function of ribosomes and microsomal membranes during induced amphibian metamorphosis

1967 ◽  
Vol 105 (2) ◽  
pp. 783-801 ◽  
Author(s):  
J. R. Tata
Keyword(s):  
Endoplasmic Reticulum ◽  
Ribosomal Proteins ◽  
Specific Activity ◽  
Tail Length ◽  
Similar Response ◽  
Carbamoyl Phosphate ◽  
Microsomal Membranes ◽  
Stimulation Of ◽  
Induction Of Metamorphosis

1. A lag period of about 4 days preceded the onset of metamorphosis precociously induced by tri-iodothyronine in tadpoles of the giant American bullfrog (Rana catesbeiana). It was established by the accelerated synthesis or induction of carbamoyl phosphate synthetase and cytochrome oxidase in the liver, serum albumin and adult haemoglobin in the blood, acid phosphatase in the tail, and the increase in the hindleg/tail length ratio. 2. A 4- to 6-fold stimulation, 2 days after the induction of metamorphosis, of the rate of synthesis of rapidly labelled nuclear RNA in liver cells was followed by an increasing amount of RNA appearing in the cytoplasm. Most of the newly formed RNA on induction of metamorphosis was of the ribosomal type. An accelerated turnover at early stages of development preceded a net accumulation of RNA in the cytoplasm, with no change in the amount of DNA per liver. 3. Most hepatic ribosomes of the pre-metamorphic tadpoles were present as 78s monomers and 100s dimers; metamorphosis caused a shift towards larger polysomal aggregates with newly formed ribosomes that were relatively more tightly bound to membranes of the endoplasmic reticulum. 4. The appearance of new polyribosomes in the cytoplasm on induction of metamorphosis was co-ordinated in time with a stimulation of synthesis of phospholipids of the smooth and rough endoplasmic reticulum, followed by a gradual shift in preponderance from the smooth to the rough type of microsomal membranes. 5. Electron- and optical-microscopic examination of intact hepatocytes revealed a striking change in the distribution and nature of ribosomes and microsomal membranes during metamorphosis. 6. Ribosomes prepared from non-metamorphosing and metamorphosing animals were identical in their sedimentation coefficients and in the structural ribosomal proteins. The base composition and sedimentation coefficients of ribosomal RNA were also identical. Induction of metamorphosis also did not alter the incorporation of 32P into the different phospholipid constituents of microsomal membranes. 7. Nascent 14C-labelled protein with the highest specific activity was recovered in the ‘heavy’ rough membrane fraction of microsomes, whereas little 14C was associated with ‘free’ polysomes. Protein synthesis in vivo was most markedly stimulated during metamorphosis in the tightly membrane-bound ribosomal fraction after the appearance of new ribosomes. 8. The rate of synthesis of macromolecules in vivo could not be followed beyond 7–8 days after induction because of variable shifts in precursor pools due to regression of larval tissues. 9. The stimulation of RNA and ribosome formation was specifically associated with the process of metamorphosis since no similar response to thyroid hormones occurred in those species (Axolotl and Necturus) in which the hormones failed to induce metamorphosis.

Chemical chaperone 4-phenylbutylate reduces mutant protein accumulation in the endoplasmic reticulum of arginine vasopressin neurons in a mouse model for familial neurohypophysial diabetes insipidus

2018 ◽  
Vol 682 ◽  
pp. 50-55 ◽  
Author(s):  
Masayoshi Tochiya ◽  
Daisuke Hagiwara ◽  
Yoshinori Azuma ◽  
Takashi Miyata ◽  
Yoshiaki Morishita ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Mouse Model ◽  
Diabetes Insipidus ◽  
Arginine Vasopressin ◽  
Mutant Protein ◽  
Protein Accumulation ◽  
Chemical Chaperone ◽  
Vasopressin Neurons
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