Alternative titles; symbols
HGNC Approved Gene Symbol: AQP1
Cytogenetic location: 7p14.3 Genomic coordinates (GRCh38): 7:30,911,853-30,925,516 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 7p14.3 | [Aquaporin-1 deficiency] | 110450 | 3 | |
| [Blood group, Colton] | 110450 | 3 |
Aquaporins, such as AQP1, are small membrane-spanning proteins that transport water and small solutes. AQP1 is involved in the transport of various cell types, including endothelial, epithelial, and smooth muscle cells (summary by Lai et al., 2014).
Aquaporin-CHIP is a 28-kD integral protein purified from the plasma membranes of red cells and renal tubules by Denker et al. (1988). The protein was thought at first to be a breakdown product of the Rh polypeptide but was later shown to be a unique molecule that is abundant in erythrocytes and renal tubules. A subpopulation is N-glycosylated. Preston and Agre (1991) isolated a cDNA for this protein, called CHIP28 (channel forming integral protein of 28 kD), from human fetal liver. Analysis of the deduced amino acid sequence suggested that CHIP28 protein contains 6 bilayer-spanning domains, 2 exofacial potential N-glycosylation sites, and intracellular N and C termini. The sequence showed strong homology with the major intrinsic protein of bovine lens (MIP26; 154050), which is the prototype of an ancient family of membrane channels. These proteins are believed to form channels permeable to water and possibly other small molecules.
Lai et al. (2014) noted that the cytoplasmic C-terminal tail of AQP1 contains potential protein-binding sites and a putative calcium-binding EF-hand motif.
Moon et al. (1995) showed that the 13-kb Aqp1 gene in the mouse contains 4 exons with intronic boundaries corresponding to other known aquaporin genes.
Moon et al. (1993) isolated the AQP1 structural gene and partially sequenced it. Genomic Southern analysis indicated the existence of a single AQP1 gene, which was localized to 7p14 by in situ hybridization. Sequence comparisons with similar proteins from diverse species suggested a common evolutionary origin. Deen et al. (1994) showed that the gene is on chromosome 7 by Southern blot hybridization to human/rodent hybrid cell lines and regionalized it to 7p15-p14 by in situ hybridization. By interspecific backcross mapping, Moon et al. (1995) showed that the mouse Aqp1 gene is located on chromosome 6 in a region with homology of synteny with human 7p14.
Keen et al. (1995) localized the AQP1 gene on chromosome 7 within a YAC contig containing 2 polymorphic markers, D7S632 and D7S526. Since aquaporin is known to be expressed in a diverse range of secretory and absorptive epithelia, including many in the eye, it had been proposed as a possible candidate for disorders involving an imbalance in ocular fluid movement. Keen et al. (1995) raised a question of possible involvement in 2 eye diseases that map to that region, retinitis pigmentosa-9 (180104) and dominant cystoid macular dystrophy (153880).
Murata et al. (2000) described an atomic model of AQP1 at 3.8-angstrom resolution from electron crystallographic data. Multiple highly conserved amino acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 angstroms over a span of 1 residue. The atomic model provided a possible molecular explanation to a longstanding puzzle in physiology--how membranes can be freely permeable to water but impermeable to protons.
Sui et al. (2001) reported the structure of the dumbbell-shaped AQP1 water channel at 2.2-angstrom resolution. The channel consists of 3 topologic elements, an extracellular and a cytoplasmic vestibule connected by an extended narrow pore or selectivity filter, averaging 4 angstroms in diameter. Within the selectivity filter, 4 bound waters are localized along 3 hydrophilic nodes, which punctuate an otherwise extremely hydrophobic pore segment, facilitating water transport. The highly conserved histidine-182 residue is critical in establishing water specificity. AQP1 lacks a suitable chain of hydrogen-bonded water molecules in the selectivity filter that could act as a proton wire, indicating that proton transport through the channel is highly energetically unfavorable.
The AQP-CHIP protein exists as a homotetramer which physically resembles channel proteins and was the first molecular water channel identified. The AQP-CHIP cDNA isolated from a human bone marrow cDNA library was found to be related to the major intrinsic protein of lens (154050). Two other related proteins were found to be water transporters (Fushimi et al., 1993; Maurel et al., 1993) and these 3 proteins were referred to as the aquaporins. AQP-CHIP is also expressed in diverse epithelia with distinct developmental patterns. By immunochemical and functional means, Smith et al. (1993) showed that AQP-CHIP is essentially absent in neonatal red cells of the rat. After birth, AQP-CHIP appears in the red cells and increases within several weeks to the adult level of expression. The neonatal kidney, while displaying low levels of AQP-CHIP expression, has a parallel increase in the amount and distribution of AQP-CHIP in the proximal tubules and the descending thin limbs of the loops of Henle, commensurate with the kidney's ability to form concentrated urine. Smith et al. (1993) suggested that the water channels act to promote the rehydration of red cells after their shrinkage in the hypertonic environment of the renal medulla. Rapid rehydration would return the cells to their normal volume, optimizing their deformability for transit in the microcirculation. See Hoffman (1993).
