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AQP2 is found in the apical cell membranes of the kidneys collecting duct principal cells and in intracellular vesicles located throughout the cell. It is the only aquaporin regulated by vasopressin. The basic job of aquaporin 2 is to reabsorb water from the urine while its being removed from the blood by the kidney. Aquaporin 2 is in kidney epithelial cells and usually lies dormant in intracellular vesicle membranes. When it is needed, vasopressin binds to the cell surface vasopressin receptor thereby activating a signaling pathway that causes the aquaporin 2 containing vesicles to fuse with the plasma membrane, so the aquaporin 2 can be used by the cell. This aquaporin is regulated in two ways by the peptide hormone vasopressin: short-term regulation (minutes) through trafficking of AQP2 vesicles to the apical region where they fuse with the apical plasma membrane long-term regulation (days) through an increase in AQP2 gene expression. This aquaporin is also regulated by food intake. Fasting ...
Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
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Aquaporin 4 is found in the basolateral cell membrane of principal collecting duct cells and provide a pathway for water to exit these cells. AQP4 is constitutively expressed. AQP4 is expressed in astrocytes and are upregulated by direct insult to the central nervous system. ...
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Aqp4 - Aqp4 (untagged) - Mouse aquaporin 4 (cDNA clone MGC:37514 IMAGE:4985265), (10ug) available for purchase from OriGene - Your Gene Company.
TY - JOUR. T1 - Aquaporin water channels - From atomic structure to clinical medicine. AU - Agre, Peter. AU - King, Landon S.. AU - Yasui, Masato. AU - Guggino, Wm B.. AU - Ottersen, Ole Petter. AU - Fujiyoshi, Yoshinori. AU - Engel, Andreas. AU - Nielsen, Søren. PY - 2002/7/1. Y1 - 2002/7/1. N2 - The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water channel protein. AQP1 is selectively permeated by water driven by osmotic gradients. The atomic structure of human AQP1 has recently been defined. Each subunit of the tetramer contains an individual aqueous pore that permits single-file passage of water molecules but interrupts the hydrogen bonding needed for passage of protons. At least 10 mammalian aquaporins have been identified, and these are selectively permeated by water (aquaporins) or water plus glycerol (aquaglyceroporins). The sites of expression ...
TY - JOUR. T1 - Expression and subcellular localization of aquaporin water channels in the polarized hepatocyte cell line, WIF-B. AU - Gradilone, Sergio A.. AU - Tietz, Pamela S.. AU - Splinter, Patrick L.. AU - Marinelli, Raúl A.. AU - LaRusso, Nicholas F.. PY - 2005/8/18. Y1 - 2005/8/18. N2 - Background: Recent data suggest that canalicular bile secretion involves selective expression and coordinated regulation of aquaporins (AQPs), a family of water channels proteins. In order to further characterize the role of AQPs in this process, an in vitro cell system with retained polarity and expression of AQPs and relevant solute transporters involved in bile formation is highly desirable. The WIF-B cell line is a highly differentiated and polarized rat hepatoma/human fibroblast hybrid, which forms abundant bile canalicular structures. This cell line has been reported to be a good in vitro model for studying hepatocyte polarity. Results: Using RT-PCR, immunoblotting and confocal immunofluorescence, ...
Aquaporin-5 is a protein that in humans is encoded by the AQP5 gene. Aquaporin 5 (AQP5) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 5 plays a role in the generation of saliva, tears and pulmonary secretions. AQP0, AQP2, AQP5, and AQP6 are closely related and all map to 12q13. Aquaporin GRCh38: Ensembl release 89: ENSG00000161798 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000044217 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Lee MD, Bhakta KY, Raina S, Yonescu R, Griffin CA, Copeland NG, Gilbert DJ, Jenkins NA, Preston GM, Agre P (Jun 1996). The human Aquaporin-5 gene. Molecular characterization and chromosomal localization. J Biol Chem. 271 (15): 8599-604. doi:10.1074/jbc.271.15.8599. PMID 8621489. Entrez Gene: AQP5 aquaporin 5. Verkman AS (2003). Role of aquaporin water channels in eye function. Exp. Eye Res. 76 (2): 137-43. ...
