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1.
J Neuroimmunol ; 220(1-2): 104-7, 2010 Mar 30.
Article in English | MEDLINE | ID: mdl-20149932

ABSTRACT

OBJECTIVE AND SUBJECTS: To examine in vivo levels of BAFF (B-cell activating factor of the tumor necrosis factor family) and APRIL (a proliferation-inducing ligand) in both the cerebrospinal fluid (CSF) and serum of 30 naïve MS patients and 79 subjects affected by acute or chronic inflammatory or non-inflammatory neurological diseases. DESIGN: Case-control study. RESULTS: No difference among groups was evidenced in serum BAFF or APRIL levels. By contrast, CSF levels of BAFF in MS (mean 144.3 pg/ml+/-141.2), although not significantly different from those observed in NIND (164.2 pg/ml+/-92.0), acute peripheral OIND (243.1 pg/ml+/-139.0) or chronic OIND (240.2 pg/ml+/-122.5), were significantly higher in acute central OIND patients (1274.0 pg/ml+/-803.8; p<0.001 vs. all groups). Similarly, CSF APRIL levels in MS (1541.0 pg/ml+/-1071.0), NIND (2629.0 pg/ml+/-1669.0), acute peripheral OIND (2834.0 pg/ml+/-1118.) or chronic OIND (2764.0 pg/ml+/-659.7) were not significantly different, while they were significantly higher in acute central OIND (6218.0 pg/ml+/-3790.0; p<0.001 vs. MS and NIND; and p<0.05 vs. acute peripheral OIND). CONCLUSIONS: Our results strongly suggest that further investigation is warranted to elucidate the role of BAFF and APRIL in MS and that serum levels of BAFF and APRIL do not reflect CSF levels.


Subject(s)
B-Cell Activating Factor/cerebrospinal fluid , Central Nervous System/immunology , Central Nervous System/metabolism , Multiple Sclerosis/cerebrospinal fluid , Multiple Sclerosis/immunology , Tumor Necrosis Factor Ligand Superfamily Member 13/cerebrospinal fluid , Adult , Aged , B-Cell Activating Factor/analysis , B-Cell Activating Factor/blood , B-Lymphocytes/immunology , B-Lymphocytes/metabolism , Biomarkers/analysis , Biomarkers/blood , Biomarkers/cerebrospinal fluid , Case-Control Studies , Central Nervous System/physiopathology , Female , Humans , Immunity, Humoral/immunology , Lymphocyte Activation/immunology , Male , Middle Aged , Multiple Sclerosis/physiopathology , Predictive Value of Tests , Tumor Necrosis Factor Ligand Superfamily Member 13/analysis , Tumor Necrosis Factor Ligand Superfamily Member 13/blood , Up-Regulation/immunology
2.
Planta ; 209(2): 187-194, 1999 Aug 12.
Article in English | MEDLINE | ID: mdl-10436220

ABSTRACT

Phosphorylation/dephosphorylation of the plasma-membrane H(+)-ATPase (EC 3.6.1.35) could act as a regulatory mechanism to control its activity. In this work, a plasmalemma-enriched fraction from maize roots and a partially purified H(+)-ATPase were used to investigate the effects of Ca(2+) and calmodulin on the H(+)-ATPase activity and on its phosphorylation status. Both the hydrolytic and the proton-pumping activities were reduced approximately 50% by micromolar Ca(2+) concentrations while calmodulin did not show any effect either alone or in the presence of Ca(2+). The lack of effect of calmodulin antagonists indicated that calmodulin was not involved in this response. The addition of staurosporine, a kinase inhibitor, abolished the inhibitory effect of Ca(2+). Phosphorylation of plasma membrane and partially purified H(+)-ATPase showed the same behavior. In the presence of Ca(2+) a polypeptide of 100 kDa was phosphorylated. This polypeptide cross-reacted with antibodies raised against the H(+)-ATPase of maize roots. The autoradiogram of the immunodetected protein clearly showed that this polypeptide, which corresponds to the H(+)-ATPase, was phosphorylated. Additional clear evidence comes from the immunoprecipitation experiments: the data obtained show that the H(+)-ATPase activity is indeed influenced by its state of phosphorylation.

