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Search results for: Rabbit Anti-Phospho-WNK1(Thr60) Polyclonal Antibody

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#35560929   // To Up

Astrocyte Reactivity in Female Rats with Persistent Low Back Pain Following Spinal Mobilization.

Low back pain (LBP) is a physiologically complex and highly disabling condition with poorly understood pathophysiology. Glial reactivity has been reported in patients with chronic LBP and astrocyte reactivity has been suggested as a potential contributor to LBP chronicity. Spinal mobilization (SM) is a non-pharmacological approach with mild to moderate efficacy in treating LBP but physiological mechanisms responsible are unknown.
Carla Rigo Lima, Snigdhasree Avatapally, Peng Li, William Reed

2981 related Products with: Astrocyte Reactivity in Female Rats with Persistent Low Back Pain Following Spinal Mobilization.

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#35553817   // To Up

Immunohistochemical localization of receptor protein tyrosine phosphatase γ in mouse renal proximal tubule, thick ascending limb and distal convoluted tubule.

Most normal physiological processes require that both intracellular (i) and extracellular (o) pH be maintained within a tight range. pH is contingent on arterial (a) pH, which is determined by the ratio of the arterial carbon dioxide to the arterial bicarbonate concentration, [CO ] /[HCO ] . Pulmonary ventilation controls [CO ] . The kidney controls [HCO ] by adjusting HCO transport rates (J ) across the basal membranes of particular nephron epithelia into the blood to maintain normal pH , or compensate for an acid-base insult. In an effort to identify the sensor proteins for pH , [CO ] , or [HCO ] , our laboratory previously reported that, in isolated proximal tubules (PTs) from receptor protein tyrosine phosphatase γ (RPTPγ) knockout (KO) mice, J is insensitive to changes in the basolateral [CO ] or [HCO ]. Furthermore, RPTPγ-KO mice have a deficiency in defending against a whole-body metabolic acidosis. These data implicate RPTPγ as a major [CO ] or [HCO ] sensor. RPTPγ possesses an extracellular catalytically inactive carbonic-anhydrase-like domain (CALD) and fibronectin type III (FNIII) domain, a single transmembrane helix, and intracellular domains D1 and D2. Dimerization of RPTPγ presumably allows the inhibitory D2 of one monomer to inhibit the otherwise catalytically active D1 of the other monomer. Thus, the dimerization/monomerization state controls downstream signaling. We hypothesize that the binding of CO or HCO to the CALD alters the CALD conformation, thereby transmitting signals that control the dimerization status of RPTPγ and thereby regulate downstream effects on J . We hypothesize that RPTPγ is localized in nephron segments important for regulating HCO transport/reabsorption, in the basal membranes that face the blood. To determine the location of RPTPγ in wild-type mouse kidney cryosections, we use a chicken IgY anti-RPTPγ antibody (Ab) raised against an epitope within the FNIII domain, and co-stain with rabbit polyclonal Abs against the Na/HCO cotransporter (NBCe1-A) as a PT marker, the Na/K/Cl cotransporter 2 (NKCC2) as a thick ascending limb (TAL) marker, and the Na/Cl cotransporter (NCC) as a distal convoluted tubule (DCT) marker. Imaging sections by confocal microscopy, we observe in 3 WT mice that RPTPγ localizes primarily to the PT basal membrane. However, 54% of PTs (NBCe1-A positive) also exhibit apical RPTPγ staining of comparable intensity to the RPTPγ staining observed in the basal membrane. We also observe both apical and basal RPTPγ staining in Bowman's capsules. We stained additional sections from the same animals with a rabbit polyclonal primary Ab that targets the RPTPγ CALD domain. In these sections, co-stained with the anti-FNIII Ab, we similarly observe both apical and basal staining in PTs. We observe RPTPγ staining in a minority of TALs, and at much lower intensity than observed in the PT. We observe minimal to no RPTPγ staining in the DCT. We validated the specificity of the RPTPγ Abs on RPTPγ-KO kidney sections, which exhibit low background levels of fluorescence for both the anti-FNIII and anti-CALD Abs. In conclusion, these data confirm RPTPγ expression in PT basal membranes, but also describe the first examples of apical RPTPγ expression in renal epithelia.
Abhi N Deverakonda, Eva Gilker, Walter F Boron, Fraser J Moss

2953 related Products with: Immunohistochemical localization of receptor protein tyrosine phosphatase γ in mouse renal proximal tubule, thick ascending limb and distal convoluted tubule.

