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Biomedical subjects

Z Qu

Publications and source records attributed to Z Qu.

At least 109 records · Page 6Linked to original sources
PubMed1997

Immunolocalization of bFGF in pterygia: association with mast cells.

PURPOSE: To examine the expression of basic fibroblast growth factor in pterygia and determine whether mast cells contain basic fibroblast growth factor (bFGF) in this disease process. METHODS: Formalin-fixed paraffin-embedded tissue samples of pterygia (n = 14) were used to study the expression of bFGF with immunohistochemistry. Seven samples were also double labeled with specific antibodies to bFGF and tryptase (a specific mast cell marker). RESULTS: In all tissue samples examined, bFGF was specifically localized in blood vessels, epithelium, and a subset of connective tissue cells. The majority of bFGF-positive connective tissue cells were also tryptase positive (90.4 +/- 3.6%). Nearly all the tryptase-positive cells (mast cells) in the pterygia tissues coexpressed bFGF (98 +/- 1.5%). CONCLUSIONS: These findings suggest that bFGF may have biologic effects on the epithelium and blood vessels in pterygia, with epithelial and endothelial cells as a possible source. In addition, mast cells contain bFGF in the pterygia tissues examined in this study. The mast cells may serve as an additional source of bFGF, possibly modulating a variety of cell types as well as the extracellular matrix in pterygia.

Adult↗
PubMed1997

Type 2 cytokine serum levels in healthy sickle cell disease patients.

Sickle cell disease (SCD) is characterized by significant morbidity and early mortality. Children with this hemoglobinopathy exhibit many of the manifestations associated with immunodeficiency disorders. Serum was obtained from 56 healthy SCD subjects and 45 normal healthy controls. Type 2 cytokines interleukin (IL)-4, IL-6, and IL-10 serum levels were measured. Concentrations were determined by reference to a standard curve, and results were expressed in pg/mL. Results revealed significant levels of IL-4 in 6 (13%) of 45 SCD patients compared with 1 (2%) of 45 controls. Increased levels of IL-6 were present in 35 (78%) of 45 SCD patients and 12 (41%) of 29 controls. Elevated levels of IL-10 were detectable in 13 (41%) of 42 SCD patients and 1 (4%) of 25 controls. High circulating levels of type 2 cytokines may suppress both humoral and cell-mediated immune functions in SCD, with resultant increased morbidity.

Adolescent↗
PubMed1997

[Effects of oxidatively modified low density lipoprotein and very low density lipoprotein on the expression of MCP-1 in macrophages].

OBJECTIVE: To examine whether oxidatively modified low density lipoprotein (OX-VLDL) and very low density lipoprotein (OX-VLDL) induce the expression of MCP-1 mRNA and protein by rabbit peritoneal exudate macrophages, and to clarify what a role of both lipoproteins play in atherogenesis. METHODS: After exposure of the macrophages to 25 micrograms/ml of LDL, VLDL, OX-LDL and OX-VLDL respectively, and a 24 hour incubation at 37 degrees C, the total RNA was extracted from the cells by guanidinium isothiocyanate method, and the media conditioned by the cultured macrophages were collected. Meanwhile, MCP-1 protein in the conditioned media was determined by using sandwich ELISA. Monocyte migration induced by the media was assayed by micropore filter method using modified Boyden chamber. RESULTS: After a 24 hour exposure to OX-LDL and OX-VLDL, the MCP-1 mRNA expression in macrophages was markedly increased (3.2-fold and 3.4-fold, respectively), and the level of MCP-1 protein was also increased (2.2-fold and 2.5-fold, separately), and furthermore, the monocyte migration distance was significantly increased. However, the expression of MCP-1 mRNA and protein was only slightly increased when exposed to LDL or VLDL. CONCLUSIONS: Rabbit peritoneal exudate macrophages can express MCP-1 mRNA and protein, and OX-LDL and OX-VLDL induce stronger MCP-1 mRNA and protein expression in the cells.

