Preferential binding of vasoactive intestinal polypeptide to basolateral membrane of rat and rabbit enterocytes.

Dharmsathaphorn, Kiertisin; Harms, Verna; Yamashiro, Darrell J.; Hughes, Richard J.; Binder, Henry J.; Wright, Ernest M.

doi:10.1172/jci110748

Cited by 72 publications

(23 citation statements)

References 28 publications

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“…The signalling cascade mediated by cAMP leads to the phosphorylation of target proteins by cAMP-dependent protein kinase. It has been reported that VIP receptors are located in intestinal basolateral membranes [27]: as a matter of fact, our results indicate that overlapping effects are obtained when cAMP is substituted by VIP + GTP in the pretreatment of basolateral membranes, whereas VIP has not been tested in brush border.…”

Section: Discussionsupporting

confidence: 46%

PKA Regulation of Bicarbonate and Lactate Movements Across Rat Jejunal Plasma Membranes

Orsenigo

Tosco²,

Laforenza³

et al. 2004

Cell Physiol Biochem

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Background/Aims: Evidence was previously given that the mechanisms involved in bicarbonate and lactate movements across rat jejunal enterocyte are modulated by PKC and Ca²⁺/CaM. Aim of this study was to investigate the possible role of PKA on bicarbonate and lactate transports. Methods: Enzymatic assays in isolated plasma membranes were performed. Moreover membrane vesicles, transiently opened and resealed, were treated with a phosphorylating solution (leading to PKA activation) and were used after that to perform uptake studies. Results: Enzymatic assays give evidence for the presence of PKA in plasma membranes from rat jejunum. Uptake experiments suggest that PKA stimulates the two systems that accomplish basolateral HCO₃^- efflux from the enterocyte, namely Cl^-/ HCO₃^- exchanger and HCO₃^- conductance, without affecting HCO₃^- influx from the lumen mediated by Na⁺/H⁺ exchanger activity. Moreover basolateral H⁺-lactate symporter is stimulated by PKA, as well as the brush border isoform of Na⁺-glucose cotransporter SGLT1. Conclusion: PKA activation evokes individual responses that could be coordinated through cellular metabolism.

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Section: Discussionsupporting

confidence: 46%

PKA Regulation of Bicarbonate and Lactate Movements Across Rat Jejunal Plasma Membranes

Orsenigo

Tosco²,

Laforenza³

et al. 2004

Cell Physiol Biochem

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“…PACAP-38 and VIP have no neuronal component in their respective secretory responses in this tissue. VIP affects epithelial transport processes directly via specific receptors within the basolateral domain (Dharmsathaphorn et al, 1983) and it is probable that PACAP-38 also affects these receptors. Neither of these peptides therefore appear to have a high enough affinity for the neuronal PACAP-27 receptors.…”

Section: Discussionmentioning

confidence: 99%

Pituitary adenylate cyclase activating polypeptides, PACAP‐27 and PACAP‐38: stimulators of electrogenic ion secretion in the rat small intestine

Cox

1992

British J Pharmacology

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1 The effects of pituitary adenylate cyclase activating polypeptide (PACAP)-27 and PACAP-38 were investigated and compared with vasoactive intestinal polypeptide (VIP) responses in voltage clamped preparations of rat jejunum. Under these conditions electrogenic ion secretion was continuously recorded. 2 PACAP-27 is the most potent secretagogue described thus far, exhibiting a concentration-dependent dual secretory action. At low concentrations it stimulated rapid, transient secretory responses (not seen with either PACAP-38 or VIP) and these were inhibited by tetrodotoxin (TTX). At higher nM concentrations of PACAP-27 more prolonged secretory responses predominated which were insensitive to TTX.3 In the presence of TTX, the concentration-response curve to PACAP-27 gave an EC50 value of 29.4 ± 5.4 nM (n = 4) compared with 0.8 ± 0.1 nM (n = 9) for PACAP-27 alone and 30.6 ± 5.6 nM (n = 5) for PACAP-38. C-terminal fragments of PACAP-38 were not significantly effective. 4 Blockade of muscarinic and nicotinic receptors partially inhibited the low concentration effects of PACAP-27. Substance P densensitization and capsaicin pretreatment were effective at inhibiting the transient secretory PACAP-27 responses. Evidence is presented for selective, high affinity PACAP-27 receptors on submucous neurones innervating the mucosal region of the rat jejunum.

