S100 Calcium Binding Protein G
EF Hand Motifs
Amyloid beta-Protein Precursor
Energy-based de novo protein folding by conformational space annealing and an off-lattice united-residue force field: application to the 10-55 fragment of staphylococcal protein A and to apo calbindin D9K. (1/704)The conformational space annealing (CSA) method for global optimization has been applied to the 10-55 fragment of the B-domain of staphylococcal protein A (protein A) and to a 75-residue protein, apo calbindin D9K (PDB ID code), by using the UNRES off-lattice united-residue force field. Although the potential was not calibrated with these two proteins, the native-like structures were found among the low-energy conformations, without the use of threading or secondary-structure predictions. This is because the CSA method can find many distinct families of low-energy conformations. Starting from random conformations, the CSA method found that there are two families of low-energy conformations for each of the two proteins, the native-like fold and its mirror image. The CSA method converged to the same low-energy folds in all cases studied, as opposed to other optimization methods. It appears that the CSA method with the UNRES force field, which is based on the thermodynamic hypothesis, can be used in prediction of protein structures in real time. (+info)
Expression of calcium binding protein D-9k messenger RNA in the mouse uterine endometrium during implantation. (2/704)To investigate the molecular mechanisms of implantation, we constructed a cDNA library of mouse uteri enriched with pregnancy-induced genes by subtractive hybridization and polymerase chain reaction (PCR). One of the isolated clones was the cDNA for the calcium binding protein D-9k (Cabp9k), which is considered to regulate intracytoplasmic concentration and transport of free calcium ions. Northern blot and in-situ hybridization analyses demonstrated that the Cabp9k mRNA was expressed in the endometrial epithelia, both luminal and glandular, in the uterus at the time of implantation. On pregnancy day 5 it was detected in the luminal, but not in the glandular, epithelia. In the oophorectomized adult mice, progesterone enhanced Cabp9k mRNA expression in the uterus, whereas oestrogen did not. Consistent with this, a nucleotide change was identified in the first intron of mouse Cabp9k gene corresponding to the oestrogen responsive element in the rat Cabp9k gene. Transfer of embryos into the uterine cavity of pseudopregnant mice reduced the expression of Cabp9k mRNA in the glandular epithelium, suggesting that Cabp9k mRNA expression is also regulated by embryonal signal(s). These findings demonstrated that Cabp9k mRNA is expressed in the endometrial epithelia during the implantation period under the control of progesterone and the presence of embryo, and suggest that CaBP9k plays a role in implantation by regulating the local calcium concentrations. (+info)
Distribution of cholinergic contacts on Renshaw cells in the rat spinal cord: a light microscopic study. (3/704)1. Cholinergic terminals in the rat spinal cord were revealed by immunohistochemical detection of the vesicular acetycholine transporter (VAChT). In order to determine the relationships of these terminals to Renshaw cells, we used dual immunolabelling with antibodies against gephyrin or calbindin D28k to provide immunohistochemical identification of Renshaw cells in lamina VII of the ventral horn. 2. A total of 50 Renshaw cells were analysed quantitatively using a computer-aided reconstruction system to provide accurate localization of contact sites and determination of somatic and dendritic surface area. Dendrites could be traced for up to 413 microm from the soma in calbindin D28k-identified Renshaw cells and up to 184 microm in gephyrin-identified cells. 3. A total of 3330 cholinergic terminals were observed on 50 Renshaw cells, with a range of 21-138 terminal appositions per cell (mean 66.6 +/- 25.56 contacts per cell). The vast majority (83.5 %) of the terminals were apposed to dendrites rather than the soma. The overall density of cholinergic contacts increased from a little above 1 per 100 microm2 on the soma and initial 25 microm of proximal dendrites to 4-5 per 100 microm2 on the surface of dendritic segments located 50-250 microm from the soma. Single presynaptic fibres frequently formed multiple contacts with the soma and/or dendrites of individual Renshaw cells. 4. VAChT-immunoreactive terminals apposed to Renshaw cells varied in size from 0.6 to 6.9 microm in diameter (mean 2.26 +/- 0.94; n = 986) and were on average smaller than the cholinergic C-terminals apposed to motoneurones, but larger than VAChT-immunoreactive terminals contacting other ventral horn interneurones. 5. The high density and relatively large size of many cholinergic terminals on Renshaw cells presumably correlates with the strong synaptic connection between motoneurones and Renshaw cells. The fact that the majority of contacts are distributed over the dendrites makes the motoneurone axon collateral input susceptible to inhibition by the prominent glycinergic inhibitory synapses located on the soma and proximal dendrites. The relative positions and structural features of the excitatory cholinergic and inhibitory glycinergic synapses may explain why Renshaw cells, although capable of firing at very high frequency following motor axon stimulation, appear to fire at relatively low rates during locomotor activity. (+info)