Using colocalization studies and biochemical analysis, Cowan et al. (2000) demonstrated that a protein complex containing mouse Ephb2 (600997) and aquaporin-1 is formed in vivo.
The location of the human AQP1 gene is the same as that of the Colton blood group (110450) on 7p. Smith et al. (1994) demonstrated that the CHIP-glycan is the molecular site of the Colton polymorphism. They also showed that Colton blood group antigen differences result from an ala-val polymorphism at residue 45, located on the first extracellular loop of CHIP. CHIP was selectively immunoprecipitated with anti-Co(a) or anti-Co(b). Approximately 92% of Caucasians are Co(a+b-), approximately 8% are Co(a+b+), and only 0.2% are Co+(a-b+).
Colton antigens cause clinical difficulties infrequently, although maternal-fetal incompatibility and transfusion reactions are known. The power of worldwide blood group referencing makes the rarest of phenotypes accessible, and the single Co+(a-b-) red cell membrane sample in the reference collection was found to lack CHIP by immunoblot. Lack of Colton antigens in association with monosomy 7 has been reported in some cases of leukemia (de la Chapelle et al., 1975; Pasquali et al., 1982).
King et al. (2001) examined the finding that aquaporin-1 deficiency had no obvious clinical consequences in the 6 kindreds identified worldwide who lacked the Colton blood group. Since aquaporin-1 is abundant in renal proximal tubular epithelium, the thin descending limb of the loop of Henle, and the descending vasa recta of the kidney, the authors hypothesized that persons with a deficiency of aquaporin-1 have defects in water homeostasis in the kidneys that can be identified only under conditions of stress. They studied 2 unrelated subjects with aquaporin-1 deficiency and found that they had impaired urinary concentrating ability, suggesting that aquaporin-1 has a physiologic role in renal function. Both were patients in whom homozygous mutations in the AQP1 gene had been identified by Preston et al. (1994). Both were women who had developed antibodies against the Colton blood group in association with pregnancy. One subject had occasional edema of the lower legs, for which she infrequently took a diuretic. She drank 2 to 4 liters of fluid per day. The second drank 2 liters of fluid per day and urinated 2 to 3 times daily, without nocturia.
King et al. (2002) studied the effect of absence of aquaporin-1 on water permeability in the human lung, with a rationale parallel to that used in the study of ability to concentrate urine maximally (King et al., 2001). AQP1 is present in endothelial cells in the lung, including those in the vascular plexus around the airways. They used high-resolution computed tomography scans of the lung to evaluate the response to intravenous fluid challenge in 2 unrelated AQP1-null individuals and 5 normal controls. The airways and pulmonary vessels were measured at baseline and after intravenous administration of 3 liters of saline. Increases in airway wall thickness after fluid administration reflected peribronchiolar edema formation. Both control and AQP1-null subjects had approximately a 20% increase in pulmonary vessel area in response to saline infusion, suggesting similar degrees of loading. Control subjects had a 44% increase in the thickness of the airway wall, consistent with peribronchiolar edema formation. In marked contrast, airway wall thickness did not change in AQP1-null subjects in response to saline infusion. These studies indicated that AQP1 is a determinant of vascular permeability in the lung, and demonstrate a role for aquaporins in human pulmonary physiology.
Worldwide blood group referencing had led to the identification of 5 kindreds in which red cells expressed no Colton antigens; these individuals were said to be Co(a-b-). Preston et al. (1994) obtained blood samples and urine sediment from 3 of these individuals, 1 member from each of 3 kindreds. They were unrelated women of northern European ancestry, and none had hematologic, renal, ocular, respiratory, gastrointestinal, reproductive, or neurologic dysfunction. Cells in these Co(a-b-) individuals appeared morphologically normal, but their red cells exhibited low osmotic water permeability. Genomic DNA analyses demonstrated that 2 individuals were homozygous for different nonsense mutations (exon deletion or frameshift), and the third had a missense mutation encoding a nonfunctioning CHIP molecule. Surprisingly, none of the 3 suffered any apparent clinical consequence, which raised questions about the physiologic importance of CHIP and implied that other mechanisms may compensate for its absence.
