Molecular cloning of KS, a novel rat gene expressed exclusively in the kidney

Hilgers, Karl F.; Nagaraj, Shashi; Karginova, Elena A.; Kazakova, Irina; Chevalier, Robert L.; Carey, Robert M.; Pentz, Ellen S.; Gomez, R. Ariel

doi:10.1046/j.1523-1755.1998.00143.x

Cited by 16 publications

(11 citation statements)

References 39 publications

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“…Some proteins with unknown or doubtful subcellular localization had 90 -100% mitochondrial prediction score with Mitopred or PSORT II (39), such as acid phosphatase 6 (with orthophosphoric monoesters dephosphorylation activity), kidney-specific protein (AMP binding), and ES1 homolog, which is annotated as potentially mitochondrial in the Swiss-Prot database. Interestingly the gene for "kidney-specific protein" that had been described previously to exhibit a unique kidneyspecific expression (40) was also associated with the liver matrix fraction in our study. Due to the high sensitivity of the mass spectrometry, it is likely that trace amounts of proteins were identified and quantitatively relevant in a relatively low protein density sample such as the intermembrane space.…”

Section: Accessionsupporting

confidence: 67%

Quantitative Proteomic Comparison of Rat Mitochondria from Muscle, Heart, and Liver

Forner

Foster

Campanaro

et al. 2006

Molecular & Cellular Proteomics

259

232

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Mitochondria, through oxidative phosphorylation, are the primary source of energy production in all tissues under aerobic conditions. Although critical to life, energy production is not the only function of mitochondria, and the composition of this organelle is tailored to meet the specific needs of each cell type. As an organelle, the mitochondrion has been a popular subject for proteomic analysis, but quantitative proteomic methods have yet to be applied to tease apart subtle differences among mitochondria from different tissues or muscle types. Here we used mass spectrometry-based proteomics to analyze mitochondrial proteins extracted from rat skeletal muscle, heart, and liver tissues. Based on 689 proteins identified with high confidence, mitochondria from the different tissues are qualitatively quite similar. However, striking differences emerged from the quantitative comparison of protein abundance between the tissues. Furthermore we applied similar methods to analyze mitochondrial matrix and intermembrane space proteins extracted from the same mitochondrial source, providing evidence for the submitochondrial localization of a number of proteins in skeletal muscle and liver. Several proteins not previously thought to reside in mitochondria were identified, and their presence in this organelle was confirmed by protein correlation profiling. Hierarchical clustering of microarray expression data provided further evidence that some of the novel mitochondrial candidates identified in the proteomic survey might be associated with mitochondria. These data reveal several important distinctions between mitochondrial and submitochondrial proteomes from skeletal muscle, heart, and liver Different mammalian tissues have distinct energy needs, and mitochondria morphology can vary widely, although the structure is not exclusively linked to respiration (1). Morphology and structure of mitochondria in mammalian skeletal muscle, heart, and liver are very different (2). In skeletal muscle mitochondria are distributed between sarcomeres and tightly embedded in the microfilaments (F-actin) and microtubules. Indeed the intimate association of mitochondria with the myofilaments minimizes diffusion distance and facilitates conversion of chemical energy to mechanical work. Mammalian skeletal muscle is a highly specialized tissue composed of fibers with a diverse range of properties. The aerobic type I fibers contain many mitochondria and rely on oxidative phosphorylation for ATP. Type IIa fibers are very rich in small mitochondria and are characterized by a high capacity for oxidative ATP generation. These mitochondria can only oxidize glycolytic products unlike those in type I fibers that can also utilize fatty acids and ketones. Type IIb fibers rely upon anaerobic glycolysis, contain few mitochondria, and have high levels of glycogen (3). Given these functional differences it is reasonable to assume that mitochondrial and mitochondria-related proteins are present in different amounts depending on the specific energy requirement...

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Section: Accessionsupporting

confidence: 67%

Quantitative Proteomic Comparison of Rat Mitochondria from Muscle, Heart, and Liver

Forner

Foster

Campanaro

et al. 2006

Molecular & Cellular Proteomics

259

232

View full text Add to dashboard Cite

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“…We reported previously that renal maturation is delayed by chronic complete UUO. This includes persistence of an immature pattern of glomerular maturation (7,8), microvascular renin distribution (7), and of tubular (25) and interstitial markers (11,38). In the present study, we showed that glomerular maturation is also delayed in the neonatal rat following partial UUO.…”

Section: Discussionsupporting

confidence: 52%

Angiotensin-converting enzyme inhibition aggravates renal interstitial injury resulting from partial unilateral ureteral obstruction in the neonatal rat

