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1.
Ann Oncol ; 32(8): 1025-1033, 2021 08.
Article in English | MEDLINE | ID: mdl-34022376

ABSTRACT

BACKGROUND: Nutritional support in patients with cancer aims at improving quality of life. Whether use of nutritional support is also effective in improving clinical outcomes requires further study. PATIENTS AND METHODS: In this preplanned secondary analysis of patients with cancer included in a prospective, randomized-controlled, Swiss, multicenter trial (EFFORT), we compared protocol-guided individualized nutritional support (intervention group) to standard hospital food (control group) regarding mortality at 30-day (primary endpoint) and other clinical outcomes. RESULTS: We analyzed 506 patients with a main admission diagnosis of cancer, including lung cancer (n = 113), gastrointestinal tumors (n = 84), hematological malignancies (n = 108) and other types of cancer (n = 201). Nutritional risk based on Nutritional Risk Screening (NRS 2002) was an independent predictor for mortality over 180 days with an (age-, sex-, center-, type of cancer-, tumor activity- and treatment-) adjusted hazard ratio of 1.29 (95% CI 1.09-1.54; P = 0.004) per point increase in NRS. In the 30-day follow-up period, 50 patients (19.9%) died in the control group compared to 36 (14.1%) in the intervention group resulting in an adjusted odds ratio of 0.57 (95% CI 0.35-0.94; P = 0.027). Interaction tests did not show significant differences in mortality across the cancer type subgroups. Nutritional support also significantly improved functional outcomes and quality of life measures. CONCLUSIONS: Compared to usual hospital nutrition without nutrition support, individualized nutritional support reduced the risk of mortality and improved functional and quality of life outcomes in cancer patients with increased nutritional risk. These data further support the inclusion of nutritional care in cancer management guidelines.


Subject(s)
Hematologic Neoplasms , Quality of Life , Humans , Length of Stay , Nutritional Support , Prospective Studies
2.
Exp Clin Endocrinol Diabetes ; 116(5): 268-71, 2008 May.
Article in English | MEDLINE | ID: mdl-18589889

ABSTRACT

A 76-year-old patient was admitted with dizzy spells and fainting. Laboratory analysis indicated the syndrome of inappropriate antidiuresis, which was further characterized as type C ("reset osmostat"). Extended workup revealed a hormone - inactive pituitary macroadenoma. After complete transsphenoidal resection, serum sodium levels and plasma and urinary osmolality promptly normalized. Except for the gonadal axis, the anterior pituitary functions remained intact. There was no adenoma recurrence over a five-year follow-up, and repetitive testing on ad libitum fluid intake showed normal sodium concentrations. Thus, the pituitary macroadenoma represents the sole detectable cause for the syndrome of inappropriate antidiuresis in this patient.


Subject(s)
Adenoma/complications , Inappropriate ADH Syndrome/etiology , Pituitary Neoplasms/complications , Adenoma/diagnosis , Adenoma/metabolism , Adenoma/pathology , Aged , Arginine Vasopressin/blood , Hormones/metabolism , Humans , Male , Osmolar Concentration , Pituitary Neoplasms/diagnosis , Pituitary Neoplasms/metabolism , Pituitary Neoplasms/pathology , Sodium/blood , Tumor Burden
3.
Praxis (Bern 1994) ; 96(17): 687-92, 2007 Apr 25.
Article in German | MEDLINE | ID: mdl-17491199

ABSTRACT

We report a female patient who was admitted to the emergency ward with suspected cerebral ischemia and in whom transvenous clot lysis was performed. Following lysis the patient developed recurrent complex partial seizures and treatment with intravenous phenytoin was started. Initial phenytoin serum levels were within the therapeutic range. During the course of the in-hospital treatment a sudden fall of phenytoin serum levels was detected and could not be explained by pharmacokinetic changes. Only when the drug application process was further analysed the reason for the fall in serum levels became obvious. Phenytoin sodium injections had not been administered directly into the veins but had been diluted in 0.9% saline infusions. As a result phenytoin sodium injections precipitated and were retained by the particle filter, thus leading to subtherapeutic phenytoin serum levels.