Agre et al. (1994) found that, compared with the adult, second and third trimester human fetal red cells had lower CHIP/spectrin ratios and reduced osmotic water permeability; CHIP was already present in human renal tubules by the second trimester.
Using molecular dynamics simulations of water permeation through AQP1, de Groot and Grubmuller (2001) showed that AQP1 acts as a 2-stage filter. The conserved NPA (asp-pro-ala) motifs form a selectivity-determining, or size-exclusion, region. The authors proposed that a second aromatic/arginine (ar/R) region functions as a proton filter.
Agre and Kozono (2003) reviewed the topic of aquaporin water channels. The atomic structure of mammalian AQP1 illustrates how this family of proteins is freely permeated by water but not protons (hydronium ions, H(3)O+). The mercury sensitivity of AQP1 is well explained by localization of the specific residue (C189) at the narrowest segment of the channel at the same level as H180 and R195. Cysteines are present at the corresponding position in several other members of the aquaporin family (AQP2, 107777; AQP5, 600442; AQP6, 601383; and AQP9, 602914). Prior to the introduction of modern loop diuretics, patients with refractory fluid overload were treated with mercurial diuretics, which deliver profound renal diuresis.
AQP1 and AQP4 (600308) regulate the movement of water in ischemic brain, and they appear to play a role in cerebral edema. By searching a microRNA (miRNA) database for miRNAs that could target the 3-prime UTRs of AQP1 and AQP4, Sepramaniam et al. (2010) identified MIR320A (614112). Knockdown of MIR320A via anti-MIR320A in a human astrocytoma cell line upregulated expression of AQP1 and AQP4 mRNA and protein. Conversely, overexpression of pre-MIR320A reduced expression of AQP1 and AQP4 mRNA and protein. Reporter gene assays confirmed direct targeting of the 3-prime UTRs of AQP1 and AQP4 by MIR320A. Astrocytes subjected to oxygen and glucose deprivation, which mimics the ischemic environment, downregulated expression of MIR320A, concomitant with upregulated expression of AQP1 and AQP4. Administration of anti-MIR320A to rats following occlusion of the middle cerebral artery reduced the infarct volume, whereas pre-MIR320A caused a further increase in infarct volume. Sepramaniam et al. (2010) concluded that MIR320 modulates AQP1 and AQP2 and may have a role in cerebral ischemia.
Lai et al. (2014) found that knockdown of Aqp1 prevented the hypoxia-induced increase in migration and proliferation of rat pulmonary arterial smooth muscle cells (PASMCs). In contrast, overexpression of Aqp1 under nonhypoxic conditions mimicked the effect of hypoxia and significantly increased PASMC migration and proliferation to levels similar to those observed with hypoxia. Mutation analysis revealed that the C-terminal tail of Aqp1 was critical for Aqp1-mediated migration and proliferation, whereas the EF-hand motif of Aqp1 and water transport of the channel were not involved.
Knepper (1994) provided a review of the aquaporin family of molecular water channels.
Sorani et al. (2008) reviewed genetic variation in human aquaporins and the effect on phenotypes of water homeostasis, focusing on naturally occurring nonsynonymous coding variants. They noted that there is a significant amount of uncharacterized variation in the aquaglyceroporins.
Ma et al. (1998) generated transgenic mice lacking detectable AQP1 by targeted gene disruption. In kidney proximal tubule membrane vesicles from knockout mice, osmotic water permeability was reduced 8-fold compared with vesicles from wildtype mice. Although the knockout mice were grossly normal in terms of survival, physical appearance, and organ morphology, they became severely dehydrated and lethargic after water deprivation for 36 hours. Body weight decreased by 35 +/- 2%, serum osmolality increased to greater than 500 mOsm, and urinary osmolality (657 +/- 59 mOsm) did not change from that before water deprivation. In contrast, wildtype and heterozygous mice remained active after water deprivation, body weight decreased by 20 to 22%, serum osmolality remained normal, and urine osmolality rose to greater than 2,500 mOsm. Urine sodium concentration in water-deprived knockout mice was less than 10 mM and urine osmolality was not increased by the V2 agonist DDAVP. The results suggested that AQP1 knockout mice are unable to create a hypertonic medullary interstitium by countercurrent multiplication. Ma et al. (1998) concluded that AQP1 is thus required for the formation of a concentrated urine by the kidney.
