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At least 1,423 records · Page 79Linked to original sources
PubMed1998

Subcellular localization and characterization of nucleoside diphosphate kinase in rat retina: effect of diabetes.

Nucleoside diphosphate kinase (NDP kinase) catalyzes the transfer of terminal phosphate from nucleotide triphosphates (e.g. ATP) to nucleotide diphosphates (e.g. GDP) to yield nucleotide triphosphates (e.g. GTP). Since guanine nucleotides play critical role(s) in GTP-binding protein (G-protein)-mediated signal transduction mechanisms in retina, we quantitated NDP kinase activity in subcellular fraction-derived from normal rat retina. A greater than 85% of the total specific activity was present in the soluble fraction, which was stimulated (up to 7 fold) by 2 mM magnesium. NDP kinase exhibited saturation kinetics towards di- and tri-phosphate substrates, and was inhibited by known inhibitors of NDP kinase, uridine diphosphate (UDP) or cromoglycate (CRG). We have previously reported significant abnormalities in the activation of G-proteins in streptozotocin (STZ)-diabetic rat retina (Kowluru et al. Diabetologia 35:624 631, 1992). Since NDP kinase has been implicated in direct interaction with and/or activation of various G-proteins, we quantitated both basal and magnesium-stimulated NDP kinase activity in soluble and particulate fractions of retina derived from STZ-diabetic rats to examine whether abnormalities in G-protein function in diabetes are attributable to alterations in retinal NDP kinase. There was no effect of diabetes either on the basal or the magnesium-activated retinal NDP kinase activity. This study represents the first characterization of NDP kinase activity in rat retina, and suggests that in diabetes, this enzyme may not be rate-limiting and/or causal for the observed alterations in retinal G-protein functions.

Animals↗
PubMed1998

Subcellular localization of low-affinity nerve growth factor receptor-immunoreactive protein in adult rat purkinje cells following traumatic injury.

Cerebellar Purkinje cells in the rat express low-affinity nerve growth factor receptor (p75 NGFR) antigen during development, but rarely in normal adult animals. In striking contrast, re-expression of p75 NGFR-immunoreactive protein was reported by light microscopy immunocytochemistry in adult rat Purkinje cells as early as 1 day after traumatic axotomy. Characteristically, varicose axons through the infraganglionic zone were also stained. To date, however, there is no information on the subcellular location of the antigenic re-expression. To address this, a pre-embedding immunocytochemical ultrastructural study using affinity-purified monoclonal 192-IgG was carried out after an experimentally induced traumatic lesion of the rat cerebellum. At the electron microscopic level, immunostaining was intense in Purkinje cells. In these cells, the immunoreactivity was always associated with the internal face of the membranes of the rough endoplasmic reticulum, Golgi apparatus and nuclear envelope. Patches of immunoreactivity were also associated with the outer surface of the plasma membrane of the cell body, dendritic processes and axons. It is noteworthy that receptor immunoreactivity was detected in recurrent collaterals of Purkinje cell axons forming symmetric synaptic contacts with the cell body and dendrites of immunonegative local circuit neurons. Results of this study show that injury-induced re-expression of p75 NGFR antigen is restricted to Purkinje cells. Also, the relative importance of the contribution of the local circuit neurons to the production of neurotrophic substances after trauma is suggested.

Animals↗
PubMed1995

Alpha-fetoprotein binding proteins: implications for transmembrane passage and subcellular localization.