Semantic Scholar extracted view of Aquaporin water channels in liver: their significance in bile formation. by Raúl Alberto Marinelli et al.
RATIONALE: Cevimeline may be effective in treating dry mouth that is caused by radiation therapy for head and neck cancer. It is not yet known if cevimeline is more effective than no therapy in treating dry mouth caused by radiation therapy.. PURPOSE: Randomized phase III trial to determine the effectiveness of cevimeline in treating patients who have dryness of the mouth caused by radiation therapy for head and neck cancer. ...
Aquaporins (AQPs) are membrane proteins that enable water transport across cellular plasma membranes in response to osmotic gradients. Phenotypic analyses have revealed important physiological roles for AQPs, and the potential for AQP water channel modulators in various disease states has been proposed. For example, AQP1 is overexpressed in tumor microvessels, and this correlates with higher metastatic potential and aggressiveness of the malignancy. Chemical modulators would help in identifying the precise contribution of water channel activity in these disease states. These inhibitors would also be important therapeutically, e.g., in anti-cancer treatment. This perceived importance contrasts with the lack of success of high-throughput screens (HTS) to identify effective and specific inhibitors of aquaporins. In this paper, we have screened a library of 1500
TY - JOUR. T1 - Role of Aquaporin 0 in lens biomechanics. AU - Sindhu Kumari, S.. AU - Gupta, Neha. AU - Shiels, Alan. AU - FitzGerald, Paul G. AU - Menon, Anil G.. AU - Mathias, Richard T.. AU - Varadaraj, Kulandaiappan. PY - 2015/4/19. Y1 - 2015/4/19. N2 - Abstract Maintenance of proper biomechanics of the eye lens is important for its structural integrity and for the process of accommodation to focus near and far objects. Several studies have shown that specialized cytoskeletal systems such as the beaded filament (BF) and spectrin-actin networks contribute to mammalian lens biomechanics; mutations or deletion in these proteins alters lens biomechanics. Aquaporin 0 (AQP0), which constitutes ∼45% of the total membrane proteins of lens fiber cells, has been shown to function as a water channel and a structural cell-to-cell adhesion (CTCA) protein. Our recent ex vivo study on AQP0 knockout (AQP0 KO) mouse lenses showed the CTCA function of AQP0 could be crucial for establishing the refractive ...
Aquaporin 1: Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen.
Aquaporin A/S is a global cleantech company located in Kongens Lyngby, Denmark. Aquaporin is dedicated to revolutionizing water purification through the use of industrial biotechn
The researchers showed that this technique was successful in monitoring gene expression in a brain tumor in mice. After implanting the tumor, they gave the mice a drug to trigger the tumor cells to express the aquaporin reporter gene, which made the tumor look darker in MRI images.. Overexpression of aquaporin has no negative impact on cells because it is exclusive to water and simply allows the molecules to go back and forth across the cell membrane, Shapiro says. Under normal physiological conditions the number of water molecules entering and exiting an aquaporin-expressing cell is the same, so that the total amount of water in each cell does not change. Aquaporin is a very convenient way to genetically change the way that cells look under MRI.. Though the work was done in mice, it has the potential for clinical translation, according to Shapiro. Aquaporin is a naturally occurring gene and will not cause an immune reaction. Previously developed reporter genes for MRI have been much more ...
Photo: Dr. Alison Bauer]. In addition to decreased overall tumor burden, mice lacking Ereg also showed reduced inflammation and, in cell studies, both human and mouse lung epithelial cells treated with Ereg had significant increases in wound healing.. Because Ereg is under-studied - as compared to its cousin, EGF - much of the science surrounding this growth factor is still poorly understood. Despite challenges, researchers believe Ereg to contain exciting opportunities as a promising biomarker.. Full story here.. ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
collections, groups of modules structured into books or course notes, or for other uses. Our open license allows for free use and reuse of all our content. ...