Yang et al. (2001) generated Aqp1/Aqp3 double-knockout mice by intercross of Aqp1 -/- and Aqp3 -/- mice. The mice had reduced survival and growth compared with single-knockout mice. Erythrocyte water permeability was not further reduced by the elimination of Aqp3, nor did the deletion affect glycerol permeability. The double-knockout mice manifested tumor-like bilateral swelling of the flanks due to kidney enlargement that was associated with serum azotemia and mortality by age 12 weeks. Most Aqp3- and Aqp3-/Aqp1-deficient mice showed medullary atrophy and cortical thinning.
Two AQP water channels are expressed in mammalian cornea, AQP1 in endothelial cells and AQP5 in epithelial cells. Thiagarajah and Verkman (2002) examined the effect of Aqp1 or Aqp5 knockout in mice. Corneal thickness in fixed sections was reduced in Aqp1-null mice and increased in Aqp5-null mice. After exposure of the external corneal surface to hypotonic saline, the rate of corneal swelling was reduced by Aqp5 deletion. After exposure of the endothelial surface to hypotonic saline by anterior chamber perfusion, the rate of corneal swelling was reduced by Aqp1 deletion. The recovery of corneal transparency and thickness after hypotonic swelling was delayed in Aqp1-null mice. Thiagarajah and Verkman (2002) concluded that AQP1 and AQP5 provide the principal routes for corneal water transport across the endothelial and epithelial barriers, respectively.
Saadoun et al. (2005) demonstrated remarkably impaired tumor growth in aquaporin-null mice after subcutaneous or intracranial tumor cell implantation, with reduced tumor vascularity and extensive necrosis. A mechanism for the impaired angiogenesis was established from cell culture studies. Although adhesion and proliferation were similar in primary cultures of aortic endothelia from wildtype and from Aqp1-null mice, cell migration was greatly impaired in Aqp1-deficient cells, with abnormal vessel formation in vitro. Stable transfection of nonendothelial cells with Aqp1 or with a structurally different water-selective transporter (AQP4; 600308) accelerated cell migration and wound healing in vitro. Motile Aqp1-expressing cells had prominent membrane ruffles at the leading edge with polarization of Aqp1 protein to lamellipodia, where rapid water fluxes occur. Saadoun et al. (2005) concluded that their findings supported a fundamental role of water channels in cell migration, which is central to diverse biologic phenomena including angiogenesis, wound healing, tumor spread, and organ regeneration.
Using Western blot and immunofluorescence analyses, Liu et al. (2019) showed that Aqp1 expression was upregulated by chronic hypoxia exposure in pulmonary arterial endothelial cells and in PASMCs of the medial layer during development of hypoxia-induced pulmonary hypertension in mice. In contrast, deletion of Aqp1 attenuated hypoxia-induced pulmonary hypertension in mice without affecting the left ventricular hemodynamics function. Aqp1 deletion reduced chronic hypoxia-induced vascular remodeling and reversed overexpression of Hif1-alpha (HIF1A; 603348) and Hif2-alpha (EPAS1; 126110) induced by hypoxia in lung of Aqp1 -/- mice. Furthermore, Aqp1 deficiency repressed Hif1-alpha protein stability in PASMCs under hypoxia. Hypoxia-induced pulmonary vascular remodeling occurred because Aqp1 deletion reduced hypoxia-induced proliferation of PASMCs, which was associated with increased apoptosis and arrested cell cycle of PASMCs. In addition to reduced proliferation, Aqp1 deletion attenuated hypoxia-induced migration and reduced cytoskeleton reorganization of PASMCs by reducing the beta-catenin (CTNNB1; 116806) protein level. Analysis with isolated mouse lung endothelial cells (MLECs) revealed that Aqp1 deletion attenuated hypoxia-induced apoptosis of MLECs and protected cells from apoptosis in response to injury.
Smith et al. (1994) found that the DNA sequence of the AQP1 gene from Colton-typed individuals (see 110450) predicted that residue 45 is alanine in the Co(a+b-) phenotype and valine in the Co(a-b+) phenotype. The nucleotide polymorphism corresponds to a PflMI endonuclease digestion site in the DNA from Co(a-b+) individuals.
One of the 3 Colton-null probands studied by Preston et al. (1994) had a pro38-to-leu missense mutation in the aquaporin-1 gene, as a result of a C-to-T transition at nucleotide 113. None of the Co(a-b-) individuals had experienced hematologic, renal, ocular, respiratory, gastrointestinal, reproductive, or neurologic dysfunction. The red cells exhibited low osmotic water permeabilities.
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