Alpha-fetoprotein (AFP) is an oncofetal protein classified in a super-family together with albumin and Vitamin-D binding (Gc) protein which present as globular proteins comprised of three domains. Several subdomain regions on AFP have been previously proposed to serve as dimerization interfaces for nuclear receptors or perhaps other co-factors/inhibitors. The cellular uptake and internalization of AFP together with its subcellular compartmentalization is now well documented in a variety of cell types. A myriad of reports have emerged which have detected, identified, and characterized various binding proteins associated with AFP in different cellular compartments. However, the literature is devoid of any attempts to summarize, categorize, and relate these proteins to the various physiological activities attributed to this fetal protein. It is conceivable that AFP could interact and/or bind cytoplasmic chaperone proteins that normally escort nuclear factors or transcription co-factors through the cytoplasm toward organelle interfaces. A dual concept proposing binding or escort proteins for AFP together with subdomain dimerization interfaces on the AFP molecule can be reconciled into a composite hypothesis to formulate a rationale for the growth regulating properties ascribed to AFP during the last decade. Thus, AFP might serve as a modulator/modifier of various cell growth regulatory pathways during embryonic and fetal development in vertebrates.

Animals↗
PubMed2004

Cellular and subcellular localization of the inhibitory glycine receptor in hippocampal neurons.

Inhibitory glycine receptors are most abundant in spinal cord and brainstem, and glycinergic synapses have a well-established role in the regulation of locomotor behavior. Little is known about the function of glycine receptors in cortex and hippocampus, where GABA plays a dominant role in synaptic inhibition. Therefore, we have investigated tissue and cellular expression of glycine receptor alpha-subunits. Western blot and immunohistochemical analyses reveal the presence of glycine receptors in hippocampal tissue. Immunocytochemical experiments in hippocampal cultures show prominent cellular expression of glycine receptors in pyramidal neurons and GAD-positive interneurons similar to the calcium-binding protein VILIP-1 with widespread hippocampal distribution. On the subcellular level we found co-staining of GlyR and the presynaptic marker synapsin I. Furthermore, co-staining with GAD at synaptic terminals indicated partial co-localization of GABA- and glycine receptors.

Animals↗
PubMed1982

Subcellular localization and characterization of HCO3(-)-ATPase from the mantle of the freshwater clam, Anodonta cataracta.

1. HCO3(-)-stimulated ATPase activity was demonstrated in mantle tissue of the freshwater clam, Anodonta cataracta. 2. Calcium (1 mM) slightly inhibited and SCN- completely inhibited HCO3(-)-stimulation of the enzyme. 3. ATPase activity had a Km of 6.8 mM for HCO3(-)-activation and was inhibited at HCO3(-)-concentrations greater than 20 mM. 4. Subcellular fractionation studies revealed the presence of both a mitochondrial and a non-mitochondrial HCO3(-)-ATPase.

Adenosine Triphosphatases↗
PubMed1980

Studies on drug-induced lipidosis: subcellular localization of phospholipid and cholesterol in the liver of rats treated with chloroquine or 4,4'-bis (diethylaminoethoxy)alpha, beta-diethyldiphenylethane.

Administration of chloroquine or 4,4'-bis(diethylaminoethoxy)alpha, beta-diethyldiphenylethane (DH) to rats in oral doses of 100 mg/kg for 7 days causes phospholipid and cholesteryl ester accumulation in liver. To further characterize this drug-induced lipidosis, we have isolated and characterized the lipids of subcellular fractions from control rats and rats treated with chloroquine, DH, and Triton WR-1339. The phospholipid content of liver is increased 1.5-fold by chloroquine or DH treatment but is unaffected by Triton WR-1339. Acid phosphatase is increased by treatment with these three agents. Chloroquine and DH cause a shift of acid phosphatase from the light mitochondrial fraction (L) to the heavy mitochondrial fraction (M). Multilamellar bodies, an ultrastructural hallmark of chloroquine and DH-induced lipidosis, were isolated in a highly-purified form from the M fraction of chloroquine- or DH-treated rats. They are highly enriched in acid phosphatase indicating their lysosomal origin. In addition, they contain large amounts of phospholipid, cholesterol, and cholesteryl ester and are the sole site of bis(monoacylglycero)phosphate and the enzyme which catalyzes its synthesis from phosphatidylglycerol. Analysis of the phospholipid content of the respective control and drug-treated liver fractions shows that the entire excess phospholipid content of chloroquine- or DH-treated liver can be accounted for by the drug-induced multilamellar bodies. Triton WR-1339-induced lysosomes, which were isolated for comparison, also contain bis(monoacyglycero)phosphate and bis(monoacyglycero)phosphate synthetase. However, they differ from the drug-induced lysosomes in that their sphingomyelin content is much higher and their total phospholipid and phosphatidylinositol content much lower. The multilamellar bodies are the principal intracellular site of accumulation of chloroquine and DH, respectively. Increased delivery of phospholipid to lysosomes and decreased lysosomal catabolism of phospholipid are the factors which are thought to cause this experimental lipidosis. High levels of phosphatidylinositol in the multilamellar body may be in part responsible for the increased content of bis(monoacyglycero)phosphate since it has been identified as an acyl donor in bis(monoacylglycero)phosphate synthesis.