Marinelli RA, Pham L, Agre P, La Russo NF. Secretin promotes osmotic water transport in rat cholangiocytes by incresing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1. J Biol Chem 1997; 272: 12984-12988 ...
Aquaporin membrane protein, molecular model. Computer illustration showing the structure of a molecule of the human aquaporin 1 protein (blue, and white ribbon). Aquaporins are membrane proteins that form channels (centre) that help water molecules (red and white spheres) pass in and out of cells. Unlike ion channels, aquaporins help prevent ions and other dissolved substances carrying electrical charge from entering the cell, as they only allow lone water molecules or certain uncharged solutes to pass through. This helps maintain the electrochemical potential of the cell membrane. - Stock Image C035/5236
TY - JOUR. T1 - Identification of a novel aquaporin, AQP12, expressed in pancreatic acinar cells. AU - Itoh, Tomohiro. AU - Rai, Tatemitsu. AU - Kuwahara, Michio. AU - Ko, Shigeru B.H.. AU - Uchida, Shinichi. AU - Sasaki, Sei. AU - Ishibashi, Kenichi. N1 - Funding Information: We thank N. Ozaki (Nagoya university, Japan) for his skillful technical assistance in isolation of pancreatic islet. This work was supported by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan.. PY - 2005/5/13. Y1 - 2005/5/13. N2 - Members of the aquaporin (AQP) water channel family are widely distributed in various tissues and contribute to the water permeability of epithelial and endothelial cells. Currently 11 members of the AQP family (AQP0-10) have been reported in mammals. Here we report the identification of AQP12, which we found by performing a BLAST program search. Northern blot analysis revealed that AQP12 was specifically expressed in the pancreas. Further analysis by in ...
After producing a recombinant form of AqpZ in E. coli, the proteins were crystallized--capturing five water molecules inside--and then analyzed by state-of-the-art high-resolution X-ray diffraction techniques. The architecture of aquaporin Z is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel. The outer membrane and cytoplasmic ends of the channel are wider than the interior, which is long and narrow. This structure demonstrates that aquaporin selectivity arises in part from erecting a physical barrier: small molecules, like water, can easily pass, but larger ones simply cant fit. And the strategic positioning of amino acid residues with hydrophilic or hydrophobic properties along the channel helps police the influx of molecules based on their affinity for water. While it seems two amino acid chains located in the middle of the channel also provide a water-friendly surface, Stroud et al. say they play a more intriguing role. Noting that the ...
Aquaporins facilitate the diffusion of water across cell membranes. We previously showed that acid pH or low Ca2+ increase the water permeability of bovine AQP0
I think it will be found that aquaporin 3 will be the item of interest (1).. Aquaporin 3 is found in normal skeletal myofibres (2).. I suspect it will be found that the problem is not a mutation, but something interfering with the normal proper function of the aqp3 channels.. Aquaporin 3 is, in addition to being a water channel, also an arsenic transporter.. Arsenic has been implicated in Alzheimers in at least a few instances. For example, this statement appears in Reference 3 below:. Arsenic can induce apoptosis in cortical neurons of rats. This process is based on the activation of JNK3 and p38 MAPK by arsenic...[which] can activate p38 MAPK and JNK3..... And the title of the last paper speaks for itself: Arsenic exposure may be a risk factor for Alzheimers disease.. ...
Polyclonal antibody for AQUAPORIN 3/AQP3 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. AQUAPORIN 3/AQP3 information: Molecular Weight: 31544 MW; Subcellular Localization: Basolateral cell membrane; Multi-pa
Aquaporin 10 antibody, C-term (aquaporin 10) for WB. Anti-Aquaporin 10 pAb (GTX45889) is tested in Human samples. 100% Ab-Assurance.