Animals↗
PubMed1996

The synapse-associated protein rapsyn regulates tyrosine phosphorylation of proteins colocalized at nicotinic acetylcholine receptor clusters.

Protein tyrosine phosphorylation has been suggested to play an important role in the clustering of the nicotinic acetylcholine receptor (AChR) at the developing neuromuscular junction. Recent studies have shown that the 43-kDa synapse-associated protein rapsyn induces clustering of the AChR in heterologous expression systems. In this study we examined whether tyrosine phosphorylation is involved in this rapsyn-induced AChR clustering. Rapsyn-induced AChR clusters in fibroblasts contain phosphotyrosine, as detected using immunofluorescent labeling with anti-phosphotyrosine antibodies. No anti-phosphotyrosine staining of rapsyn clusters is seen in the absence of AChR expression, indicating that the AChR is required for the appearance of phosphotyrosine at clusters. In addition, coexpression of rapsyn with the AChR induces the tyrosine phosphorylation of the beta amd delta subunits of the AChR. Surprisingly, mutation of the tyrosine phosphorylation sites in the AChR did not inhibit rapsyn-induced clustering of the AChR and clusters of the mutant AChRs still contained high levels of phosphotyrosine. Experiments with single AChR subunits demonstrate that the alpha subunit of the AChR appears to be necessary and sufficient for codistribution of phosphotyrosine with rapsyn-induced clusters of AChR subunits. Finally, transfection of cells with rapsyn activates cellular protein tyrosine kinase activity, resulting in the tyrosine phosphorylation of several membrane-associated proteins. These results suggest that rapsyn may therefore regulate clustering at least in part by regulating the tyrosine phosphorylation of cellular proteins.

Animals↗
PubMed1996

Partial purification of smooth muscle cell derived growth factor.

The serum free medium conditioned by cultured rabbit aortic smooth muscle cells was partially purified using ultrafiltration and heparin affinity chromatography. Incorporation of [3H]-thymidine (3H-TdR) into cell DNA was used to measure the mitogenic activity of the fractions from chromatography for NIH 3T3 fibroblasts. The molecular weight and the iso-electric point of these fractions were determined by NaDodSO4-polyacrylamide gel electrophoresis (SDS-PAGE) and iso-electric focusing, respectively. The results showed that the protein eluted in 1.0-1.6 mol/L NaCl from the heparin-Sepharose was mitogenic for 3T3 cells, and this protein had a molecular weight of 22.8-26.7 ku and an iso-electric point of about 4.6. The fact that the above-mentioned biochemical properties differed from that of PDGF, IGF and FGF suggests that this mitogenic protein may be a separate growth factor.

3T3 Cells↗
PubMed1996

Determinants of plasma concentrations of insulin-like growth factor-I and albumin and their hepatic mRNAs: the role of dietary protein content and tumor necrosis factor in malnourished rats.

Protein restriction decreases plasma concentrations of albumin and insulin-like growth factor-I (IGF-I) by reducing their hepatic mRNA levels, whereas protein restriction increases IGF-I binding protein-2 (IGFBP-2) gene expression in the liver. Tumor necrosis factor (TNF), as an inducer of the injury response, decreases plasma albumin concentration and albumin mRNA in the liver. The present study was designed to evaluate the effects of protein repletion and TNF on plasma albumin and IGF-I and their mRNAs and IGFBP-2 mRNA in the liver of protein-restricted rats. After 2 weeks of feeding a 2% casein diet, rats were assigned to four groups according to either being refed with a 2% or 20% casein diet or receiving saline or TNF by intraperitoneal injection (50 microg/kg x d) for 4 days. Plasma IGF-I and albumin were assayed. Hepatic mRNAs of IGF-I, albumin, and IGFBP-2 were determined. Protein repletion increased plasma concentrations of IGF-I and albumin and their mRNA content in the liver, but decreased IGFBP-2 mRNA. TNF did not alter plasma IGF-I concentration but did increase hepatic IGF-I mRNA in protein-repleted animals, and plasma albumin concentration was significantly decreased with unaltered hepatic albumin mRNA. Thus, protein repletion of malnourished rats increased plasma IGF-I and albumin concentrations in association with increased expression of their mRNAs in the liver. However, plasma albumin but not IGF-I decreased following TNF in protein-restricted rats, whereas TNF increased hepatic IGF-I mRNA in protein-repleted rats. Thus, only plasma albumin concentration responds to both principal determinants, diet and injury, in the development of malnutrition.