Molecular identification of the apical Ca2+ channel in 1, 25-dihydroxyvitamin D3-responsive epithelia. (4/704)In mammals, the extracellular calcium concentration is maintained within a narrow range despite large variations in daily dietary input and body demand. The small intestine and kidney constitute the influx pathways into the extracellular Ca2+ pool and, therefore, play a primary role in Ca2+ homeostasis. We identified an apical Ca2+ influx channel, which is expressed in proximal small intestine, the distal part of the nephron and placenta. This novel epithelial Ca2+ channel (ECaC) of 730 amino acids contains six putative membrane-spanning domains with an additional hydrophobic stretch predicted to be the pore region. ECaC resembles the recently cloned capsaicin receptor and the transient receptor potential-related ion channels with respect to its predicted topology but shares less than 30% sequence homology with these channels. In kidney, ECaC is abundantly present in the apical membrane of Ca2+ transporting cells and colocalizes with 1,25-dihydroxyvitamin D3-dependent calbindin-D28K. ECaC expression in Xenopus oocytes confers Ca2+ influx with properties identical to those observed in distal renal cells. Thus, ECaC has the expected properties for being the gatekeeper of 1,25-dihydroxyvitamin D3-dependent active transepithelial Ca2+ transport. (+info)
Immunohistological studies of metabotropic glutamate receptor subtype 6-deficient mice show no abnormality of retinal cell organization and ganglion cell maturation. (5/704)Immature retinal ganglion cells (RGCs) initially show a multistratified dendritic pattern, and, during the postnatal period, these dendrites gradually monostratify into ON and OFF sublaminae. The selective agonist of group III metabotropic glutamate receptors (mGluR), L-2-amino-4-phosphonobutyrate (L-AP-4), hyperpolarizes ON bipolar cells and reduces glutamate release. On the basis of L-AP-4-evoked inhibitory effects on ON-OFF segregation of developing RGCs, it has been hypothesized that glutamate-mediated synaptic activity is crucial for formation of the ON-OFF network. Gene-targeted ablation of mGluR6 specifically expressed in ON bipolar cells blocks normal ON responses but has been predicted to enhance glutamate release from ON bipolar cells. The mGluR6 knock-out mouse therefore provides a unique opportunity to investigate whether glutamate release and ON responses are important factors in the development of ON-OFF segregation. The combination of several different morphological analyses indicates that ON bipolar cells, as well as several distinct amacrine cells, in mGluR6 knock-out mice are normally distributed and correctly extend their terminals to defined retinal laminae. Importantly, both alpha and delta RGCs in adult mGluR6 knock-out mice are found monostratified into cell type-specific layers. Furthermore, no difference between wild-type and mGluR6 knock-out mice is observed in the maturation and dendritic stratification of developing RGCs. Hence, despite a deficit in normal ON responses, mGluR6 deficiency causes no abnormality in the retinal cellular organization nor in the stratifications of both ON bipolar cells and developing and mature RGCs. Based on these findings, we discuss several possible mechanisms that may underlie ON-OFF segregation of RGCs. (+info)
Expression of type 2 iodothyronine deiodinase in hypothyroid rat brain indicates an important role of thyroid hormone in the development of specific primary sensory systems. (6/704)Thyroid hormone is an important epigenetic factor in brain development, acting by modulating rates of gene expression. The active form of thyroid hormone, 3,5,3'-triiodothyronine (T3) is produced in part by the thyroid gland but also after 5'-deiodination of thyroxine (T4) in target tissues. In brain, approximately 80% of T3 is formed locally from T4 through the activity of the 5'-deiodinase type 2 (D2), an enzyme that is expressed mostly by glial cells, tanycytes in the third ventricle, and astrocytes throughout the brain. D2 activity is an important point of control of thyroid hormone action because it increases in situations of low T4, thus preserving brain T3 concentrations. In this work, we have studied the expression of D2 by quantitative in situ hybridization in hypothyroid animals during postnatal development. Our hypothesis was that those regions that are most dependent on thyroid hormone should present selective increases of D2 as a protection against hypothyroidism. D2 mRNA concentration was increased severalfold over normal levels in relay nuclei and cortical targets of the primary somatosensory and auditory pathways. The results suggest that these pathways are specifically protected against thyroid failure and that T3 has a role in the development of these structures. At the cellular level, expression was observed mainly in glial cells, although some interneurons of the cerebral cortex were also labeled. Therefore, the T3 target cells, mostly neurons, are dependent on local astrocytes for T3 supply. (+info)