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#35552054   // To Up

MOTS-c protein expression increases following aerobic exercise training and remains elevated during detraining.

Mitochondrial open reading frame of the 12S rRNA-c (MOTS-c) is a mitochondrial-derived peptide that is released into the circulation following intense physical activity and, purportedly, has systemic impacts on energy metabolism and insulin sensitivity. Exogenous administration of MOTS-c in rodent models enhances physical activity / endurance and reduces fat mass in aged mice through the regulation of, in part, the glycolysis / pentose phosphate pathway and amino acid metabolism. Considering that mitochondrial volume and mitochondrial DNA copy number increase following chronic aerobic exercise training, we hypothesized that MOTS-c expression also would be elevated in exercise-trained skeletal muscle. MOTS-c protein expression from phenotypically mixed plantaris muscles of adult female Sprague Dawley rats were compared from six conditions: sedentary (SED; n=11), voluntary exercise training for four (EX4; n=9), six (EX6; n=6), or eight weeks (EX8; n=8), and detraining after four (DETR4) or six (DETR6) weeks, which followed four or six weeks of exercise training, respectively. Total running distances were ~551±61, 371±94, 560±71, 321±44, and 519±27 km for EX4, EX6, EX8, DETR4 and DETR6, respectively. DETR4 rat running distance was significantly lower than EX4, EX8, and DETR6 rats (p<0.01). Total muscle protein homogenate was isolated from mid-belly muscle chunks and separated using 15% SDS-PAGE gels (10 μg/sample). Following transfer, membranes were incubated with a custom rabbit anti-rat MOTS-c polyclonal antibody, developed, scanned, stripped and re-probed for GAPDH as a loading control. MOTS-c protein was significantly elevated from SED (set at 100%) to 188±61, 158±37, 212±27, 168±29, 223±36% in EX4, EX6, EX8, DETR4 and DETR6, respectively (p<0.05). Furthermore, preliminary findings indicate that MOTS-c is present exclusively within the cytoplasm of skeletal muscle and not compartmentalized within the nuclei or mitochondria. Given that long-term aerobic exercise augments mitochondrial volume within skeletal muscle, our data suggest that the observed increase in MOTS-c protein in the present study parallels this mitochondrial adaptation to aerobic physical activity. Taken together, these findings indicate that a more aerobically-trained individual would have an enhanced MOTS-c presence within skeletal muscle and, therefore, a greater potential to regulate energy and insulin sensitivity when MOTS-c is released systemically; additionally, the potential benefits of MOTS-c are sustained during a period of physical inactivity (e.g., detraining) following exercise training.
Beau R Pullman, Jon-Philippe K Hyatt

1085 related Products with: MOTS-c protein expression increases following aerobic exercise training and remains elevated during detraining.

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#35457172   2022/04/14 To Up

Detection of VAMP Proteolysis by Tetanus and Botulinum Neurotoxin Type B In Vivo with a Cleavage-Specific Antibody.

Tetanus and Botulinum type B neurotoxins are bacterial metalloproteases that specifically cleave the vesicle-associated membrane protein VAMP at an identical peptide bond, resulting in inhibition of neuroexocytosis. The minute amounts of these neurotoxins commonly used in experimental animals are not detectable, nor is detection of their VAMP substrate sensitive enough. The immune detection of the cleaved substrate is much more sensitive, as we have previously shown for botulinum neurotoxin type A. Here, we describe the production in rabbit of a polyclonal antibody raised versus a peptide encompassing the 13 residues C-terminal with respect to the neurotoxin cleavage site. The antibody was affinity purified and found to recognize, with high specificity and selectivity, the novel N-terminus of VAMP that becomes exposed after cleavage by tetanus toxin and botulinum toxin type B. This antibody recognizes the neoepitope not only in native and denatured VAMP but also in cultured neurons and in neurons in vivo in neurotoxin-treated mice or rats, suggesting the great potential of this novel tool to elucidate tetanus and botulinum B toxin activity in vivo.
Federico Fabris, Petra Šoštarić, Ivica Matak, Thomas Binz, Anna Toffan, Morena Simonato, Cesare Montecucco, Marco Pirazzini, Ornella Rossetto

2086 related Products with: Detection of VAMP Proteolysis by Tetanus and Botulinum Neurotoxin Type B In Vivo with a Cleavage-Specific Antibody.