Animals↗
PubMed1996

Protein and lipid refeeding changes protein metabolism and colonic but not small intestinal morphology in protein-depleted rats.

In this study, we fed rats a 2% casein AIN 76 diet for 2 wk to produce protein malnutrition. We determined in these animals the effects of different concentrations of dietary protein refeeding (2% and 20% casein) on recovery and gut mucosal repletion and the potential role of type of dietary fat in the regulation of protein metabolism and mucosal growth by providing conventional long-chain triglyceride (LCT), a structured lipid composed of long-, medium- and short-chain fatty acids (SC/SL), or a physical mixture of the same components present in the structured lipid given as individual pure triglycerides (SC/PM) along with adequate amounts of protein and energy. The results confirmed that protein malnutrition can be reversed rapidly by protein refeeding, as indicated by an increase in body weight, positive nitrogen balance, liver growth and elevations in plasma concentrations of insulin-like growth factor-1, leucine and albumin. In the colon, crypt cell number, crypt depth and number of crypt cells in the rapidly proliferating fraction of the colon were greater in rats fed the higher protein diet. However, the general architecture of small intestinal mucosa, including duodenum, jejunum and ileum, was not affected by protein malnutrition. Although the number of colonic cells was similar with fat refeeding, there were significantly fewer displaying the proliferating cell nuclear antigen in the colonic epithelium when rats were fed SC/PM compared with SC/SL. Therefore, changes in colonic mucosal proliferation were only seen with repletion by adequate protein and by SC/SL feeding.

Absorption↗
PubMed1996

Characterization of the murine antibody response to peptides representing the variable domains of the major outer membrane protein of Chlamydia pneumoniae.

In an attempt to gain more knowledge about the immunogenicity of the variable domains (VDs) of the major outer membrane protein (MOMP) of Chlamydia pneumoniae, peptides representing these areas were used to immunize BALB/c and C57BL/6 mice. Antisera to the peptides and to peptides conjugated to keyhole limpet hemocyanin (KLH) were characterized by their ability to recognize the immunizing peptide and elementary bodies (EBs) of C. pneumoniae by enzyme-linked immunosorbent assay (ELISA) and Western blot (immunoblot). In addition, antiserum was analyzed for its molecular specificity by a pepscan as well as its in vitro neutralizing ability. In general, results obtained with antisera to the peptides paralleled the results obtained with the antisera to the KLH-conjugated peptides except that the titers or strength of reaction in the assays was less. Antisera to the VDs in both strains of mice gave ELISA titers to the homologous VD peptide ranging from 1,000 to >64,000. The strength of reactivity with the reduced MOMP as judged by Western blot, in most cases, paralleled the ELISA titer to the peptide. However, only antisera raised in both strains of mice to the VD1 and VD4 peptides reacted strongly with the EBs, suggesting surface exposure of these VDs. In addition, antisera to VD3 from C57BL/6 mice gave strong reactivity to EBs. By pepscan analysis antisera from both strains of mice reacted with several VD1 and VD3 octameric peptides, with weaker reactivity being seen with the octameric peptides in the other two VDs. This was in contrast to antisera raised to EBs of C. pneumoniae TW-183, which identified two immunogenic regions, one in VD1 and the other mapped to VD4. While antisera raised to EBs strongly neutralized the infectivity of C. pneumoniae, none of the peptide antisera was able to neutralize. In addition, peptides to the VDs were not able to block the neutralizing ability of the antisera to EBs of C. pneumoniae. Therefore, these results suggest that the VDs of the MOMP of C. pneumoniae are surface exposed but do not elicit neutralizing antibodies when linear peptides representing them are used as the immunogen.