Acyltransferases↗
PubMed2001

Metallothionein expression in renal cell carcinoma: subcellular localization and prognostic significance.

PURPOSE: We investigated the immunohistochemical localization of metallothionein (MT) in renal cell carcinoma and determined the potential role of MT expression as a possible prognostic variable for tumor proliferation and progression. MATERIALS AND METHODS: Tumor tissue blocks from 70 patients with renal cell carcinoma who underwent radical or partial nephrectomy were investigated. Mean followup plus or minus standard error was 36 +/- 3 months. Immunohistochemical testing was performed by the avidin-streptavidin method using a monoclonal mouse antiMT antibody. MT staining intensity in samples was evaluated semiquantitatively. The subcellular distribution of MT was also determined. Staining characteristics were compared with the clinicopathological results. RESULTS: MT immunostaining was found in 39 of 70 tumors (55.7%) and subcellulary MT was localized in the cytoplasm, nucleus and cell membrane. The survival of patients with MT immunostaining was significantly worse than that of those with MT negative results (p = 0.02). A significant relationship of higher tumor grade and MT staining intensity was observed in grades I and III (p = 0.01), and grades II and III (p = 0.02) tumors. No association was found of MT expression and pathological stage. Sarcomatoid tumors showed significantly higher MT expression than clear cell, papillary, granular or chromophobe tumors (p = 0.02, 0.001, 0.01 and 0.01, respectively). MT expression was not an independent prognostic variable. CONCLUSIONS: MT over expression seems to be associated with malignant behavior and poor prognosis in renal cell carcinoma. Therefore, MT expression may be considered a useful marker of less differentiated and more aggressive renal cell carcinoma.

Adult↗
PubMed2003

Independent signals determine the subcellular localization of NEP in prostate cancer cells.

NEP (Neutral endopeptidase 24.11) is a cell surface enzyme that hydrolyzes bioactive neuropeptides implicated in the transition from androgen-dependent prostate cancer (PC) to androgen-independent PC. We report the cloning and sequence analyses of NEP cDNAs from human androgen-responsive LNCaP PC cells and prostatic stromal cells. To investigate the functional role of a nuclear localization sequence (NLS) detected within the N-terminus and of an endoplasmic reticulum retention signal within the C-terminus, NEP-GFP expression vectors were constructed containing the whole NEP gene, fragments encoding the N-terminus/C-terminus of the protein (5(')NEP-GFP/3(')NEP-GFP), and 5(')NEP-GFP constructs lacking the NLS. 3(')NEP-GFP transfected cells showed plasma membrane/cytoplasmic fluorescence whereas the 5(')NEP-GFP fusion protein was also detected in the nucleus. The omission of the NLS resulted in no reduction in nuclear and an increase in cytoplasmic staining. The results suggest that the analyzed structural motifs determine the subcellular distribution of NEP in epithelial LNCaP PC cells and stromal prostatic cells and therefore could be responsible for the altered cellular localization of NEP observed in PC.

Amino Acid Sequence↗