Specification of somatosensory area identity in cortical explants. (7/704)The H-2Z1 transgene is restricted to a subset of layer IV neurons in the postnatal mouse cortex and delineates exactly the somatosensory area. Expression of the H-2Z1 transgene was used as an areal marker to determine when the parietal cortex becomes committed to a somatosensory identity. We have shown previously that grafts dissected from embryonic day 13.5 (E13.5) H-2Z1 cortex and transplanted into the cortex of nontransgenic newborns express H-2Z1 according to their site of origin. Expression was not modified on heterotopic transplantation (). In the present study, whole cortical explants were isolated at E12.5 from noncortical tissues. The explants developed a regionalized expression of H-2Z1, indicating that regionalization takes place and is maintained in vitro. We used this property and confronted embryonic H-2Z1 cortex with presumptive embryonic sources of regionalizing signals in an in vitro grafting procedure. A great majority of E11.5-E13.5 grafts maintained their presumptive expression of H-2Z1 when grafted heterotopically on nontransgenic E13.5-E15.5 explants. However, a significantly lower proportion of E11.5 parietal grafts expressed H-2Z1 in occipital compared with parietal cortex, indicating that somatosensory identity may be partially plastic at E11.5. Earlier stages could not be tested because the E10.5 grafts failed to develop in vitro. The data suggest that commitment to the expression of a somatosensory area-specific marker coincides with the onset of neurogenesis and occurs well before the birth of the non-GABAergic neurons that express H-2Z1 in vivo. (+info)
Expression of the striatal DARPP-32/ARPP-21 phenotype in GABAergic neurons requires neurotrophins in vivo and in vitro. (8/704)The medium spiny neuron (MSN) is the major output neuron of the caudate nucleus and uses GABA as its primary neurotransmitter. A majority of MSNs coexpress DARPP-32 and ARPP-21, two dopamine and cyclic AMP-regulated phosphoproteins, and most of the matrix neurons express calbindin. DARPP-32 is the most commonly used MSN marker, but previous attempts to express this gene in vitro have failed. In this study we found that DARPP-32 is expressed in <12% of E13- or E17-derived striatal neurons when they are grown in defined media at high or low density in serum, dopamine, or Neurobasal/N2 (Life Technologies), and ARPP-21 is expressed in <1%. The percentage increases to 25% for DARPP-32 and 10% for ARPP-21 when the same cells are grown in Neurobasal/B27 (Life Technologies) for 7 d. After growth in Neurobasal/B27 plus brain-derived neurotrophic factor (BDNF) for 7 d, E13-derived MSNs are 53.7% DARPP-32-positive and 29. 0% ARPP-21-positive; E17-derived MSNs are 66.8% DARPP-32-positive and 51.5% ARPP-21-positive. The percentage of calbindin-positive neurons also is increased under these conditions. Finally, ARPP-21 expression is reduced in mice with a targeted deletion of the BDNF gene. We conclude that BDNF is required for the maturation of a large subset of patch and matrix MSNs in vivo and in vitro. In addition, we introduce a culture system in which highly differentiated MSNs may be generated, maintained, and studied. (+info)
Calbindins are a family of calcium-binding proteins that play important roles in the regulation of calcium homeostasis in various tissues and organs in the body. They are primarily found in the endoplasmic reticulum and mitochondria of cells, where they help to transport and store calcium ions. There are several different types of calbindins, including calbindin-D28k, calbindin-D9k, and calbindin-1. Calbindin-D28k is the most abundant and widely distributed of the calbindins, and it is found in a variety of tissues, including the brain, liver, and kidneys. Calbindin-D9k is found primarily in the brain and spinal cord, and it is thought to play a role in the regulation of calcium signaling in neurons. Calbindin-1 is found in the pancreas and is thought to play a role in the regulation of insulin secretion. Calbindins are important for maintaining proper calcium levels in the body, and disruptions in their function have been linked to a number of diseases, including osteoporosis, hypertension, and certain neurological disorders.