Animals↗
PubMed1996

Growth hormone stimulates tyrosine phosphorylation of JAK2 and STAT5, but not insulin receptor substrate-1 or SHC proteins in liver and skeletal muscle of normal rats in vivo.

GH has been shown to stimulate tyrosine phosphorylation of JAK2, several STAT proteins, insulin receptor substrate-1 (IRS-1), and SHC proteins in cultured cells. The goal of this study was to determine GH effects on protein tyrosine phosphorylation in liver and skeletal muscle of normal rats in vivo. Nonfasted male Sprague-Dawley rats (225-250 g) were injected with GH iv, and tissues were obtained after 5, 15, 30, or 60 min. At a maximally effective GH dose (1.5 mg/kg body weight), phosphotyrosine antibody immunoblots demonstrated marked stimulation of the tyrosine phosphorylation of JAK2 (maximal at 5 min) and a 95,000 Mr protein (maximal at 15 min) in both liver and skeletal muscle. The 95,000 Mr protein was recognized and immunodepleted by STAT5 antibody, but not by other STAT protein antibodies. Although basal tyrosine phosphorylation of IRS-1 and SHC was evident, GH did not stimulate tyrosine phosphorylation of either of these proteins in liver or skeletal muscle. In conclusion, GH stimulates the tyrosine phosphorylation of JAK2 and STAT5, but not IRS-1, SHC, or other STAT proteins in liver and skeletal muscle of normal rats. These results differ from findings in cultured cells and support the concept that selectivity for tyrosine kinase substrates is an important determinant of postreceptor signaling specificity in vivo.

Adaptor Proteins, Signal Transducing↗
PubMed1996

The Synapse-Associated Protein Rapsyn Regulates Tyrosine Phosphorylation of Proteins Colocalized at Nicotinic Acetylcholine Receptor Clusters

Protein tyrosine phosphorylation has been suggested to play an important role in the clustering of the nicotinic acetylcholine receptor (AChR) at the developing neuromuscular junction. Recent studies have shown that the 43-kDa synapse-associated protein rapsyn induces clustering of the AChR in heterologous expression systems. In this study we examined whether tyrosine phosphorylation is involved in this rapsyn-induced AChR clustering. Rapsyn-induced AChR clusters in fibroblasts contain phosphotyrosine, as detected using immunofluorescent labeling with anti-phosphotyrosine antibodies. No anti-phosphotyrosine staining of rapsyn clusters is seen in the absence of AChR expression, indicating that the AChR is required for the appearance of phosphotyrosine at clusters. In addition, coexpression of rapsyn with the AChR induces the tyrosine phosphorylation of the beta amd delta subunits of the AChR. Surprisingly, mutation of the tyrosine phosphorylation sites in the AChR did not inhibit rapsyn-induced clustering of the AChR and clusters of the mutant AChRs still contained high levels of phosphotyrosine. Experiments with single AChR subunits demonstrate that the alpha subunit of the AChR appears to be necessary and sufficient for codistribution of phosphotyrosine with rapsyn-induced clusters of AChR subunits. Finally, transfection of cells with rapsyn activates cellular protein tyrosine kinase activity, resulting in the tyrosine phosphorylation of several membrane-associated proteins. These results suggest that rapsyn may therefore regulate clustering at least in part by regulating the tyrosine phosphorylation of cellular proteins.

Journal Article↗
PubMed1996

[Experimental study on delayed effect of external skin expansion].

In using the external skin expander, we found that the expanded skin had the feature similar to a delayed flap. To study its mechanism, we chose 20 New Zealand rabbits and divided them into 2 groups randomly. The skin on the animal's back in the experimental group was expanded with the external skin expander. The laser Doppler flowmeter (LDF) and oxyhemograph (SpO2) were applied to detect skin microcirculation. The survival area and the results of microangiography of the two groups were compared. Results showed that the value of LDF of the expanded skin increased and the value of SpO2 returned to its origingal level at 12 days after expansion. The survival area in the experimental group was larger than the control. Microangiographic examinations indicated that the subcutaneous vascular anastomoses were obviously increased in the experimental group. We conclude that external skin expansion does not affect the quality of the expanded skin, and its effect is similar to delay technique.