Subject(s)
Anticonvulsants/blood , Medication Errors , Phenytoin/blood , Aged , Aged, 80 and over , Anticonvulsants/administration & dosage , Anticonvulsants/pharmacokinetics , Diagnosis, Differential , Drug Interactions , Drug Monitoring , Female , Hospitalization , Humans , Injections, Intravenous , Phenytoin/administration & dosage , Phenytoin/pharmacokinetics , Seizures/drug therapy , Sodium Chloride/administration & dosage , Solutions , Status Epilepticus/diagnosis
5.
Postgrad Med J ; 79(928): 106-7, 2003 Feb.
Article in English | MEDLINE | ID: mdl-12612329

ABSTRACT

A patient with simultaneous bilateral spontaneous pneumothorax (SBSP) due to pulmonary and pleural manifestations of recurrent multiple myeloma is presented. The patient died in shock of unknown cause. The diagnosis was suspected from pleural fluid examination showing an exudate with numerous plasmocytes. Macroscopically and histologically, the visceral organs and the bone marrow were infiltrated with multiple monoclonal proliferations of plasma cells staining positively for IgG and lambda chains. SBSP is a rare condition and may be caused by trauma, parenchymal lung disease, infections, or neoplasms. This is the first report of SBSP caused by pleuropulmonary infiltration of multiple myeloma.


Subject(s)
Multiple Myeloma/complications , Pleural Neoplasms/complications , Pneumothorax/etiology , Aged , Fatal Outcome , Female , Humans , Multiple Myeloma/pathology , Pleural Neoplasms/pathology , Pneumothorax/diagnostic imaging , Radiography , Recurrence
6.
J Biol Chem ; 274(27): 18965-72, 1999 Jul 02.
Article in English | MEDLINE | ID: mdl-10383395

ABSTRACT

Autosomal dominant neurohypophyseal diabetes insipidus is caused by mutations in the gene encoding the vasopressin precursor protein, prepro-vasopressin-neurophysin II. We analyzed the molecular consequences of a mutation (DeltaG227) recently identified in a Swiss kindred that destroys the translation initiation codon. In COS-7 cells transfected with the mutant cDNA, translation was found to initiate at an alternative ATG, producing a truncated signal sequence that was functional for targeting and translocation but was not cleaved by signal peptidase. The mutant precursor was completely retained within the endoplasmic reticulum. The uncleaved signal did not affect folding of the neurophysin portion of the precursor, as determined by its protease resistance. However, formation of disulfide-linked aggregates indicated that it interfered with the formation of the disulfide bond in vasopressin, most likely by blocking its insertion into the hormone binding site of neurophysin. Preventing disulfide formation in the vasopressin nonapeptide by mutation of cysteine 6 to serine was shown to be sufficient to cause aggregation and retention. These results indicate that the DeltaG227 mutation induces translation of a truncated signal sequence that cannot be cleaved but prevents correct folding and oxidation of vasopressin, thereby causing precursor aggregation and retention in the endoplasmic reticulum.


Subject(s)
Endoplasmic Reticulum/metabolism , Protein Precursors/genetics , Protein Sorting Signals/metabolism , Vasopressins/genetics , Amino Acid Sequence , Amino Acid Substitution , Animals , COS Cells , Diabetes Insipidus , Disulfides/metabolism , Guanosine/metabolism , Molecular Sequence Data , Mutagenesis, Site-Directed , Protein Folding , Protein Precursors/metabolism , Vasopressins/metabolism
7.
Mol Genet Metab ; 67(1): 89-92, 1999 May.
Article in English | MEDLINE | ID: mdl-10329029

ABSTRACT

Autosomal-dominant familial neurohypophyseal diabetes insipidus (adFNDI) is caused by heterozygous mutations in the gene encoding vasopressin-neurophysin II (AVP-NPII) on chromosome 20p13. We analyzed the AVP-NP II gene in a family with adFNDI by direct sequencing. A novel C to T transition (289C-->T in the cDNA, resulting in the substitution of Arg 97 by Cys (R97C) in the prepro-AVP-NPII precursor molecule) was identified in the gene region encoding neurophysin II in the index patient. This amino acid change is thought to result in the formation of an incorrectly folded hormone precursor, which may lead to chronic neurotoxicity and explain the dominant inheritance of the disease.


