Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The hypothesis that the growth of mammalian cells is regulated by hormones is now supported by considerable evidence. Two rat pituitary cell lines, GH3 and GC, a mouse melanoma, M2R (B16), and a human cervical carcinoma cell, HeLa S-3, have been grown indefinitely in serum-free (SF) hormone-supplemented medium. No visible changes of growth characteristics were observed in the cells grown continuously in the SF condition. However, changes in the activity of a plasma membrane enzyme, alkaline phosphatase, and in the relative intensity of surface proteins that are labeled by the [125I] lactoperoxidase technique were found in HeLa cells grown in the SF condition. To study the role of hormones required in the regulation of cell growth, HeLa cells were grown in the absence of one of the required hormones. The following results were obtained. Epidermal growth factor is probably involved in the regulation of the synthesis of macromolecules such as RNA and of the protein content per cell. Transferrin, the accessory factor in the SF condition, supplies iron for cells. The two basic peptides in this SF system, fibroblast growth factor and insulin, are probably involved in the balance of nutrients and energy inside the cell. The replacement of F12 medium with a better-balanced medium, MCDB 105, can mimic the requirements for these two peptides. The steroid hydrocortisone (HC) is probably involved in alteration of the cell surface. This is indicated by the effects of HC on cell morphology, rate of detachment from the dish, and the pattern of [125I] lactoperoxidase labeling of surface proteins. In addition, it is necessary to change the medium more frequently to maintain the culture in the medium without HC. This observation suggests that HC may be involved in the control of homeostatic properties of the cell surface. The production of rat prolactin by GH3 cells was also studied. GH3 cells in the SF condition produce 1.6 microgram prolactin per 10(5) cells in 24 h, while 2.4 microgram is produced in the presence of serum. Prolactin production in the SF condition is enhanced by the presence of thyrotropin-releasing hormone and inhibited by triiodothyronine (T3). T3 is the major growth factor for these cells. Without it cell growth is severely limited, while prolactin production is elevated. This result suggests that the GH3 cell line in the SF condition may be an ideal system for the study of hormonal regulation of cell growth and specific gene expression.
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PMID:Replacement of serum in cell culture by hormones: a study of hormonal regulation of cell growth and specific gene expression. 66 Jun 66

Phenotypes of the cells developing into small colonies after days of primary culture of adult rat hepatocytes in serum-free modified Dulbecco Modified Eagles' medium containing 10 mM nicotinamide and 10 ng/ml epidermal growth factor were analyzed immunocytochemically, cytochemically and ultrastructurally. Albumin, cytokeratin 8 and 18 were seen by immunocytochemical techniques in the cells of the small colonies at Day 6. Transferrin, alpha 1-antitrypsin, ceruloplasmin, and haptoglobin, proteins secreted by mature hepatocytes, were faintly stained in these cells as was alpha-fetoprotein. These proteins were secreted into the culture medium as evidenced by immunoblot analysis. gamma-Glutamyltransferase, alkaline phosphatase and glucose 6-phosphatase were not present in the cells of the small colonies as well as the surrounding hepatocytes at Day 6 of culture. In addition, ultrastructural examinations of the cells in the small colonies indicated that these cells not only had many characteristic mitochondria and desmosomes, but also a few small peroxisomes. Such cells, even after 20 days in culture were proliferating, as evidenced by the intranuclear presence of the proliferating cell nuclear antigen. The potential relation of these cells to hepatocytes which may serve as the principal reserve for replicating hepatocytes is discussed.
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PMID:Characteristics of small cell colonies developing in primary cultures of adult rat hepatocytes. 127 92

Transferrin (TF) has a growth promoting activity in cell culture. The aim of this work was to study possible relationships between serum TF, alkaline phosphatase activity (ALP), plasma insulin-like growth factor 1 (IGF-1) levels and rate of height increase in boys. 149 boys aged 13-15 yrs were studied. TF levels were measured using turbidimetric method. The serum levels of ALP could be used as a biochemical marker for bone formation. Significant correlation was found between serum TF levels and ALP levels (r = 0.31, P less than 0.0005). The TF levels are higher in iron-deficiency anemia. The hemoglobin (Hb) and serum ferritin were measured in all boys. Thirty-one of 149 boys had no iron-deficiency anemia (Hb 14.0 g/dl and serum ferritin 23 ng/ml). The rate of growth in height was estimated over a 5 month period. In these boys, the rate of growth in height was significantly correlated with serum TF levels (r = 0.37; P less than 0.05). A significant correlation was found between serum TF levels and plasma IGF-1 levels (r = 0.45; P less than 0.05). These data indicate that serum TF levels may be a marker of skeletal growth in normal boys.
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PMID:Serum transferrin as a marker of bone growth in boys: correlation with serum alkaline phosphatase activity, plasma insulin-like growth factor 1 and rate of growth in height. 187 82