Chen¹,

Park²,

Forbes³

et al. 2007

American Journal of Physiology-Renal Physiology

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Congenital urinary tract obstruction is the most important cause of renal insufficiency in infants and children, and angiotensin-converting enzyme (ACE) inhibitors attenuate the progression of renal disease in adults. ACE inhibitors are increasingly utilized in children with progressive renal disease. Because angiotensin is necessary for normal renal development, we examined the effects of ACE inhibition both during and immediately following the period of postnatal nephrogenesis in the neonatal rat subjected to sham operation or partial unilateral ureteral obstruction (UUO) under general anesthesia within the first 48 h of life. Rats in group I received enalapril 30 mg/kg body wt (or vehicle) daily for the first 10 days, while in group II, the 10 days of treatment began 10 days after surgery. Kidneys were harvested at day 21 and analyzed for apoptosis (TUNEL), interstitial macrophages (ED-1 immunohistochemistry), myofibroblasts (α-smooth muscle actin), and collagen (Sirius red). Partial UUO delayed glomerular maturation and increased ipsilateral renal macrophage infiltration, α-smooth muscle actin and Sirius red staining. In group I, enalapril increased myofibroblast accumulation in sham-operated kidneys, but not in obstructed kidneys. In contrast, in group II, enalapril further increased macrophage, myofibroblast, and collagen accumulation following partial UUO. The relative abundance of components of the kallikrein-kinin system, measured by Western blot, was not altered by partial UUO in the 14- and 28-day-old rat. Thus, in contrast to its salutary effects at later ages, ACE inhibition can worsen injury to the partially obstructed kidney during renal maturation even after the completion of nephrogenesis.

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“…A literature review revealed the recent identification of a protein called KS (kidney specific) of the exact size as SA and sharing 55% homology at the amino acid level. 14 Over the epitope used to generate the SA106 antibody, 9/15 amino acids are common between the SA and KS (Figure 4), supporting the likelihood that the absence of SA in the kidneys of SA -/-mice was being obscured by the SA106 antibody binding to KS. This was confirmed by examining protein extracts from the liver, which expresses SA but does not express KS (Figure 3b and Hilgers et al 14 ).…”

Section: Discussionmentioning

confidence: 83%

“…14 Over the epitope used to generate the SA106 antibody, 9/15 amino acids are common between the SA and KS (Figure 4), supporting the likelihood that the absence of SA in the kidneys of SA -/-mice was being obscured by the SA106 antibody binding to KS. This was confirmed by examining protein extracts from the liver, which expresses SA but does not express KS (Figure 3b and Hilgers et al 14 ). Here, a protein of the size for SA was only detected in the livers of SA ϩ/ϩ mice, and again there was no evidence of a truncated protein.…”

Section: Discussionmentioning

confidence: 83%

“…6 Steady-state mRNA levels for SA, GAPDH (loading control), KS, 14 and renin (kidneys only) were assessed by standard Northern blotting, 6,13 using as probes a 1.6-kb rat SA cDNA, 6 a 29-mer complementary oligonucleotide to GAPDH, 6 a 361-bp cDNA (nucleotides 1134 to 1495) to the KS gene, 14 and a rat renin cDNA, 15 respectively. All probes were radioactively labeled with ␣ 32 P-dCTP.…”

Section: Rna Analysismentioning

confidence: 99%

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Analysis of the Role of the SA Gene in Blood Pressure Regulation by Gene Targeting

Walsh

Somody²,

Farrell³

et al. 2003

Hypertension

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Abstract-The SA gene is expressed in the proximal tubule of the kidney and may be involved in blood pressure (BP) regulation. However, direct evidence for this is lacking. We constructed and analyzed an SA-null mouse in which exons 2 and 3 of the SA gene (including the start codon) had been deleted by homologous recombination. Basal BP and BP changes in response to increased salt and to treatment with losartan were compared between mice homozygous for the targeted SA allele (SA -/-mice) and littermates carrying the wild-type allele (SA ϩ/ϩ mice). Molecular and biochemical analysis confirmed the lack of SA gene product in SA -/-mice. SA -/-mice grew normally, were fertile, and had no overt phenotype. With both indirect and direct techniques, basal BP was similar in SA -/-and SA ϩ/ϩ mice. A high salt diet for 4 weeks caused a significant increase in BP in SA -/-and SA ϩ/ϩ , mice but there was no difference between the 2 strains. Losartan caused a significant decrease in BP, but again the response was similar between SA -/-and SA ϩ/ϩ mice, as were their kidney renin mRNA levels. SA is not involved in the regulation of either basal or salt related BP, and the lack of differential effect in SA -/-mice is not a consequence of compensatory activation of the renin-angiotensin system.

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Molecular cloning of KS, a novel rat gene expressed exclusively in the kidney

Abstract: KS, a novel rat gene, exhibits a unique tissue-specific expression exclusively in mature kidneys. The data suggest KS may encode an adenosine monophosphate binding enzyme.

Cited by 16 publications

References 39 publications

Quantitative Proteomic Comparison of Rat Mitochondria from Muscle, Heart, and Liver

Quantitative Proteomic Comparison of Rat Mitochondria from Muscle, Heart, and Liver

Angiotensin-converting enzyme inhibition aggravates renal interstitial injury resulting from partial unilateral ureteral obstruction in the neonatal rat

Analysis of the Role of the SA Gene in Blood Pressure Regulation by Gene Targeting

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