S100 Calcium Binding Protein G (S100G) is a protein that belongs to the S100 family of calcium-binding proteins. It is primarily expressed in the brain, where it plays a role in the regulation of intracellular calcium levels and the modulation of neuronal excitability. S100G has also been implicated in the development and progression of certain neurological disorders, such as Alzheimer's disease and multiple sclerosis. In addition, S100G has been shown to have anti-inflammatory and neuroprotective effects, and it may have potential as a therapeutic target for these conditions.
Calbindin 1 is a calcium-binding protein that is primarily expressed in the parathyroid gland, where it plays a role in regulating calcium homeostasis. It is also found in other tissues, including the brain, pancreas, and bone. In the brain, calbindin 1 is expressed in several regions, including the cerebellum, hippocampus, and neocortex. It is thought to play a role in regulating calcium signaling and neurotransmitter release, and has been implicated in a number of neurological disorders, including epilepsy, autism, and schizophrenia. In the pancreas, calbindin 1 is expressed in the beta cells, where it may play a role in regulating insulin secretion. In the bone, calbindin 1 is expressed in osteoblasts, where it may play a role in regulating bone mineralization. Overall, calbindin 1 is a multifunctional protein that plays important roles in regulating calcium homeostasis and neurotransmitter release in various tissues throughout the body.
Calbindin 2, also known as calbindin-D28K, is a calcium-binding protein that is primarily expressed in the parathyroid gland, where it plays a role in regulating calcium homeostasis. It is also found in other tissues, including the brain, pancreas, and kidneys, where it has various functions. In the brain, calbindin 2 is expressed in several regions, including the cerebellum, hippocampus, and neocortex. It is thought to play a role in regulating calcium signaling and neurotransmitter release, and has been implicated in a number of neurological disorders, including epilepsy, Alzheimer's disease, and schizophrenia. In the pancreas, calbindin 2 is expressed in the beta cells, where it is involved in regulating insulin secretion. In the kidneys, it is thought to play a role in calcium reabsorption and regulation of blood calcium levels. Overall, calbindin 2 is a multifunctional protein that plays important roles in regulating calcium homeostasis in various tissues throughout the body.
In the medical field, binding sites refer to specific locations on the surface of a protein molecule where a ligand (a molecule that binds to the protein) can attach. These binding sites are often formed by a specific arrangement of amino acids within the protein, and they are critical for the protein's function. Binding sites can be found on a wide range of proteins, including enzymes, receptors, and transporters. When a ligand binds to a protein's binding site, it can cause a conformational change in the protein, which can alter its activity or function. For example, a hormone may bind to a receptor protein, triggering a signaling cascade that leads to a specific cellular response. Understanding the structure and function of binding sites is important in many areas of medicine, including drug discovery and development, as well as the study of diseases caused by mutations in proteins that affect their binding sites. By targeting specific binding sites on proteins, researchers can develop drugs that modulate protein activity and potentially treat a wide range of diseases.
Amyloid beta-Protein Precursor (AβPP) is a protein that plays a crucial role in the development of Alzheimer's disease. It is a transmembrane protein that is primarily found in the brain and is responsible for the production of amyloid-beta peptides, which are the main components of the amyloid plaques that are characteristic of Alzheimer's disease. AβPP is synthesized in the endoplasmic reticulum and is transported to the Golgi apparatus, where it is processed into different forms. One of the main forms is the amyloid-beta peptide, which is produced by the cleavage of AβPP by enzymes called beta-secretase and gamma-secretase. The accumulation of amyloid-beta peptides in the brain is thought to be a key factor in the development of Alzheimer's disease. The peptides can aggregate and form insoluble plaques, which can disrupt the normal functioning of neurons and lead to the death of brain cells. In addition to its role in Alzheimer's disease, AβPP has also been implicated in other neurological disorders, such as frontotemporal dementia and Parkinson's disease.