Subject(s)
Arginine Vasopressin/genetics , Diabetes Insipidus/genetics , Genes, Dominant , Mutation , Neurophysins/genetics , Oxytocin , Protein Precursors/genetics , DNA Mutational Analysis , Female , Humans , Male , Models, Genetic , Pedigree
9.
Infection ; 27(4-5): 259-60, 1999.
Article in English | MEDLINE | ID: mdl-10885838

ABSTRACT

The incidence of severe invasive infections caused by Streptococcus pyogenes, a group A streptococcus (GAS), has increased in the past 10 years. Most cases occur outside of the hospital setting. We report on two patients with nosocomial streptococcal toxic shock syndrome (StrepTSS). In patient 1 the syndrome was associated with the development of necrotizing fasciitis following inguinal hernia repair. Patient 2 suffered from StrepTSS shortly after receiving a tetanus vaccine in her left deltoid. Epidemiologic investigations of these cases, which were noted within 48 hours of each other, showed that the same surgeon performed the vaccination on patient 2 after assisting a colleague during the hernia repair procedure on patient 1. He was found to be a nasal carrier of GAS. All GAS isolates from the patients and the surgeon were indistinguishable by pulsed field gel electrophoresis. PCR analysis demonstrated the presence of streptococcal pyogenic exotoxins A and F. All strains were of the T-1 serotype and possessed the gene for M-protein 1. This report demonstrates that a virulent strain of GAS may be spread by asymptomatically colonized medical personnel via the air route.


Subject(s)
General Surgery , Infectious Disease Transmission, Professional-to-Patient , Shock, Septic/diagnosis , Shock, Septic/transmission , Streptococcal Infections/diagnosis , Streptococcal Infections/transmission , Streptococcus pyogenes/isolation & purification , Adult , Carrier State , DNA, Bacterial/analysis , Electrophoresis, Gel, Pulsed-Field , Female , Follow-Up Studies , Health Personnel , Humans , Male , Middle Aged
12.
J Clin Endocrinol Metab ; 81(1): 192-8, 1996 Jan.
Article in English | MEDLINE | ID: mdl-8550751

ABSTRACT

Autosomal dominant neurohypophyseal diabetes insipidus (ADNDI) is a rare variant of idiopathic central diabetes insipidus. Several different mutations in the human vasopressin-neurophysin II (AVP-NP II) gene have been described. We studied nine family members from three generations of an ADNDI pedigree at the clinical, morphological, and molecular levels. AVP concentrations were measured during diagnostic fluid restriction tests. Coronal and sagittal high resolution T1-weighted images of the pituitary were obtained from affected and healthy family members. PCR was used to amplify the AVP-NP II precursor gene, and PCR products were directly sequenced. Under maximal osmotic stimulation, AVP serum levels were close to or below the detection limit in affected individuals. Magnetic resonance imaging studies revealed the characteristic hyperintense ("bright spot") appearance of the posterior pituitary in two healthy family members. This signal was absent in all four ADNDI patients examined. The coding sequences of AVP and its carrier protein, neurophysin II, were normal in all family members examined. Affected individuals showed a novel single base deletion (G 227) in the translation initiation codon of the AVP-NP II signal peptide on one allele. The mutation in the AVP-NP II leader sequence appears to be responsible for the disease in this kindred, possibly by interfering with protein translocation. The absence of the hyperintense posterior pituitary signal in affected individuals could reflect deficient posterior pituitary function.


Subject(s)
Arginine Vasopressin/genetics , Diabetes Insipidus/genetics , Neurophysins/genetics , Pituitary Diseases/genetics , Point Mutation , Protein Precursors/genetics , Protein Sorting Signals/genetics , Adolescent , Adult , Aged , Base Sequence , Codon , Humans , Middle Aged , Molecular Sequence Data , Pituitary Gland, Posterior
13.
J Clin Invest ; 95(1): 179-86, 1995 Jan.
Article in English | MEDLINE | ID: mdl-7529258

