SLC26A2 (Diastrophic Dysplasia Sulfate Transporter) is Expressed in Developing and Mature Cartilage But Also in Other Tissues and Cell Types

Haila, Siru; Hästbacka, Johanna; Böhling, Tom; Karjalainen–Lindsberg, Marja-Liisa; Kere, Juha; Saarialho–Kere, Ulpu

doi:10.1177/002215540104900805

Cited by 82 publications

(68 citation statements)

References 21 publications

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“…The anti-A2, -A6, and -A7 antibodies were purified from whole serum by affinity chromatography (Amersham Pharmacia Biotech). The specificity of these antibodies except for anti-A8 has been shown previously (Haila et al 2001, Lohi et al 2002, Kujala et al 2005.…”

Section: Antibodiesmentioning

confidence: 63%

Expression of ion transport-associated proteins in human efferent and epididymal ducts

Kujala¹,

Hihnala²,

Tienari³

et al. 2007

Reproduction

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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 C /H C exchanger 3 (NHE3), the Cl K channel cystic fibrosis transmembrane conductance regulator (CFTR), the proton pump V-ATPase, their regulator Na C /H C 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. Reproduction (2007) 133 775-784

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Section: Antibodiesmentioning

confidence: 63%

Expression of ion transport-associated proteins in human efferent and epididymal ducts

Kujala¹,

Hihnala²,

Tienari³

et al. 2007

Reproduction

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“…NMR Spectroscopy-Uniformly and isotopically enriched 15 N wild type and ⌬Y526/7 SLC26A3 STAS domain were expressed in M9 minimal media with [ 15 N]ammonium chloride as the nitrogen source, supplemented with 5% uniformly 15 Nlabeled BioExpress cell growth media (Cambridge Isotope Lab-oratories). The proteins were purified as described above with the only change being that the protein was eluted off of the gel filtration column in 50 mM potassium phosphate, pH 6.8, 400 mM potassium chloride, 100 mM arginine, 2% glucose, 2 mM DTT.…”

Section: Methodsmentioning

confidence: 99%

Congenital Chloride-losing Diarrhea Causing Mutations in the STAS Domain Result in Misfolding and Mistrafficking of SLC26A3

Dorwart

Shcheynikov

Baker

et al. 2008

Journal of Biological Chemistry

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Congenital chloride-losing diarrhea (CLD) is a genetic disorder causing watery stool and dehydration. Mutations in SLC26A3 (solute carrier 26 family member 3), which functions as a coupled Cl ؊ /HCO 3 ؊ exchanger, cause CLD. SLC26A3 is a membrane protein predicted to contain 12 transmembranespanning ␣-helices and a C-terminal STAS (sulfate transporters and anti-sigma-factor) domain homologous to the bacterial anti-sigma-factor antagonists. The STAS domain is required for SLC26A3 Cl ؊ /HCO 3 ؊ exchange function and for the activation of cystic fibrosis transmembrane conductance regulator by SLC26A3. Here we investigate the molecular mechanism(s) by which four CLD-causing mutations (⌬Y526/7, I544N, I675/ 6ins, and G702Tins) in the STAS domain lead to disease. In a heterologous mammalian expression system biochemical, immunohistochemical, and ion transport experiments suggest that the four CLD mutations cause SLC26A3 transporter misfolding and/or mistrafficking. Expression studies with the isolated STAS domain suggest that the I675/6ins and G702Tins mutations disrupt the STAS domain directly, whereas limited proteolysis experiments suggest that the ⌬Y526/7 and I544N mutations affect a later step in the folding and/or trafficking pathway. The data suggest that these CLD-causing mutations cause disease by at least two distinct molecular mechanisms, both ultimately leading to loss of functional protein at the plasma membrane.

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“…More over, SLC26A2 expression is also detected in tissues not affected in chondrodysplasias caused by SLC26A2 mutations. 19 ACG-2 is characterized genetically by a mutation in the COL2A1 gene. The COL2A1 gen located on chromosome 12.…”

Section: The Genetically Of Achondrogenesismentioning

confidence: 99%

The genetic aspect and morphological appearance of achondrogenesis

Parwanto

2017

Int J Reprod Contracept Obstet Gynecol

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Achondrogenesis (ACG) is a number of disorders that are the most severe form of congenital chondrodysplasia characterized with bones and cartilage malformation. Generally, characteristic of ACG is a small body, short limbs, and other skeletal abnormalities. As a result of infants with ACG their serious health problems, usually born prematurely, are stillborn, or die shortly after birth from respiratory failure. Currently 3 type variants of ACG such as ACG-1A, ACG-1B and ACG-2. ACG-1A appears to be autosomal recessive (AR), with thyroid hormone receptor interactor 11 (TRIP11) gen mutation, while ACG1B also appears to be AR, with diastrophic dysplasia sulfate transporter or DTDST (SLC26A2) gen mutation. ACG-2 is caused by autosomal dominant (AD), with type 2 collagen (COL2A1) gen mutation. ACG-1A had characterizid such as physis abnormal, vertebral bodies with unossified or smal and oval, skull poorly ossified, periodic acid–Schiff (PAS) stain positive chondrocyte inclusions finding in long bones. ACG-1B had physis abnormal, vertebral bodies with unossified or smal and oval, skull ossified, perichondrocyte collagen rings finding in long bones. ACG-2 also had physis abnormal, metaphyseal cupping, vertebral bodies with unossified or small and oval, enlarged chondrocyte lacunae.

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SLC26A2 (Diastrophic Dysplasia Sulfate Transporter) is Expressed in Developing and Mature Cartilage But Also in Other Tissues and Cell Types

Cited by 82 publications

References 21 publications

Expression of ion transport-associated proteins in human efferent and epididymal ducts

Expression of ion transport-associated proteins in human efferent and epididymal ducts

Congenital Chloride-losing Diarrhea Causing Mutations in the STAS Domain Result in Misfolding and Mistrafficking of SLC26A3

The genetic aspect and morphological appearance of achondrogenesis

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