Cystatin C is a small protein that is produced by most cells in the body. It is a member of the cystatin family of proteins, which are known to play a role in regulating the activity of cysteine proteases, enzymes that break down proteins. Cystatin C is primarily filtered by the kidneys and is excreted in the urine. It is a useful biomarker for assessing kidney function, as its levels in the blood and urine can be used to detect and monitor kidney disease. In addition to its role in kidney function, cystatin C has been implicated in a number of other biological processes, including inflammation, cell proliferation, and cancer.
Cathepsin B is a protease enzyme that is found in the lysosomes of cells in the human body. It plays a role in the degradation of proteins and other molecules within the cell, and is involved in a number of cellular processes, including cell growth, differentiation, and apoptosis (programmed cell death). In the medical field, cathepsin B has been studied in relation to a number of diseases and conditions, including cancer, neurodegenerative disorders, and infections. For example, cathepsin B has been shown to be involved in the development and progression of certain types of cancer, including breast cancer and pancreatic cancer. It has also been implicated in the development of neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease, and in the pathogenesis of certain viral infections, including HIV and influenza. In addition to its role in disease, cathepsin B has also been studied as a potential therapeutic target. For example, drugs that inhibit the activity of cathepsin B have been investigated as potential treatments for cancer and other diseases.
Alzheimer's disease is a progressive neurodegenerative disorder that affects memory, thinking, and behavior. It is the most common cause of dementia, a condition characterized by a decline in cognitive abilities severe enough to interfere with daily life. The disease is named after Alois Alzheimer, a German psychiatrist who first described it in 1906. Alzheimer's disease is characterized by the accumulation of abnormal protein deposits in the brain, including amyloid-beta plaques and neurofibrillary tangles. These deposits disrupt the normal functioning of brain cells, leading to their death and the progressive loss of cognitive abilities. Symptoms of Alzheimer's disease typically begin with mild memory loss and gradually worsen over time. As the disease progresses, individuals may experience difficulty with language, disorientation, and changes in personality and behavior. Eventually, they may become unable to care for themselves and require around-the-clock care. There is currently no cure for Alzheimer's disease, but treatments are available to manage symptoms and improve quality of life for those affected by the disease. These treatments may include medications, lifestyle changes, and support from caregivers and healthcare professionals.
Cathepsins are a family of proteolytic enzymes that are found in the lysosomes of cells. They are responsible for breaking down a variety of proteins, including enzymes, hormones, and cellular debris. In the medical field, cathepsins are of interest because they play a role in many physiological processes, including cell growth and differentiation, immune function, and the degradation of damaged proteins. They are also involved in a number of pathological conditions, including cancer, neurodegenerative diseases, and inflammatory disorders. As such, cathepsins are the subject of ongoing research in the field of medicine, with the goal of developing new therapeutic strategies based on their activity.
Cystatins are a family of cysteine protease inhibitors that play important roles in regulating the activity of proteases in the body. They are found in a variety of tissues and fluids, including blood, saliva, and pancreatic juice. Cystatins are synthesized as inactive precursors that are activated by proteolytic cleavage. Once activated, they bind to and inhibit the activity of cysteine proteases, which are enzymes that cleave proteins at specific cysteine residues. This inhibition helps to regulate the activity of these proteases and prevent them from causing damage to cells and tissues. Cystatins have been implicated in a number of physiological and pathological processes, including inflammation, cancer, and neurodegenerative diseases.