3.
Eur J Biochem ; 241(1): 286-90, 1996 Oct 01.
Article in English | MEDLINE | ID: mdl-8898918

ABSTRACT

A low-molecular-mass protein able to bind GTP in both native and SDS-denaturating conditions was detected in the cytosol of embryos from wheat (Triticum aestivum L.) seeds germinated for 40 h. The protein fulfilled most of the distinguishing criteria common to eukaryotic small GTP-binding proteins. It retained the ability to bind GTP after SDS/PAGE and nitrocellulose blotting. The protein eluted from Sephadex G-200 gel filtration with a Ve/Vo value corresponding to a molecular mass of 18 kDa, whereas on SDS/PAGE the molecular mass was 20 kDa. The native protein, which showed an intrinsic GTPase activity highly sensitive to NaF, bound the guanine nucleotide with high specificity and with a relatively high affinity (Kd approximately 85 nM). The GTP-binding protein was not detectable in other subcellular fractions; in the microsomal fraction, two other peptides of low molecular mass (23.5 and 21.5 kDa) with GTP-binding activity were detected. These results indicate that in the cytosolic fraction of germinating wheat embryos there is a 20-kDa protein which is biochemically similar to the known small GTP-binding proteins that currently have been detected almost exclusively in the membrane fraction of plant material.


Subject(s)
GTP-Binding Proteins/chemistry , Triticum/chemistry , Cell Fractionation , Chromatography, Gel , Cytoplasm/chemistry , Electrophoresis, Polyacrylamide Gel , GTP Phosphohydrolases/metabolism , GTP-Binding Proteins/isolation & purification , Germination/physiology , Guanosine Triphosphate/metabolism , Molecular Weight , Protein Binding , Triticum/embryology
4.
J Pediatr Gastroenterol Nutr ; 23(1): 34-7, 1996 Jul.
Article in English | MEDLINE | ID: mdl-8811521

ABSTRACT

We evaluated the nutritional status of 173 consecutive children with newly diagnosed leukemia compared with that of 307 children with benign acute diseases. Nutritional status was assessed by anthropometric measurements including weight, height, weight for height, midarm circumference (MAC) and triceps skin-fold (TSF), and by biochemical indices, in particular prealbumin (TBPA) and retinol-binding protein (RBP). On admission, no significant differences were found between groups in weight, height, weight for height, MAC, and TSF values. TBPA and RBP, lower than normal in most cases, were not significantly different in the two groups. Furthermore, no differences were observed when children with high-risk leukemia were compared with those at standard risk. In conclusion, children with newly diagnosed leukemia do not seem to present significant nutritional depletion, and their nutritional status is similar to that of children admitted for other nonmalignant acute diseases. However, nutritional indices should be monitored in children with high-risk leukemia because treatment intensity is likely to result in a malnutritional status later, which might be prevented by early adequate nutritional support.


Subject(s)
Leukemia/physiopathology , Nutrition Disorders/etiology , Nutritional Status , Acute Disease , Adolescent , Anthropometry , Child , Child, Preschool , Female , Humans , Incidence , Infant , Leukemia/complications , Male , Nutrition Disorders/epidemiology , Nutrition Disorders/prevention & control , Prealbumin/analysis , Prospective Studies , Retinol-Binding Proteins/analysis , Risk Factors
5.
Pediatr Hematol Oncol ; 13(4): 349-58, 1996.
Article in English | MEDLINE | ID: mdl-8837141

ABSTRACT

Total parenteral nutrition (TPN) is an important issue in supportive care of children with leukemia. We studied 131 consecutive children (87 male, 44 female) with hematological malignancies who received TPN at our center from July 1984 to July 1990 with the aim of evaluating the efficacy and complications of TPN. The use of TPN was associated with lack of any alteration of the anthropometric indexes used in this study. The complications were prevalently metabolic, generally mild, and easily controlled. Laboratory monitoring of nutritional status during TPN is probably of little value in this setting. The feasibility of in-ward preparation of TPN by nurses makes TPN possible at low cost provided that patients are selected carefully.


