PMID- 10347194
OWN - NLM
STAT- MEDLINE
DCOM- 19990701
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 23
DP  - 1999 Jun 4
TI  - Cloning and characterization of KCC3 and KCC4, new members of the cation-chloride
      cotransporter gene family.
PG  - 16355-62
AB  - The K+-Cl- cotransporters (KCCs) belong to the gene family of electroneutral
      cation-chloride cotransporters, which also includes two bumetanide-sensitive
      Na+-K+-2Cl- cotransporters and a thiazide-sensitive Na+-Cl- cotransporter. We
      have cloned cDNAs encoding mouse KCC3, human KCC3, and human KCC4, three new
      members of this gene family. The KCC3 and KCC4 cDNAs predict proteins of 1083 and
      1150 amino acids, respectively. The KCC3 and KCC4 proteins are 65-71% identical
      to the previously characterized transporters KCC1 and KCC2, with which they share
      a predicted membrane topology. The four KCC proteins differ at amino acid
      residues within key transmembrane domains and in the distribution of putative
      phosphorylation sites within the amino- and carboxyl-terminal cytoplasmic
      domains. The expression of mouse KCC3 in Xenopus laevis oocytes reveals the
      expected functional characteristics of a K+Cl- cotransporter: Cl--dependent
      uptake of 86Rb+ which is strongly activated by cell swelling and weakly sensitive
      to furosemide. A direct functional comparison of mouse KCC3 to rabbit KCC1
      indicates that KCC3 has a much greater volume sensitivity. The human KCC3 and
      KCC4 genes are located on chromosomes 5p15 and 15q14, respectively. Although
      widely expressed, KCC3 transcripts are the most abundant in heart and kidney, and
      KCC4 is expressed in muscle, brain, lung, heart, and kidney. The unexpected
      molecular heterogeneity of K+-Cl- cotransport has implications for the physiology
      and pathophysiology of a number of tissues.
FAU - Mount, D B
AU  - Mount DB
AD  - Department of Medicine, Vanderbilt University Medical Center, Nashville,
      Tennessee 37232, USA. david.mount@mcmail.vanderbilt.edu
FAU - Mercado, A
AU  - Mercado A
FAU - Song, L
AU  - Song L
FAU - Xu, J
AU  - Xu J
FAU - George, A L Jr
AU  - George AL Jr
FAU - Delpire, E
AU  - Delpire E
FAU - Gamba, G
AU  - Gamba G
LA  - eng
SI  - GENBANK/AF087436
SI  - GENBANK/AF105365
SI  - GENBANK/AF105366
GR  - K-11 DK02103/DK/NIDDK NIH HHS/United States
GR  - R-29 HL-49251/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Chlorides)
RN  - 0 (SLC12A6 protein, human)
RN  - 0 (SLC12A7 protein, human)
RN  - 0 (Slc12a6 protein, mouse)
RN  - 0 (Slc12a7 protein, mouse)
RN  - 0 (Symporters)
RN  - 0 (potassium-chloride symporters)
RN  - RWP5GA015D (Potassium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Blotting, Northern
MH  - Carrier Proteins/*genetics/metabolism
MH  - Chlorides/*metabolism
MH  - Cloning, Molecular
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Phylogeny
MH  - Potassium/*metabolism
MH  - Rabbits
MH  - Sequence Alignment
MH  - *Symporters
MH  - Xenopus laevis
EDAT- 1999/05/29 10:00
MHDA- 2001/03/28 10:01
CRDT- 1999/05/29 10:00
PHST- 1999/05/29 10:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1999/05/29 10:00 [entrez]
AID - 10.1074/jbc.274.23.16355 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Jun 4;274(23):16355-62. doi: 10.1074/jbc.274.23.16355.