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- Calbindins are three different calcium-binding proteins: calbindin, calretinin and S100G. (wikipedia.org)
- In the brain, its synthesis is independent of vitamin-D. Calretinin, also known as calbindin 2, is a 29 kDa protein with 58% homology to calbindin 1 and principally found in nervous tissues. (wikipedia.org)
- Rat brain cerebellum stained with mouse anti-calbindin (green, 1:1,000) and rabbit anti-calretinin (R-1800-50, red, 1:5,000) by Immunohistochemistry . (biosensis.com)
- Calcium-binding proteins such as calbindin D28K and calretinin are used as markers of nervous and enteric nervous systems, but they are present in numerous other cells. (unime.it)
- In this study we demonstrated, for the first time, the presence of calretinin and calbindin D28K in skin club cells of Danio rerio exposed to different wavelengths by immunohistochemistry analysis. (unime.it)
- Exposure to white-blue light and blue light causes the expression and colocalization of calbindin-D28K and calretinin. (unime.it)
- These results demonstrate that calbindin and calretinin could be involved in the pathophysiology of skin injury due to exposure to short-wavelength visible light spectrums. (unime.it)
- ELISA: Human Calbindin D ELISA Kit (Colorimetric) - These standard curves are provided for demonstration only. (assaysolution.com)
- A calbindin protein that is differentially expressed in distinct populations of NEURONS throughout the vertebrate and invertebrate NERVOUS SYSTEM, and modulates intrinsic neuronal excitability and influences LONG-TERM POTENTIATION. (lookformedical.com)
- Product Description google Mouse anti-Calbindin-binding protein Monoclonal Antibody (Unconjugated), suitable for WB, IHC-Frozen. (biosensis.com)
- The band at ~25 kDa corresponds to calbindin protein, heavily expressed in the cerebellum, but less in hippocampus. (biosensis.com)
- One potential candidate is calbindin D 9k, a monomeric calcium-binding protein of the S100 family of the calmodulin-related proteins, involved in Ca 2+ buffering and in trans-cellular transport of Ca 2+ ions. (lu.se)
- We investigate the solution structure of calbindin D 9k using SAXS and quantify the protein-protein interactions through second virial coefficients as a function of the calcium binding state (holo and apo) and the screening conditions, both experimentally and via Monte Carlo computer simulations. (lu.se)
- The structure of calbindin is characteristic of an EF-hand protein, with two helix-loop-helix calcium binding motifs joined by a flexible linker, and a short anti-parallel beta-type interaction between the two ion-binding sites. (molmovdb.org)
- Calbindin-D9k (S100G) is found in mammalian intestine and calbindin-D28k is in avian intestine and in mammalian kidney and other tissues. (assaysolution.com)
- In this process, cytosolic Ca2+ remains at low nontoxic concentrations because the Ca2+ influx is buffered rapidly by calbindin-D28K. (researchwithrutgers.com)
- Subsequently, Ca2+ that is bound to calbindin-D28K is shuttled toward the basolateral Ca2+ extrusion systems. (researchwithrutgers.com)
- Left and middle: Detection of calbindin immunoreactivity in rat brain cerebellum (Left) and cortex (Middle) sections by Immunohistochemistry . (biosensis.com)
- To explore these questions, we performed a genome -wide CRISPR screen in a cellular model of DBA and identified Calbindin 1 (CALB1), a member of the calcium -binding superfamily, as a potential modifier of the disordered erythropoiesis in DBA. (bvsalud.org)
- Regional and cellular dystrophin distribution was evaluated in both human and rat hippocampi and in rat cerebellar tissue by immunofluorescent colocalization with neuronal (NeuN and calbindin) and glial (GFAP) markers. (frontiersin.org)
- The researchers showed that CysC ablation in the APP mice prevented premature mortality and increased expression of calbindin (a neuronal marker whose decreased levels correlate with cognitive decline in APP-J20 mice). (alzforum.org)
- Nonetheless, there is no homology between calbindin 1 and S100G, apart from their calcium binding domains (EF-hands): S100G has two EF-hands, and calbindin 1 has six. (wikipedia.org)
- Unlike calbindin 1 and 2, S100G is a member of the S100 family of calcium-binding proteins. (wikipedia.org)
- Expression of S100G, like that of calbindin 1, is stimulated by the active vitamin D metabolite, calcitriol although the precise mechanisms are still controversial. (wikipedia.org)
- This assay has high sensitivity and excellent specificity for detection of human Calbindin D. No significant cross-reactivity or interference between human Calbindin D and analogues was observed. (assaysolution.com)