Animals↗
PubMed1996

[Effects of oxidized low density lipoprotein and very low density lipoprotein on the expression of MCP-1 by monocytes].

Monocyte chemoattractant protein-1 (MCP-1) is a potent chemotatic factor for monocytes. This study aimed at examination of the effects of oxidized low density lipoprotein (OX-LDL) and oxidized very low density lipoprotein (OX-VLDL) on the expression of MCP-1 mRNA and protein by monocytes. The guanidinium isothiocyanate method was used to extract total RNA from monocytes which were exposed to LDL, OX-LDL, VLDL and OX-VLDL for 24 hours respectively and the monocyte derived conditioned media collected. MCP-1 mRNA expression in monocytes was examined by slot blot and Northern blot analysis using a gamma 32P-end-labelled 35 mer oligonucleotide probe of MCP-1. Meanwhile, MCP-1 protein in the conditioned media was examined by use of sandwich ELISA. It was found that monocytes from human peripheral blood can express MCP-1 mRNA and protein after 24 hours incubation at 37 degrees C and the expression of MCP-1 mRNA and protein was markedly increased by a 24 hour exposure to OX-LDL and OX-VLDL, whereas the expression of MCP-1 mRNA and protein was only sightly increased when exposed to LDL and VLDL. It is concluded that monocytes can express MCP-1 that induce additional monocyte migration into the subendothelial space, and that OX-LDL and OX-VLDL enhance this function by inducing stronger MCP-1 expression in monocytes.

Cells, Cultured↗
PubMed1996

[Protective effects of radix Salviae miltiorrhizae on azathioprine hepatotoxicity in rats].

The changes of liver function and malondialdehyde (MDA) and glutathione (GSH) were studied in rats intoxicated with azathioprine (Aza) 15mg/(kg.d) and in rats treated with Aza mixed Salviae 8g/(kg.d). The results showed that in the Aza group, the levels of ALT, AKP, MDA increased and GSH decreased significantly in week 1 and week 2. But in the Salviae group the levels of ALT, AKP, MDA decreased and GSH increased significantly, approaching the normal levels, It follows that Salviae has protective effects on Aza hepatotoxicity in rats.

Animals↗
PubMed1995

Phosphorylation of the nicotinic acetylcholine receptor by protein tyrosine kinases.

Most neurotransmitter receptors examined to date are either regulated by phosphorylation or contain consensus sequences for phosphorylation by protein kinases. The nicotinic acetylcholine receptor (AChR), which mediates depolarization at the neuromuscular junction, has served as a model for the study of the structure, function, and regulation of ligand-gated ion channels. The AChR is phosphorylated by protein kinase A, protein kinase C, and an unidentified protein tyrosine kinase. Tyrosine phosphorylation of the AChR is correlated with a modulation of the rate of receptor desensitization and is associated with AChR clustering. We showed that agrin, a neuronally derived extracellular matrix protein, induces AChR clustering and tyrosine phosphorylation. In addition, we identified two protein tyrosine kinases, Fyn and Fyk, that appear to be involved in the regulation of synaptic transmission at the neuromuscular junction by phosphorylating the AChR. The two kinases are highly expressed in Torpedo electric organ, a tissue enriched in synaptic components including the AChR. As demonstrated by coimmunoprecipitation, Fyn and Fyk associate with the AChR. Furthermore, the AChR is phosphorylated in Fyn and Fyk immunoprecipitates. We investigated the molecular basis for the association of the AChR with Fyn and Fyk using fusion proteins derived from the kinases. The AChR bound specifically to the SH2 domain fusion proteins of Fyn and Fyk. The association of the AChR with the SH2 domains is dependent on the state of AChR tyrosine phosphorylation and is mediated by the delta subunit of the receptor. These data provide evidence that the protein tyrosine kinases Fyn and Fyk may act to phosphorylate the AChR in vivo.

Agrin↗