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“…The half-maximal stimulation of the adenylate cyclase reported above will therefore be over-estimated 8 VIP AND RENAL FUNCTION 9 by approximately 1P2-fold. Since the relative degradative capacity of renal cortical membranes could conceivably alter the apparent specificity to related hormones, and in particular glucagon, we have determined the relative response of basolateral membranes to both VIP and glucagon in the presence of 1 % w/v bacitracin, a concentration known to completely inhibit the degradation of glucagon by purified basolateral membranes (Talor et al 1983) [125I]VIP in a variety of tissues (Dharmsathaphorn et al 1983;Couvineau & Laburthe, 1985 Fig. 5) compared to cortical tubules, confirming previous workers (Dousa, N. M. GRIFFITHS AND N. L. SIMMONS Shah, & Abboud, 1980).…”

Section: Vip and Renal Functionmentioning

confidence: 99%

Vasoactive intestinal polypeptide regulation of rabbit renal adenylate cyclase activity in vitro.

Griffiths

Simmons

1987

The Journal of Physiology

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SUMMARY1. The effect of vasoactive intestinal polypeptide (VIP) upon adenylate cyclase activity was determined in purified cortical basolateral membranes and in glomeruli and tubular elements obtained from rabbit kidney.2. In purified basolateral membranes prepared from cortex, 1 /LM-VIP consistently stimulated adenylate cyclase activity above basal levels (1 55 ± 009-fold (mean + S.E. ofmean), n = 10 animals). Half-maximal stimulation was observed at 17 + 11 nM-VIP (S.D., n = 9).3. Related peptides, e.g. secretin, glucagon, gastric inhibitory peptide, human pancreatic growth hormone releasing factor, and peptide having N-terminal histidine and C-terminal isoleucine amide (PHI), were without effect or gave lower stimulations of adenylate cyclase activity when tested at 1 ,/bM. 4. Significant VIP degradation was observed under the assay conditions used but this did not substantially alter the response or selectivity to VIP. 5. In separate preparations of isolated glomeruli and proximal tubules addition of 1 /LM-VIP resulted in a 3-3+ 1 1-fold (S.D., n = 3) and 2-2+1 0-fold (S.D., n = 3) stimulation (respectively) of adenylate cyclase activity.6. In isolated medullary tubule suspensions, isolated by collagenase-hyaluronidase digestion of outer (red) medulla, and in thick ascending-limb-enriched preparations prepared by Percoll density gradient fractionation, 1 ,tM-VIP significantly increased adenylate cyclase activity by 2-4+0-6-fold (S.D., n = 3) and 2-1 +0-7-fold (S.D., n = 3) respectively. 7. A possible role for VIP in the regulation of renal function in the rabbit is discussed in relation to the occurrence of VIP stimulation of adenylate cyclase activity in several renal cellular elements.

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Preferential binding of vasoactive intestinal polypeptide to basolateral membrane of rat and rabbit enterocytes.

Cited by 72 publications

References 28 publications

PKA Regulation of Bicarbonate and Lactate Movements Across Rat Jejunal Plasma Membranes

PKA Regulation of Bicarbonate and Lactate Movements Across Rat Jejunal Plasma Membranes

Pituitary adenylate cyclase activating polypeptides, PACAP‐27 and PACAP‐38: stimulators of electrogenic ion secretion in the rat small intestine

Vasoactive intestinal polypeptide regulation of rabbit renal adenylate cyclase activity in vitro.

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