Principal cells in the cauda epididymidis resorb zinc eliminated from spermatozoa

Andrologia ◽  
2003 ◽  
Vol 35 (1) ◽  
pp. 3-3 ◽  
Author(s):  
C. Baldauf ◽  
W. Miska ◽  
W. Weidner ◽  
W.-B. Schill ◽  
R. Henkel
Keyword(s):  
Principal Cells ◽  
Cauda Epididymidis

Detection of ClC-3 and ClC-5 in epididymal epithelium: immunofluorescence and RT-PCR after LCM

2003 ◽  
Vol 284 (1) ◽  
pp. C220-C232 ◽  
Author(s):  
Corinne Isnard-Bagnis ◽  
Nicolas Da Silva ◽  
Valérie Beaulieu ◽  
Alan S. L. Yu ◽  
Dennis Brown ◽  
...  
Keyword(s):  
Vas Deferens ◽  
Chloride Transport ◽  
The Body ◽  
Transepithelial Transport ◽  
Rt Pcr ◽  
Clear Cells ◽  
Principal Cells ◽  
Endosome Trafficking ◽  
Cauda Epididymidis ◽  
Laser Capture

Epithelial cells of the epididymis and vas deferens establish an optimum luminal environment in which spermatozoa mature and are stored. This is achieved by active transepithelial transport of various ions including Cl−and H+. We investigated the localization of three closely related members of the ClC family, ClC-3, ClC-4, and ClC-5, in the epididymis and vas deferens. RT-PCR using mRNA isolated by laser capture microdissection (LCM)-detected ClC-3 and ClC-5 transcripts but did not detect any ClC-4-specific transcript. Western blot and immunofluorescence analysis demonstrated that ClC-3 and ClC-5 proteins are present in all regions of the epididymis and in the vas deferens. ClC-5 is expressed exclusively in H+-ATPase-rich cells (narrow and clear cells). Confocal microscopy showed that ClC-5 partially colocalizes with the H+-ATPase in the subapical pole of clear cells. ClC-3 is strongly expressed in the apical membrane of principal cells of the caput epididymidis and the vas deferens and is less abundant in principal cells of the body and cauda epididymidis. These findings are consistent with a potential role for ClC-3 in transepithelial chloride transport by principal cells and for ClC-5 in the acidification of H+-ATPase-containing vesicles in narrow and clear cells. ClC-5 might facilitate endosome trafficking in the epididymis, as has been proposed in the kidney.

1110: Increased Intercalated Versus Principal Cells in Inner Medullary Collecting Ducts in Human Stone Formers

2005 ◽  
Vol 173 (4S) ◽  
pp. 301-301
Author(s):  
Chung Kuang Su ◽  
Jonathan N. Rubenstein ◽  
Affonso H.L.A. Camargo ◽  
Stephen L. Gluck ◽  
Marshall L. Stoller
Keyword(s):  
Principal Cells ◽  
Stone Formers ◽  
Collecting Ducts

The hamster cauda epididymidis after coitus

1970 ◽  
Vol 77 (1) ◽  
pp. 98-108 ◽  
Author(s):  
R. Vitale-Calpe ◽  
Agustin Aoki
Keyword(s):  
Cauda Epididymidis

pHi determines rate of sodium transport in frog skin: results of a new method to determine pHi

1994 ◽  
Vol 266 (3) ◽  
pp. F367-F374 ◽  
Author(s):  
R. Rick
Keyword(s):  
Frog Skin ◽  
Nuclear Potential ◽  
Na Channel ◽  
Cytoplasmic Ph ◽  
Na Transport ◽  
Principal Cells ◽  
Weak Organic Acid ◽  
Transepithelial Na Transport ◽  
Cell Layers ◽  
Important Regulator

The pH of the isolated frog skin epithelium was determined on a cellular and subcellular level based on the distribution of a weak organic acid, 4-bromobenzoic acid. The indicator is detectable by X-ray microanalysis due to the presence of an element label. The results show that the pH of principal cells, but not the Na concentration, is closely correlated with the rate of transepithelial Na transport. Acidification leads to an inhibition of Na transport, regardless of whether the change was spontaneous or experimentally induced. Under the conditions of this study, the pH of principal cells was not well regulated. At a bath pH of 7.0, large pH differences between the cell layers were detectable. In mitochondria-rich cells, the pH was a function of the intracellular Cl concentration but not the Na transport rate. The cytoplasmic pH consistently exceeded the nuclear pH. The nuclear-cytoplasmic pH differential in principal cells amounted to 0.3 pH units, which is equivalent to a nuclear potential of -17 mV. The results support the view that the intracellular pH (pHi) is an important regulator of transepithelial Na transport. Regulation is primarily achieved at the level of the apical Na channel, making the Na influx the rate-limiting step in Na reabsorption.

