[Dynamic investigation of nutritional risk in patients with malignant tumor during hospitalization].

Objective: To prospectively investigate the changes in nutritional status of patients with malignant tumors during hospitalization by using nutritional risk screening (NRS2002), and to analyze the correlation between the nutritional status and clinical outcomes . Methods: This was a prospective and parallel research done by multi-center collaboration from 34 hospitals in China from June to September 2014.Hospitalized patients with malignant tumors inthese departments (Department of Gastroenterology, respiratory medicine, oncology, general surgery, thoracic surgery and geriatrics)were investigated. Only the patients with age≥ 18 years and hospitalization time between 7-30 days were included. During hospitalization, the physical indexes of human bodywere measured, and the NRS 2002 scores, and monitored the nutritional support at the time points of admission and 24 hours before discharge were recorded.And whether there was a nutritional risk in hospitalized patients and its association with clinical outcomes were investigated. Results: A total of 2 402 patients with malignancies were enrolled in this study. Seventy fourpatients who did not complete NRS2002 were eliminated, and 2 328 patients were included. The number of the main diseases was the top five, including 587 cases of colorectal cancer, 567 cases of lung cancer, 564 cases of gastric cancer, 146 cases of esophageal cancer, and 119 cases of liver tumor. At the time of discharge, compared with admission, the BMI, body weight, grip and calf circumferences of patients with malignant tumor were significantly decreased (P<0.05). The total protein, albumin, prealbumin and hemoglobin were significantly lower than those at admission (P<0.05). In 2 328 patients who were completed nutritional risk screening, the rate of malnutrition at admission was 11.1% (BMI =18.5, 258/2 328) and the rate of malnutrition at discharge was 10.9% (BMI =18.5, 254/2 328), there were no significant differences (χ(2)=0.019 7, P=0.888). There were 1 204 patients with nutritional risk at admission (51.7%, NRS2002 score≥3)and 1 352 patients with nutritional risk at discharge (58.1%, NRS2002 score≥3), with significant differences (χ(2)=49.9, P<0.001). The incidence of nutritional risk in patients with colorectal, stomach, and lung tumors at discharge was significantly higher than that at admission (P<0.05). The infective complications and other complications of patients with nutritional risk were significantly greater than those without nutritional risk at admission and at discharge.ICU hospitalization stay of patients with nutritional risk was increased significantly than those without nutritional risk at admission(P=0.042). Hospitalization expenses of patients with nutritional risk was increased significantly than those of patients without nutritional risk at discharge(P<0.01). Conclusion: The patients with malignant tumor have a higher incidence rate of malnutrition at both admission and discharge and malnutritionhas correlation with adverse clinical outcomes.The aboveindicators did not improve significantly at discharge.Doctors should pay more attention to the nutritional status (screening and evaluation)of patients before discharge and use appropriate and adequate nutrition support in order to prevent the weight loss and improve the life quality of patients.

Nucleotide sequence of the 5' region of the human platelet-derived growth factor A-chain gene.

We have isolated and characterized genomic clones of the 5' region of the human PDGF A-chain gene. The putative "TATAA" box was identified 876 bp upstream of the translation initiation site. A significant number of potential regulatory elements were identified in DNA sequences upstream of the "TATAA" box and were also found within the introns sequenced. The DNA sequence results differ significantly from those reported for the PDGF B-chain gene, suggesting a basis for the expression of the PDGF A-chain gene and the B-chain gene under very different conditions.

Expression of nucleotide pyrophosphatase and alkaline phosphodiesterase I activities of PC-1, the murine plasma cell antigen.

Nucleotide pyrophosphatase (EC 3.6.1.9) is a membrane enzyme purified from a number of mammalian sources that may have alkaline phosphodiesterase I (EC 3.1.4.1) activity as well. The mol. wt and subunit structure of this membrane glycoprotein are similar to that of the murine plasma cell alloantigen, PC-1. The PC-1 protein is a disulfide-bonded dimer of identical 115 kDa polypeptides that is selectively expressed on B lineage cells that have reached the degree of maturation associated with immunoglobulin secretion. It also has restricted expression in certain non-lymphoid tissues. In this report, we show that alkaline phosphodiesterase I activity parallels PC-1 mRNA expression in a number of B lineage cell lines at different stages of differentiation. Furthermore, we demonstrate increases in both nucleotide pyrophosphatase and alkaline phosphodiesterase I enzymatic activities in transiently transfected COS-7 cells expressing a cloned PC-1 cDNA construction. These results extend our previous immunological and correlative studies and directly ascribe an enzymatic activity to this cell surface differentiation antigen. These experiments also demonstrate that a single protein is responsible for both alkaline phosphodiesterase I and nucleotide pyrophosphatase activities.

Identification of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity associated with the mouse plasma cell differentiation antigen PC-1.