We have investigated the individual and combined actions of epidermal growth factor (EGF), transferrin and hydrocortisone on the maturation of whole fetal mouse metanephroi maintained in serum-free conditions for up to 5 days. The presence of EGF (100 ng/ml) resulted in elevated levels of [3H]-thymidine incorporation when compared to controls; autoradiograms showed that the proliferation of mesenchymal cells in the nephrogenic zone is particularly enhanced as verified by cell counting. Brush border hydrolase activities (alkaline phosphatase and gamma-glutamyltransferase), on the other hand, were significantly diminished. Transferrin (5 micrograms/ml) slightly stimulated DNA synthesis and potentiated EGF mitogenic action. The activation of DNA replication by the growth factor seems to be mediated through the protein kinase C pathway. When added alone, hydrocortisone (10(-6) M) strongly inhibited DNA synthesis, stimulated hydrolase activities and exerted a positive effect on brush border differentiation. When combined with EGF or to EGF + transferrin, hydrocortisone counteracted the effects of these latter peptides on DNA synthesis and enzyme activities. Considering the earlier observation of a reciprocal relation between proliferation and differentiation during the neotubulogenic phase of kidney development, the results described in the current study suggest that synergistic and synarchic actions of these heterologous factors are involved in the regulation of tubulogenesis.
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PMID:Fetal mouse kidney maturation in vitro: coordinated influences of epidermal growth factor, transferrin and hydrocortisone. 195 5

Rat placental cells (RPCs) derived from the chorioallantoic placenta of day-12 Holtzman rats were tested for the expression of class I and class II RT I histocompatibility antigens, transferrin receptors, intermediate filaments, and alkaline phosphatase. The binding of mouse monoclonal antibodies to those antigens by RPCs was compared with the binding of the same reagents to rat placental cells in situ. RPCs expressed low levels of class I antigens and failed to express detectable levels of class II antigens. RPCs resisted up-regulation of expression of class I antigens by interferon-gamma, and did not express class II antigens following exposure to medium containing interferon. Transferrin receptors; cytokeratin intermediate filaments, and alkaline phosphatase were universally expressed by RPCs. Taken together with the patterns of expression of the same antigens by rat placental cells in situ, the results suggest that RPCs comprise labyrinthine trophoblast cells. Those cells may provide a valuable new approach for studying the structures and functions of trophoblast cells in vitro.
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PMID:Expression of histocompatibility antigens, transferrin receptors, intermediate filaments, and alkaline phosphatase by in vitro cultured rat placental cells and rat placental cells in situ. 313 46

The hyposideremia of inflammation was found to be based on a three-step mechanism involving lactoferrin, the iron-binding protein from the specific granules of neutrophilic leukocytes. (a) Lactoferrin is Released from Neutrophils in an Iron-Free Form. When phagocytosis was induced in neutrophils by zymosan or bacteria, lactoferrin was recovered in the incubation medium together with other constituents of the specific granules, such as alkaline phosphatase and lysozyme. Lactoferrin extracted from leukocytes was able to bind the amount of iron corresponding to its theoretical iron-binding capacity. After injection of endotoxin into rats, lactoferrin was detected in various tissues where it was normally absent, or in the plasma when the reticuloendothelial system (RES) had previously been blocked by injections of India ink or aggregated albumin. (b) Lactoferrin is Able to Remove the Iron from Transferrin. Significant exchange of iron from transferrin to lactoferrin was observed in vitro only at a pH below 7.0 or in the presence of a high concentration of citrate. However, the fast elimination of lactoferrin in vivo, when saturated with iron, might account for the observed transfer of iron to endogenous or administered apolactoferrin. Intravenous injection of human apolactoferrin into rats caused a marked decrease of the plasma iron level. The kinetics of this process, as well as controls with other proteins, ruled out the possibility of a secondary inflammatory effect due to phlogogenic contaminants. (c) Fe-Lactoferrin is Taken-up by the RES. By immunofluorescence, lactoferrin was shown to be bound and ingested by monocytes. The rate of elimination of human Fe-lactoferrin injected into rats was particularly fast when compared to that of human apolactoferrin, succinylated Fe-lactoferrin, or other human proteins. Blockade of the RES slowed down the rate of clearance of Fe-lactoferrin and was also found to retard the elimination of endogenous rat lactoferrin released by endotoxin. These experiments suggest the existence of specific receptors for Fe-lactoferrin on the membrane of macrophages.
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PMID:The involvement of lactoferrin in the hyposideremia of acute inflammation. 421 90