Purpose: The expression of aquaporin water channel genes are shown to be affected in several pathological conditions of retina, such as in diabetic retinopathy, retinal ischemia and in autoimmune uveitis. Human native retinal pigment epithelial (RPE) cells and immortalized human RPEs are formerly shown to express aquaporins, still the expression of aquaporins in stem cell derived RPE have not been previously elucidated. The objective of this study was to determine the expression of several aquaporin genes (aquaporin1,- 3, -4, -5, -6, -7, -10, -11 and -12) and assess the localization of aquaporin 1 water channel protein in human embryonic (hESCs) and induced pluripotent stem cells (hiPSCs) derived RPE cells.. Methods: hESC- and hiPSC derived RPE cells were grown as monolayer in serum-free media. The expression of aquaporin genes was determined with qRT-PCR. The localization of AQP1-protein was studied with confocal microscopy. Finally, the functionality of aquaporins was assessed with dye ...
With Aquaporin Inside™ Reverse Osmosis membranes, water treatment can be done with lower energy consumption compared to conventional membrane technology. The benefit comes from the aquaporin proteins which are very efficient in transporting water. This enables the water treatment plant to increase the capacity of treated wastewater without increasing the energy consumption, or remaining at the same capacity level while lowering the energy consumption. At the same time, Aquaporin membranes has the potential to remove also small, neutral compounds such as micro pollutants/trace organics, improving re-use water quality.. Aquaporin Inside™ Forward Osmosis ...
Looking for online definition of Aquaporin1 or what Aquaporin1 stands for? Aquaporin1 is listed in the Worlds largest and most authoritative dictionary database of abbreviations and acronyms
Background Aquaporins (Aqps) are integral membrane proteins that facilitate the transport of water and small solutes across cell membranes. Among vertebrate species, Aqps are highly conserved in both gene structure and amino acid sequence. These proteins are vital for maintaining water homeostasis in living organisms, especially for aquatic animals such as teleost fish. Studies on teleost Aqps are mainly limited to several model species with diploid genomes. Common carp, which has a tetraploidized genome, is one of the most common aquaculture species being adapted to a wide range of aquatic environments. The complete common carp genome has recently been released, providing us the possibility for gene evolution of aqp gene family after whole genome duplication. Results In this study, we identified a total of 37 aqp genes from common carp genome. Phylogenetic analysis revealed that most of aqps are highly conserved. Comparative analysis was performed across five typical vertebrate genomes. We found that
Aquaporins play a direct role in plant water relation under salt stress, but the effects of 5-aminolevulinic acid (ALA) on aquaporin gene expression in salt-treated plants remain unknown. This study investigated the potential effects of exogenous ALA (50 mg/dm3) on aquaporin expression levels under salt stress (75 mM NaCl) in the salt-sensitive (Jinchun No.4) and the relatively salt-tolerant cucumber (Jinyou No.1) seedlings.
Müller glial cells are important regulators of physiological function of retina. In a model disease of retinal inflammation and spontaneous recurrent uveitis in horses (ERU), we could show that retinal Müller glial cells significantly change potassium and water channel protein expression during autoimmune pathogenesis. The most significantly changed channel protein in neuroinflammatory ERU was aquaporin 11 (AQP11). Aquaporins (AQP, 13 members) are important regulators of water and small solute transport through membranes. AQP11 is an unorthodox member of this family and was assigned to a third group of AQPs because of its difference in amino acid sequence (conserved sequence is only 11 %) and especially its largely unknown function. In order to gain insight into the distribution, localization, and function of AQP11 in the retina, we first developed a novel monoclonal antibody for AQP11 enabling quantification, localization, and functional studies. In the horse retina, AQP11 was exclusively expressed
An important thing in our body is the saliva. It keeps our mouth hydrated always without our knowledge. What will happen to our mouth and body if there is no saliva?. The work of saliva is to help us digest the food and it also controls the bacteria and fungi in our body.. Bacteria will increase if the saliva secretion in our mouth reduces. Tongue dryness, gum crack might occur if there is less saliva in the mouth. Let us now understand the truth behind saliva secretion and the reason for less secretion.. Do you want white teeth…? Eat this!!! ...