The protein responsible for both nucleotide pyrophosphatase (EC 3.6.1.9) and alkaline phosphodiesterase I (EC 3.1.4.1) activities was purified from MOPC 315 plasmacytoma cells. A single SDS/PAGE-purified 115-kDa protein band was used to produce a rabbit polyclonal antiserum. This antibody preparation precipitated alkaline phosphodiesterase I activity, indicating that the SDS/PAGE-purified protein was nucleotide pyrophosphatase/alkaline phosphodiesterase I. When used for Western blot analysis, the antiserum detected a 115-kDa protein as well as a 220-kDa protein band. Multiple overlapping cDNA clones were isolated from a cDNA expression library screened with this anti-nucleotide pyrophosphatase/alkaline phosphodiesterase I antiserum. Sequence analysis indicated that the isolated cDNA clones encoded PC-1, a murine plasma cell differentiation antigen. To confirm the suspected enzymatic identity of PC-1, a recombinant PC-1 fusion protein was expressed in bacteria, purified, and used to produce another rabbit polyclonal antiserum. This antiserum likewise immunoprecipitated alkaline phosphodiesterase I activity and recognized the 115-kDa and 220-kDa proteins in Western blot analyses of cell extracts. Furthermore, expression of nucleotide pyrophosphatase/alkaline phosphodiesterase I corresponded directly with mRNA and protein levels of PC-1 in cells known to express different levels of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity. Finally, steroid induction of enzymatic activity was mirrored by levels of PC-1 mRNA and protein expression. Together, these data indicate that the plasma cell differentiation antigen PC-1 is a membrane-bound enzyme, nucleotide pyrophosphatase/alkaline phosphodiesterase I.

Expression of mitogenically active human recombinant platelet-derived growth factor A-chain.

Expression vectors encoding cDNAs for the human platelet-derived growth factor (PDGF) A-chain (pJKl) and murine dihydrofolate reductase (pTKDHFR) were cotransfected into dihydrofolate reductase-deficient Chinese hamster ovary cells. Methotrexate-induced coamplification of clones, expressing PDGF A-chain resulted in enhanced levels of A-chain-specific DNA, RNA and protein. A 30,500 Mr protein was immunoprecipitated with PDGF antisera from the conditioned media of metabolically labeled cells. Reducing conditions resolved the A-chain-specific protein into two polypeptides of 16,500 and 17,000 Mr, confirming the homodimeric nature of the recombinant A-chain protein. The recombinant PDGF A-chain produced constitutively by these amplified clones proved to be mitogenically active. The secretion of a recombinant PDGF A-chain into conditioned media may provide a continuous and abundant source of PDGF A.A dimers, normally produced by specific tissues in only minute quantities. Future purification of the recombinant homodimeric A-chain will allow the assessment of its ability to function in clinical applications such as wound healing.

cDNA clones reveal differences between human glial and endothelial cell platelet-derived growth factor A-chains.

Human platelet-derived growth factor (PDGF) is a potent mitogenic polypeptide which is believed to be a heterodimer of A- and B-chains stabilized by interchain disulphide bonds. The B-chain of PDGF is encoded by the c-sis gene, the normal cellular homologue of the transforming gene of the simian sarcoma virus (SSV). cDNA clones of the B-chain from both normal and transformed cells have mutually consistent DNA sequences. Recently, an A-chain cDNA clone (D-1) was isolated from a transformed human glial cell cDNA library. We report the complete sequence of an A-chain cDNA clone (BT-1) isolated from a normal human umbilical vein endothelial (HUVE) cell cDNA library. BT-1 differs from the sequence of the D-1 clone by a 69 base pair deletion containing the predicted carboxy terminus of the protein. The mRNA levels of the A- and B-chains of PDGF in HUVE cells were analysed and shown to respond differently to the endothelial cell growth factor (ECGF).

Isolation and sequencing of a cDNA clone homologous to the v-sis oncogene from human endothelial cells.

A clone containing the 3' end of the mRNA for the human c-sis gene (homologous to the B chain of platelet-derived growth factor) was isolated from a cDNA library derived from human umbilical vein endothelial cells and then sequenced. The analysis of possible translation products in all three reading frames indicated that the A chain of platelet-derived growth factor was not coded for within the 3' end of the c-sis mRNA. The 3' end of the mRNA for c-sis is contained in or adjacent to exon 6.

Platelet-derived growth factor: roles in normal and v-sis transformed cells.

Platelet-derived growth factor (PDGF) is the most potent mitogenic protein in human serum. The normal roles of this protein may relate to its potent mitogenic properties and its activities in directed cell migration and at sites of wounds. PDGF is a heterodimeric protein of approximately 30,000 molecular weight; one polypeptide chain of PDGF is highly homologous to the predicted amino acid sequence of p28v-sis, the putative transforming protein of simian sarcoma virus (SSV), suggesting a major role of growth factor activity in transformation by SSV. PDGF-like growth promoting activity is found in SSV-transformed cells and is secreted into conditioned media where it appears to interact with PDGF cell surface receptors to stimulate 3H-thymidine incorporation into DNA of cells secreting this protein. Transformation by SSV may in part be mediated by the autocrine stimulation of cell growth by the PDGF-like mitogenic properties of the transforming protein of SSV.

The formation of erythrocyte membrane proteins during erythropoietin-induced differentiation.

The effect of erythropoietin on the synthesis of the proteins characteristic of mature erythrocyte membranes was studied in cultures of bone marrow cells from adult, polycythemic rats. Stimulated synthesis of the major glycoprotein, glycophorin, was maximal at 30 h and fell to control level by 66 h. Stimulated synthesis of the major integral membrane protein, band 3, occurred at about 18 h was maximal at 66 h, and fell to control level by 114 h. In contrast, stimulated hemoglobin synthesis did not start until after 24 h, was maximal at 96 h, and was at control level at 114 h. Erythropoietin had, in addition, a transient effect on the synthesis of some membrane proteins found in marrow cells but not in mature red cells.