scholarly journals Synthesis and glycosylation of CD52, the major 'maturation-associated' antigen of rat spermatozoa, in the cauda epididymidis

Reproduction ◽  
2001 ◽  
pp. 435-446 ◽  
Author(s):  
P Derr ◽  
CH Yeung ◽  
TG Cooper ◽  
C Kirchhoff
Keyword(s):  
Blot Analysis ◽  
Cdna Sequence ◽  
Northern Blot Analysis ◽  
Lectin Binding ◽  
Transcriptional Level ◽  
Lectin Blot ◽  
Molecular Masses ◽  
Rat Epididymis ◽  
Sperm Membrane ◽  
Cauda Epididymidis

A western and lectin blot analysis was performed of the major 'maturation-associated' antigen of rat spermatozoa, which is the rat counterpart of human CD52. In the absence of a suitable antibody, direct study of this approximately 26 kDa antigen, named previously SMemG, had been difficult. In the present study, these problems were overcome by raising a polyclonal antibody against a chemosynthetic peptide predicted from the cDNA sequence of the antigen. The antibody bound to a glycoprotein of rat cauda epididymidal tissue and spermatozoa, this glycoprotein was cleaved by phosphatidylinositol-specific phospholipase C and, after deglycosylation, was reduced to approximately 6 kDa. Northern blot analysis confirmed that the CD52 mRNA was transcribed only post-testicularly, and antibody binding to testicular and sperm proteins of different molecular masses was shown to be nonspecific. Flow cytometry also indicated that the antigen was inserted into the sperm membrane during epididymal transit. Moreover, despite the presence of CD52 mRNA in all parts of the rat epididymis, only the 'long' mRNA molecules of the cauda region were efficiently translated and the antigen glycosylated, indicating that expression of rat CD52 is regulated on a post-transcriptional level. Lectin binding and deglycosylation studies supported the contention that there is extensive mucin-type O-glycosylation of rat CD52. In rats, there was no indication of complex N-linked carbohydrates similar to those described for human CD52.

scholarly journals Vasopressin/V2 receptor stimulates renin synthesis in the collecting duct

2016 ◽  
Vol 310 (4) ◽  
pp. F284-F293 ◽  
Author(s):  
Alexis A. Gonzalez ◽  
Flavia Cifuentes-Araneda ◽  
Cristobal Ibaceta-Gonzalez ◽  
Alex Gonzalez-Vergara ◽  
Leonardo Zamora ◽  
...  
Keyword(s):  
Collecting Duct ◽  
Critical Role ◽  
Combined Treatment ◽  
Receptor Activation ◽  
Ang Ii ◽  
Principal Cells ◽  
Protein Levels ◽  
Renin Synthesis ◽  
Renin Mrna ◽  
Creb Pathway

Renin is synthesized in the principal cells of the collecting duct (CD), and its production is increased via cAMP in angiotensin (ANG) II-dependent hypertension, despite suppression of juxtaglomerular (JG) renin. Vasopressin, one of the effector hormones of the renin-angiotensin system (RAS) via the type 2-receptor (V2R), activates the cAMP/PKA/cAMP response element-binding protein (CREB) pathway and aquaporin-2 expression in principal cells of the CD. Accordingly, we hypothesized that activation of V2R increases renin synthesis via PKA/CREB, independently of ANG II type 1 (AT1) receptor activation in CD cells. Desmopressin (DDAVP; 10−6 M), a selective V2R agonist, increased renin mRNA (∼3-fold), prorenin (∼1.5-fold), and renin (∼2-fold) in cell lysates and cell culture media in the M-1 CD cell line. Cotreatment with DDAVP+H89 (PKA inhibitor) or CREB short hairpin (sh) RNA prevented this response. H89 also blunted DDAVP-induced CREB phosphorylation and nuclear localization. In 48-h water-deprived (WD) mice, prorenin-renin protein levels were increased in the renal inner medulla (∼1.4- and 1.8-fold). In WD mice treated with an ACE inhibitor plus AT1 receptor blockade, renin mRNA and prorenin protein levels were still higher than controls, while renin protein content was not changed. In M-1 cells, ANG II or DDAVP increased prorenin-renin protein levels; however, there were no further increases by combined treatment. These results indicate that in the CD the activation of the V2R stimulates renin synthesis via the PKA/CREB pathway independently of RAS, suggesting a critical role for vasopressin in the regulation of renin in the CD.

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