ABSTRACT

Insulin-like growth factor (IGF) circulates in blood in two large molecular mass forms of 150 and 40 kD. Under normal conditions, most of the IGF is bound to the 150-kD complex by which it is retained in the circulation and therefore unable to exert acute insulin-like actions. The aim of this study was to answer the question whether or not IGF in the 40-kD complex is bioavailable to insulin target tissues and thus can cause acute insulin-like effects in vivo. Intravenously injected 1:1 molar recombinant human (rh) IGF I/rhIGF binding protein (BP)-3 complex lowered blood glucose and stimulated glycogen synthesis in diaphragm of hypophysectomized, but not of normal rats. The serum half-lives of the two components of the complex were similar to each other, but considerably shorter in hypox than in normal rats. On neutral gel filtration of serum both components of the injected complex appeared predominantly in the 150-kD region in normal rats. In hypox rats which lack the 150-kD complex they were found in the 40-kD region and disappeared rapidly from the circulation. We conclude that in the absence of the 150-kD complex, IGF associated with the 40-kD complex can rapidly leave the vascular compartment, reach insulin or type 1 IGF receptors and exert acute insulin-like effects.


Subject(s)
Carrier Proteins/pharmacology , Hypophysectomy , Insulin-Like Growth Factor I/pharmacology , Animals , Blood Glucose/analysis , Diaphragm/metabolism , Drug Interactions , Glycogen/metabolism , Half-Life , Injections, Intravenous , Insulin/pharmacology , Insulin-Like Growth Factor Binding Proteins , Macromolecular Substances , Male , Protein Binding , Rats , Recombinant Proteins/pharmacology
14.
FEBS Lett ; 334(1): 23-6, 1993 Nov 08.
Article in English | MEDLINE | ID: mdl-7693512

ABSTRACT

Insulin-like growth factor binding proteins (IGFBPs) modulate IGF action. Proteolytic cleavage of IGFBPs yields lower molecular forms with reduced ability to bind IGFs, thereby increasing IGF bioavailability. In serum from normal adult rats, we found a proteolytic activity for IGFBP-3, presumably a cation-dependent serine protease. It is lacking in serum from hypophysectomized rats and restored by infusion of growth hormone (GH), but not IGF I. Thus, IGF I does not appear to mediate the GH effect on IGFBP-3 proteolysis. Rather, GH seems to modulate IGF action indirectly via alteration of IGFBP-3 structure.


Subject(s)
Carrier Proteins/metabolism , Growth Hormone/pharmacology , Insulin-Like Growth Factor I/pharmacology , Serine Endopeptidases/blood , Somatomedins/metabolism , Animals , Blotting, Western , Electrophoresis, Polyacrylamide Gel , Hypophysectomy , Insulin-Like Growth Factor Binding Proteins , Male , Rats
15.
Biochem Biophys Res Commun ; 179(1): 579-85, 1991 Aug 30.
Article in English | MEDLINE | ID: mdl-1715698

ABSTRACT

IGFBP-3 is the predominant IGFBP in serum and the major IGFBP secreted by osteoblasts. Native and recombinant IGFBP-3 and a truncated form lacking the carboxyterminal third were tested for their effects on 2 osteoblastic cell lines. Intact but not truncated IGFBP-3 blocked IGF I-stimulated DNA and glycogen synthesis. Inhibition was dose-dependent and found whenever the concentration of intact IGFBP-3 exceeded the concentration of IGF I. Truncated IGFBP-3 appears to result from proteolytic cleavage and does occur in vivo. The loss of inhibition by IGFBP-3 may be regulated at the site of IGF target cells and thus be essential for IGF I-induced osteoblast growth.


Subject(s)
Carrier Proteins/physiology , DNA Replication/drug effects , Insulin-Like Growth Factor I/pharmacology , Osteoblasts/physiology , Signal Transduction , Animals , Carrier Proteins/genetics , Cell Line , Glucose/metabolism , Glycogen/biosynthesis , Humans , Insulin/pharmacology , Insulin-Like Growth Factor Binding Proteins , Insulin-Like Growth Factor I/metabolism , Osteoblasts/drug effects , Osteosarcoma , Rats , Recombinant Proteins/metabolism , Recombinant Proteins/pharmacology , Signal Transduction/drug effects
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