When K562 human erythroleukemic cells are induced to differentiate by addition of hemin to their medium, the number of binding sites for transferrin on the cell surface is substantially reduced. This reflects an internalization of receptors since no such reduction is observed when the total binding sites in soluble extracts of uninduced and differentiating cells are compared. The internalization of transferrin receptors has also been shown using lactoperoxidase-mediated radioiodination of cell surfaces and by immune precipitation of total and surface labeled receptors using an anti-receptor monoclonal antibody. Transferrin receptors from uninduced and differentiating cells were partially purified by affinity chromatography on transferrin-Sepharose and shown to be disulfide-bridged homodimers of a polypeptide with an apparent molecular weight of approximately 90,000. This protein is a phosphoprotein that can be resolved by isoelectric focusing into three major and two minor forms. By digestion with bacterial alkaline phosphatase, it was shown that at least four of these forms are probably phosphorylation variants of a single polypeptide. As differentiation proceeds, the proportions of the individual forms of the receptor change with a shift to the more phosphorylated polypeptides.
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PMID:Alterations in the transferrin receptor of human erythroleukemic cells after induction of hemoglobin synthesis. 608 61

The effect of transferrin was tested on osteoblastic cells (clone MC3T3-E1) cultured in serum-free medium containing 1% bovine serum albumin (BSA). Transferrin (Tf) stimulated increases of protein content and protein synthesis, but not of DNA content and cell number, in the cells. This protein also increased alkaline phosphatase activity and collagen synthesis in combination with 1% BSA. Actinomycin D and cycloheximide inhibited alkaline phosphatase activity induced by Tf, suggesting that Tf may enhance de novo synthesis of the enzyme. These results indicate that Tf may be involved in differentiation of osteoblastic cells, but not in their proliferation, in vitro.
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PMID:Effect of transferrin on alkaline phosphatase activity and collagen synthesis in osteoblastic cells derived from newborn mouse calvaria. 673 40

A group of 291 children aged 3 weeks to 6 1/2 years was examined at a public maternal and child health center and 260 of them - who were considered to be healthy - were included in the present study. By venipuncture, serum was obtained for the analysis of 6 enzymes, and plasma for the estimation of 9 proteins and for lipid analyses. In different age groups, high levels were found for alkaline phosphatase, lactate dehydrogenase, aspartate aminotransferase, alanine aminotransferase, creatine kinase and gamma-glutamyl transferase. Haptoglobin, alpha 1-antitrypsin, prealbumin and transferrin were present at low concentrations during the first months of life. Transferrin rose later in childhood to above adult levels. Only immunoglobulin M showed a sex difference, with higher values for girls. Breast-fed infants had higher (non-fasting) concentrations of cholesterol and triglycerides than formula-fed babies, and they also had higher levels of aspartate aminotransferase and alanine aminotransferase.
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PMID:The levels of serum enzymes, plasma proteins and lipids in normal infants and small children. 731 Mar 26

Microcytosis, hypochromasia, and low mean corpuscular hemoglobin are frequent hematologic abnormalities in dogs with portosystemic vascular anomalies (PSVA). The relationship of iron status to these abnormalities is unclear. We evaluated iron status and hematologic and biochemical parameters in dogs with congenital PSVA before (25 dogs) and after (11 dogs) partial ligation of the vascular anomaly. Serum iron concentration and total iron binding capacity were subnormal in 56% and 20% of dogs with PSVA, respectively. Transferrin saturation was normal in 68%, decreased in 20%, and increased in 12% of the dogs. Plasma ferritin concentration was either normal (56%) or high (44%), and was not associated with increases in ceruloplasmin concentration. Hepatic stainable iron was increased in 10 of 16 dogs. Mean corpuscular volume (MCV), mean corpuscular hemoglobin, and mean corpuscular hemoglobin concentration were decreased in more than 60% of dogs with PSVA. Serum biochemical abnormalities included high bile acid concentration and alanine transaminase (ALT) and alkaline phosphatase (ALP) activities; and low urea, creatinine, cholesterol, and total protein concentrations. Serum iron concentration and clinical status (normal or PSVA) significantly influenced MCV (P = .003 and P < .001, respectively), whereas age, ceruloplasmin, ferritin, cholesterol, bile acids, and total iron binding capacity did not. Partial ligation of PSVA was associated with resolution of clinical signs and the return to normal of iron status and all clinicopathologic abnormalities, except total fasting bile acid concentrations. These findings indicate that iron status is frequently abnormal in dogs with PSVA and that low serum iron concentration appears to be related to the development of microcytosis. The normalization of iron status and clinicopathologic abnormalities after treatment suggests that they are direct consequences of PSVA.
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PMID:Iron status and erythrocyte volume in dogs with congenital portosystemic vascular anomalies. 913 78


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