Subject(s)
Hematologic Neoplasms/therapy , Parenteral Nutrition, Total , Adolescent , Child , Child, Preschool , Energy Intake , Equipment Failure , Feasibility Studies , Female , Hematologic Neoplasms/nursing , Humans , Hyperglycemia/epidemiology , Infant , Leukemia/therapy , Lymphoma, Non-Hodgkin/therapy , Male , Monitoring, Physiologic , Myelodysplastic Syndromes/therapy , Nutritional Status , Parenteral Nutrition, Total/adverse effects , Retrospective Studies , Sepsis/epidemiology
6.
Plant Mol Biol ; 24(3): 515-23, 1994 Feb.
Article in English | MEDLINE | ID: mdl-8123793

ABSTRACT

The Opaque-2 (O2) gene from maize encodes a transcriptional activator of the b-ZIP class. We have isolated and characterized a gene from sorghum, related in sequence to the O2 gene from maize. A single copy of the gene is present in sorghum. Both genomic and cDNA sequences of the O2-related sorghum gene were determined. The sequence is highly homologous to maize O2 both in the promoter and in the coding region. The most closely related sequences contain the b-ZIP domain with only 11 amino acid substitutions in a total of 122 residues. In transient expression assays, the sorghum O2-related coding sequence, expressed from a CaMV 35S promoter, activates expression from the maize b-32 promoter as effectively as that obtained with the maize O2 sequence.


Subject(s)
DNA-Binding Proteins/genetics , Genes, Plant , Plant Proteins/genetics , Poaceae/genetics , Promoter Regions, Genetic , Transcription Factors/genetics , Zea mays/genetics , Amino Acid Sequence , Base Sequence , G-Box Binding Factors , Glucuronidase/biosynthesis , Glucuronidase/genetics , Leucine Zippers/genetics , Molecular Sequence Data , Oligodeoxyribonucleotides , Open Reading Frames , Protein Sorting Signals/genetics , Sequence Homology, Amino Acid , Sequence Homology, Nucleic Acid , Transfection
7.
Eur J Cancer ; 27(6): 758-62, 1991.
Article in English | MEDLINE | ID: mdl-1829920

ABSTRACT

The aggressive radiotherapy and chemotherapy used in conditioning regimens for children with leukaemia undergoing bone marrow transplantation (BMT) cause a severe catabolic state. Total parenteral nutrition (TPN) is indispensable in the management of these patients. 25 children with leukaemia undergoing BMT were studied to evaluate the efficacy of TPN and the value of anthropometric parameters and biochemical variables (albumin, retinol-binding protein and prealbumin) in monitoring nutritional status in the critical post-BMT phase. The complications of TPN were mainly metabolic, generally mild and easily controlled. The hyperalimentation solution and infusion line were not responsible for infection in any patient. The marked variations in anthropometric parameters and albumin expected in such patients were not observed in our children due to the nutritional support given. Prealbumin and retinol-binding protein showed statistically significant, positive variations (P less than 0.01), thus proving sensitive indices of the response to nutritional repletion.


Subject(s)
Bone Marrow Transplantation , Leukemia/therapy , Nutritional Status , Parenteral Nutrition, Total , Adolescent , Anthropometry , Child , Child, Preschool , Combined Modality Therapy , Female , Humans , Kidney/physiopathology , Leukemia/physiopathology , Leukemia/surgery , Liver/physiopathology , Male , Parenteral Nutrition, Total/adverse effects , Retinol-Binding Proteins/metabolism , Serum Albumin/analysis
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