Purpose: : To demonstrate in the conjunctiva the presence of aquaporin type 5 (AQP5), a water channel homologue found in the apical membrane of several tissues including the cornea. Presently, there are no reports indicating as to which AQP might be expressed apically in the conjunctiva; only AQP3 has been identified in the lateral membranes of rat and human conjunctival epithelia. Because we had data from gene-expression microarray assays (Turner; ARVO 2004) indicating message for AQP5 in the human conjunctiva, tissue samples from human, as well as from rats and rabbits (given the ease of their procurement), were analyzed to confirm that the AQP5 protein was indeed expressed in mammalian conjunctivae. Methods: : Goat polyclonal IgG against AQP5 was purchased commercially and used in immunoblotting and immunohistochemical techniques to identify and localize the water channel in rat, rabbit and human epithelia. Results: : Immunoblot analysis of rabbit bulbar-plus-palpebral plasma membrane ...
Cevimeline is a parasympathomimetic and muscarinic agonist, with particular effect on M3 receptors. It is indicated by the Food and Drug Administration for the treatment of dry mouth associated with Sjögrens syndrome.
Youll soon see a new drug for severe dry mouth called Evoxac (EE-vo-zak, cevimeline). ... Learn more with Pharmacists Letter.
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Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP ...
摘要(Abstract): 目的探讨头孢曲松钠在水通道蛋白4(AQP4)抗体诱导的星形胶质细胞损伤中的作用以及机制。方法常规体外培养新生SD大鼠大脑皮质细胞,将培养的细胞分为4组,分别加入健康人血清(对照组)、AQP4抗体阳性患者血清、头孢曲松钠+AQP4抗体阳性血清以及单纯头孢曲松钠。细胞培养24h后采用免疫组织化荧光染色观察不同组星形胶质细胞数目的变化,采用比色法测定上清液谷氨酸浓度以及免疫印迹分析谷氨酸转运体-1(GLT-1)蛋白表达水平。结果和对照组比较,AQP4抗体阳性血清组星形胶质细胞数目和谷氨酸转运体-1(GLT-1)蛋白表达明显减少,上清液谷氨酸浓度明显增高(均 ...
The main role of salivary glands (SG) is the production and secretion of saliva, in which aquaporins (AQPs) play a key role by ensuring water flow. The AQPs are transmembrane channel proteins permeable to water to allow water transport across cell membranes according to osmotic gradient. This review gives an insight into SG AQPs. Indeed, it gives a summary of the expression and localization of AQPs in adult human, rat and mouse SG, as well as of their physiological role in SG function. Furthermore, the review provides a comprehensive view of the involvement of AQPs in pathological conditions affecting SG, including Sjögren’s syndrome, diabetes, agedness, head and neck cancer radiotherapy and SG cancer. These conditions are characterized by salivary hypofunction resulting in xerostomia. A specific focus is given on current and future therapeutic strategies aiming at AQPs to treat xerostomia. A deeper understanding of the AQPs involvement in molecular mechanisms of saliva secretion and diseases
This paper strongly supports the conclusion that AQP0 has a high permeability mode and a low permeability mode. How do these two modes differ? Available structural data on the nature of the water-filled pore through AQP1 and the glycerol facilitator suggest a possible answer. For both, water and glycerol must move through the pore by single-file diffusion. The crystal structure and molecular dynamic simulations suggest that there are multiple water molecules in the pore. There are ∼6 waters seen in the narrow constriction of the pore in the X-ray structure (Sui et al., 2001), and molecular dynamic simulations suggest that there are ∼7 or 8 water molecules moving in concert in the single-file portion of the pore (Tajkhorshid et al., 2002; Zhu et al., 2004). The lack of passage of ionic current through AQP0 and AQP1 is explained by electrostatic considerations that strongly inhibit the movement of protons into the NPA region or hydroxyls into regions flanking either side of the NPA region (de ...