- It is encoded in humans by the CALB2 gene and was formerly known as calbindin-D29k. (wikipedia.org)
- The antibody shows strong immunoractivity with one calbindin band at ~30 kDa. (biosensis.com)
- Calbindin antibody prominently labels the dendrites and perikarya of Purkinje cells in the molecular layer of cerebellum. (biosensis.com)
- Right: Western blot analysis of calbindin expression (antibody dilution: 1:2,000) in rat cerebellum (2), pig hippocampus (3), and cow cerebellum (4). (biosensis.com)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Calbindin (CALB) in serum, plasma, tissue homogenates, urine and other biological fluids. (clinical-trial-logistics.com)
- As predicted, the effects on calbindin immunostaining and hippocampal synaptic function in the CysC-deficient APP mice disappeared when CatB was out of the picture. (alzforum.org)
- Description: A sandwich quantitative ELISA assay kit for detection of Rat Calbindin (CALB) in samples from serum, plasma, tissue homogenates or other biological fluids. (clinical-trial-logistics.com)
- Calbindin is a vitamin D-responsive gene in many tissues, in particular the chick intestine, where it has a clear function in mediating calcium absorption. (wikipedia.org)
- Intestinal Ca 2+ absorption and expression of calbindin-D 9K and TRPV6, as well as serum parameters of the calbindin-D 28K -/- mice, did not differ from those of wild-type mice. (researchwithrutgers.com)
- Western blot analysis of calbindin expression in cow cerebellum homogenate. (biosensis.com)
- The similarity between TRPV5 -/- /calbindin-D 28K -/- and TRPV5 -/- mice was supported further by an equivalent increase in renal calbindin-D 9K expression and in intestinal Ca 2+ hyperabsorption as a result of upregulation of calbindin-D 9K and TRPV6 expression in the duodenum. (researchwithrutgers.com)
- Reiswig, J.D., Frazer, G.S. and Inpanbutr, N. (1995) Calbindin-D9k expression in the pregnant cow uterus and placenta. (scirp.org)
- These results underline the gatekeeper function of TRPV5 being the rate-limiting step in active Ca 2+ reabsorption, unlike calbindin-D 28K , which possibly is compensated by calbindin-D 9K . (researchwithrutgers.com)
- Calbindin (red) is predominantly expressed in the dendrites and perikarya of Purkinje cells in the molecular layer of cerebellum (left), and selectively expressed in certain type of interneurons (calbindin-postive interneuron) in the cortex (middle). (biosensis.com)
- C ) Cerebellar tissue from Control and Ttbk2 c.mut mice at 3 months after loss of Ttbk2 , immunostained for Calbindin to label Purkinje cells (red) and VGLUT2 to show climbing fiber synapses (green). (elifesciences.org)
- For addressing the in vivo role of TRPV5 and calbindin-D 28K in the maintenance of the Ca 2+ balance, single- and double-knockout mice of TRPV5 and calbindin-D 28K (TRPV5 -/- , calbindin-D 28K -/- , and TRPV5 -/- /calbindin-D 28K -/- ) were characterized. (researchwithrutgers.com)
- Urine analysis indicated that TRPV5 -/- / calbindin-D 28K -/- mice exhibit on both diets hypercalciuria compared with wild-type mice. (researchwithrutgers.com)
- Ca 2+ excretion in TRPV5 -/- /calbindin-D 28K -/- mice was not significantly different from TRPV5 -/- mice, whereas calbindin-D 28K -/- mice did not show hypercalciuria. (researchwithrutgers.com)
- Calbindin acts as a calcium buffer and calcium sensor and can hold four Ca2+ in the EF-hands of loops EF1, EF3, EF4 and EF5. (wikipedia.org)
- Small angle X-ray scattering indicates that the crystal structure better predicts the properties of calbindin in solution compared with the structure determined by nuclear magnetic resonance. (wikipedia.org)
- The structure of rat calbindin was originally solved by nuclear magnetic resonance and was one of the largest proteins then to be determined by this technique. (wikipedia.org)
- In 2018 the X-ray crystal structure of human calbindin was published (PDB entry 6FIE). (wikipedia.org)
- The structure of calbindin has been solved in the apo (Conformation 1), (Ca2+)(2) (Conformation 2), and (Cd2+)(1) (Conformation 3) states in x-ray and NMR studies. (molmovdb.org)
- Targeting of Calbindin 1 rescues erythropoiesis in a human model of Diamond Blackfan anemia. (bvsalud.org)
- They were found to exist in two distinct sizes with a molecular weight of approximately 9 kDa and 28 kDa, and they were renamed calbindins. (wikipedia.org)
- Calbindin contains 4 active calcium-binding domains, and 2 modified domains that have lost their calcium-binding capacity. (wikipedia.org)