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  The adenylate cyclase-coupled vasopressin V2-receptor is highly laterally mobile in membranes of LLC-PK1 renal epithelial cells at physiological temperature

Jans, D. A., Peters, R., Zsigo, J., & Fahrenholz, F. (1989). The adenylate cyclase-coupled vasopressin V2-receptor is highly laterally mobile in membranes of LLC-PK1 renal epithelial cells at physiological temperature. The EMBO Journal, 8(9), 2481-2488. doi:10.1002/j.1460-2075.1989.tb08384.x.

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 Creators:
Jans, David A.1, Author           
Peters, Reiner2, Author           
Zsigo, Josef2, Author           
Fahrenholz, Falk1, Author           
Affiliations:
1Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_3273414              
2Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3264817              

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Free keywords: vasopressin; V2-receptor; epithelialcellline; lateralmobility; photobleaching
 Abstract: The lateral mobility of membrane-associated hormone receptors has been proposed to play an important role in signal transduction. Direct measurements, however, have shown that the receptors for insulin, epidermal growth factor and beta-adrenergic antagonists exhibit low mobility at physiological temperature. The present study, which represents the first report of lateral mobility of a polypeptide hormone receptor coupled to adenylate cyclase, yielded quite different results. The lateral mobility of the vasopressin renal-type V2-receptor was measured in the basal plasma membrane of cells of the LLC-PK1 porcine epithelial line, using the technique of fluorescence microphotolysis (photobleaching) and a rhodamine-labelled analogue of vasopressin. The analogue, 1-deamino[8-lysine(N6-tetramethylrhodamylaminothiocarbonyl)] vasopressin (TR-LVP) was synthesized and shown to have binding properties and biological activities very similar to those of Arg8-vasopressin (AVP). TR-LVP could be used to label specifically the V2-receptor of living LLC-PK1 cells, whereby LLC-PK1 cells incubated with TR-LVP in the presence of a 100-fold excess of AVP, or cells from the LLC-PK1 V2-receptor-deficient line M18 incubated with TR-LVP could be used as controls for non-specific binding. Using optical sectioning, specific receptor mobility could be measured both in the absence and presence of free TR-LVP. The V2-receptor was found to be largely mobile at 37 degrees C: the mobile fraction (f) was approximately 0.9, and the apparent lateral diffusion coefficient (D) approximately 3.0 X 10(-10) cm2/s. V2-receptor mobility greatly decreased with decreasing temperature: at 10 degrees C f was reduced to approximately 0.1.

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Language(s): eng - English
 Dates: 1989-06-121989-04-101989-09-01
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: The EMBO Journal
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 8 (9) Sequence Number: - Start / End Page: 2481 - 2488 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061_1