Aquaporin (AQP) proteins comprise a group of membrane intrinsic proteins (MIPs) that are responsible for transporting water and other small molecules, which is crucial for plant survival under stress conditions including salt stress. Despite the vital role of AQPs, little is known about them in cucumber (Cucumis sativus L.). In this study, we identified 39 aquaporin-encoding genes in cucumber that were separated by phylogenetic analysis into five sub-families (PIP, TIP, NIP, SIP, and XIP). Their substrate specificity was then assessed based on key amino acid residues such as the aromatic/Arginine (ar/R) selectivity filter, Frogers positions, and specificity-determining positions. The putative cis-regulatory motifs available in the promoter region of each AQP gene were analyzed and results revealed that their promoter regions contain many abiotic related cis-regulatory elements. Furthermore, analysis of previously released RNA-seq data revealed tissue- and treatment-specific expression patterns of
Aquaporin 8 (AQP8) is a water channel protein. Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). Aquaporin 8 mRNA is found in pancreas and colon but not other tissues. [provided by RefSeq, Jul 2008 ...
Bronchopulmonary dysplasia (BPD) remains a major respiratory illness in extremely premature infants. The biological mechanisms leading to BPD are not fully understood, although an arrest in lung development has been implicated. The current study aimed to investigate the occurrence of autophagy in the developing mouse lung and its regulatory role in airway branching and terminal sacculi formation. We found 2 windows of epithelial autophagy activation in the developing mouse lung, both resulting from AMPK activation. Inhibition of AMPK-mediated autophagy led to reduced lung branching in vitro. Conditional deletion of beclin 1 (Becn1) in mouse lung epithelial cells (Becn1Epi-KO), either at early (E10.5) or late (E16.5) gestation, resulted in lethal respiratory distress at birth or shortly after. E10.5 Becn1Epi-KO lungs displayed reduced airway branching and sacculi formation accompanied by impaired vascularization, excessive epithelial cell death, reduced mesenchymal thinning of the interstitial ...
Bronchopulmonary dysplasia (BPD) remains a major respiratory illness in extremely premature infants. The biological mechanisms leading to BPD are not fully understood, although an arrest in lung development has been implicated. The current study aimed to investigate the occurrence of autophagy in the developing mouse lung and its regulatory role in airway branching and terminal sacculi formation. We found 2 windows of epithelial autophagy activation in the developing mouse lung, both resulting from AMPK activation. Inhibition of AMPK-mediated autophagy led to reduced lung branching in vitro. Conditional deletion of beclin 1 (Becn1) in mouse lung epithelial cells (Becn1Epi-KO), either at early (E10.5) or late (E16.5) gestation, resulted in lethal respiratory distress at birth or shortly after. E10.5 Becn1Epi-KO lungs displayed reduced airway branching and sacculi formation accompanied by impaired vascularization, excessive epithelial cell death, reduced mesenchymal thinning of the interstitial ...
Objective: It is well known that VEGFR expression is correlated with peritumoral brain edema in meningiomas. Also Aquaporin4 seems to induce the perifocal edema. In our study we analyzed the correlation of VEGFR1, VEGFR2 and Aquaporin4 to the brain edema. Additionally a potential correlation between[for full text, please go to the a.m. URL ...
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Hi, Bit more than a month ago my mom developed burning sensation on her back and stomach, she went to a doc but he said its nothing lifetreatening and she waited for for her turn for the tests, it was like this for a week or two. Few weeks ago the burning sensation became too much to bear and my mom went to a hospital. They took her in and the next day she had issues walking and day later she couldnt walk on her own at all. After a few days they put her on some steroid IV thing for
Pringle S, Maimets M, van der Zwaag M, Stokman MA, van Gosliga D, Zwart E, Witjes MJ, de Haan G, van Os R, Coppes RP. (2016) Human Salivary Gland Stem Cells Functionally Restore Radiation Damaged Salivary Glands. Stem Cells.. Back to previous page ...
Immunohistochemistry: STK39 Antibody [NBP2-49347] - Staining of human salivary gland shows strong cytoplasmic and nuclear positivity in glandular cells ...