PMID- 17504921
OWN - NLM
STAT- MEDLINE
DCOM- 20070926
LR  - 20220408
IS  - 1470-1626 (Print)
IS  - 1470-1626 (Linking)
VI  - 133
IP  - 4
DP  - 2007 Apr
TI  - Expression of ion transport-associated proteins in human efferent and epididymal 
      ducts.
PG  - 775-84
AB  - Appropriate intraluminal microenvironment in the epididymis is essential for 
      maturation of sperm. To clarify whether the anion transporters SLC26A2, SLC26A6, 
      SLC26A7, and SLC26A8 might participate in generating this proper intraluminal 
      milieu, we studied the localization of these proteins in the human efferent and 
      the epididymal ducts by immunohistochemistry. In addition, immunohistochemistry 
      of several SLC26-interacting proteins was performed: the Na(+)/H(+) exchanger 3 
      (NHE3), the Cl(-) channel cystic fibrosis transmembrane conductance regulator 
      (CFTR), the proton pump V-ATPase, their regulator Na(+)/H(+) exchanger regulating 
      factor 1 (NHERF-1), and carbonic anhydrase II (CAII). Our results show that 
      SLC26A6, CFTR, NHE3, and NHERF-1 are co-expressed on the apical side of the 
      nonciliated cells, and SLC26A2 appears in the cilia of the ciliated cells in the 
      human efferent ducts. In the epididymal ducts, SLC26A6, CFTR, NHERF-1, CAII, and 
      V-ATPase (B and E subunits) were co-localized to the apical mitochondria rich 
      cells, while SLC26A7 was expressed in a subgroup of basal cells. SLC26A8 was not 
      found in the structures studied. This is the first study describing the 
      localization of SLC26A2, A6 and A7, and NHERF-1 in the efferent and the 
      epididymal ducts. Immunolocalization of human CFTR, NHE3, CAII, and V-ATPase in 
      these structures differs partly from previous reports from rodents. Our findings 
      suggest roles for these proteins in male fertility, either independently or 
      through interaction and reciprocal regulation with co-localized proteins shown to 
      affect fertility, when disrupted.
FAU - Kujala, Minna
AU  - Kujala M
AD  - Department of Medical Genetics, University of Helsinki, Helsinki, Finland. 
      minna.kujala@helsinki.fi
FAU - Hihnala, Satu
AU  - Hihnala S
FAU - Tienari, Jukka
AU  - Tienari J
FAU - Kaunisto, Kari
AU  - Kaunisto K
FAU - Hastbacka, Johanna
AU  - Hastbacka J
FAU - Holmberg, Christer
AU  - Holmberg C
FAU - Kere, Juha
AU  - Kere J
FAU - Hoglund, Pia
AU  - Hoglund P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Reproduction
JT  - Reproduction (Cambridge, England)
JID - 100966036
RN  - 0 (Anion Transport Proteins)
RN  - 0 (Antiporters)
RN  - 0 (Membrane Transport Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (SLC26A2 protein, human)
RN  - 0 (SLC26A6 protein, human)
RN  - 0 (SLC26A7 protein, human)
RN  - 0 (SLC26A8 protein, human)
RN  - 0 (SLC9A3 protein, human)
RN  - 0 (Sodium-Hydrogen Exchanger 3)
RN  - 0 (Sodium-Hydrogen Exchangers)
RN  - 0 (Sulfate Transporters)
RN  - 0 (sodium-hydrogen exchanger regulatory factor)
RN  - 126880-72-6 (Cystic Fibrosis Transmembrane Conductance Regulator)
RN  - EC 3.6.1.- (Vacuolar Proton-Translocating ATPases)
RN  - EC 4.2.1.- (Carbonic Anhydrase II)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Anion Transport Proteins/analysis
MH  - Antiporters/analysis
MH  - Carbonic Anhydrase II/analysis
MH  - Cystic Fibrosis Transmembrane Conductance Regulator/analysis
MH  - Epididymis/*chemistry
MH  - Humans
MH  - Immunohistochemistry
MH  - Ion Transport/*physiology
MH  - Male
MH  - Membrane Transport Proteins/*analysis
MH  - Middle Aged
MH  - Phosphoproteins/analysis
MH  - Sodium-Hydrogen Exchanger 3
MH  - Sodium-Hydrogen Exchangers/analysis
MH  - Sulfate Transporters
MH  - Tissue Fixation
MH  - Vacuolar Proton-Translocating ATPases/analysis
MH  - Vas Deferens/*chemistry
EDAT- 2007/05/17 09:00
MHDA- 2007/09/27 09:00
CRDT- 2007/05/17 09:00
PHST- 2007/05/17 09:00 [pubmed]
PHST- 2007/09/27 09:00 [medline]
PHST- 2007/05/17 09:00 [entrez]
AID - 133/4/775 [pii]
AID - 10.1530/rep.1.00964 [doi]
PST - ppublish
SO  - Reproduction. 2007 Apr;133(4):775-84. doi: 10.1530/rep.1.00964.