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PubMed2001

Fine mapping of Ath6, a quantitative trait locus for atherosclerosis in mice.

Ath6 is a novel quantitative trait locus associated with differences in susceptibility to atherosclerosis between C57BL/6J (B6) and C57BLKS/J (BKS) inbred mouse strains. Combining data from an intercross and a backcross (1593 meioses) between mice from B6 and BKS strains and from The Jackson Laboratory interspecific backcross panels, (C57BL/6J x Mus spretus) F1 x C57BL/6J and (C57BL/6J x SPRET/Ei) F1 x SPRET/Ei, we constructed a consensus genetic map and narrowed Ath6 to a 1.07 +/- 0.26 cM interval between the anonymous DNA marker D12Pgn4 and the gene Nmyc1. This region is near the proximal end of murine Chromosome (Chr) 12, which is homologous to the human chromosomal region 2p24-p25. Marker order in the Ath6 region was concordant among the two crosses and The Jackson Laboratory interspecific backcross panels. This high resolution map rules out candidate genes encoding apolipoprotein B, syndecan 1, and Adam17. The two Ath6 crosses have a combined potential resolution of 0.06 cM.

Alleles↗

PubMed1999

Linkage mapping of rat chromosome 5 markers generated from chromosome-specific libraries.

Seventy-six novel microsatellite markers with various simple sequence repeat (SSR) motifs are reported in this paper. They were generated on the basis of non-radioactive library screening procedures from flow-sorted rat Chromosome (Chr) 5-specific DNA, and were mapped in three rat backcross populations. Fifty-four of these markers mapped to Chr 5, while the other 22 mapped to other chromosomes of the rat genome. The marker D3Uwm8 is a new microsatellite marker for the rat syndecan 4 (ryudocan) gene. A genotyping protocol based on agarose gel electrophoresis is also provided in this paper.

Animals↗

PubMed2006

Effect of hyperglycemic condition on proteoglycan secretion in cultured human endothelial cells.

BACKGROUND: Proteoglycans (PGs) are important constituents of the plasma membrane and of the basement membrane supporting the endothelial cell layer. Changes in the amounts or the structures of PGs in the endothelium may affect important functions such as turnover of lipoproteins, filtration properties, and regulation of chemokines during inflammation, which are all relevant in diabetes. AIM OF THE STUDY: The purpose of this study was to investigate if hyperglycemic conditions would affect the biosynthesis and secretion of PGs in cultured primary human endothelial cells. METHODS: Primary human umbilical cord vein endothelial cells were established and cultured in vitro. The cells were cultured either in medium with low glucose (LG) (1 g/l) or high glucose (HG) (4.5 g/l). From day 3-4 cells were labeled with (35)S-sulfate for 24 h. (35)S-Labeled macromolecules (medium) were purified by gel chromatography, and isolated macromolecules were analyzed by gel chromatography after different types of treatment, electrophoresis, and immunoprecipitation. RESULTS: Lower levels of secreted PGs were found in human endothelial cells exposed to HG. The major part of the PGs released was of the heparan sulfate (HS) type, and immunoprecipitation experiments showed that one such PG was syndecan-1. However, there was no difference in the ratio between HS and chondroitin sulfate (CS) under the different experimental conditions. Further, the PGs expressed neither differ with regard to molecular size of the glycosaminoglycan (GAG) chains, nor were their polyanionic properties affected by the different experimental conditions. CONCLUSION: The results obtained suggest that treatment of primary human endothelial cells with hyperglycemia leads to a decrease in PG secretion in primary cultures of human endothelial cells.

Basement Membrane↗

PubMed2002

Differential expression of glycosaminoglycans and proteoglycans in the migratory pathway of the primordial germ cells of the mouse.

Primordial germ cells are an embryonic cell line that give rise to gametes in vertebrates. They originate outside the embryo proper and migrate by a well-defined route to the genital ridges. Proteoglycans and glycosaminoglycans have distinctive properties that affect many of the characteristics of the extracellular microenvironment of migratory pathways in a variety of developmental systems. The purpose of this work was to identify the proteoglycans and glycosaminoglycans that are spatially and temporally expressed in the migratory pathway of primordial germ cells. We showed that the expression of proteoglycans and glycosaminoglycans in the primordial germ cells migratory pathway changes according to the different phases of the migratory process. Some molecules such as chondroitin-0-sulfate, decorin, and biglycan are present only in certain phases of the migratory process of primordial germ cells. Heparan sulfate, chondroitin-6-sulfate, versican, perlecan, and syndecan-4, although exhibiting some variation in expression were detected during all phases of the migratory process. Our results indicate that the successive steps of primordial germ cell migration require a coordinated expression of proteoglycans and glycosaminoglycans, that should be present in appropriate levels and in specific areas of the embryo, and that the sequential expression of these extracellular matrix molecules is under a genetic program that appears to be common to a variety of cell types during embryonic development.

Animals↗

PubMed2002

Anaplastic plasmacytoma with malignant pleural effusion lacking evidence of monoclonal gammopathy.

A case of plasmacytoma of the pleural cavity is reported with massive malignant pleural effusion, which, most unusually, lacked monoclonal gammopathy, thereby making it difficult to distinguish from lymphoma. The pleural tumor and pleural effusion contained large mononuclear lymphoma-like cells with distinct nucleoli. Immunohistochemistry revealed neither lymphoma markers nor clonal cytoplasmic nor cell surface immunoglobulins. Tumor cells were stained with vimentin and the plasma cell markers, VS38c, CD138 (syndecan-1), and MUM1 antibodies. Bone marrow contained small amounts of tumor consisting of similar cells. Electron microscopy showed well developed rough endoplasmic reticulum and peripherally positioned nuclei with euchromatin. Flow cytometry of bone marrow revealed a minimal involvement of CD38-positive cells. Chromosomal analysis of marrow cells revealed a complex abnormal karyotype. A polymerase chain reaction demonstrated clonal re-arrangement of the immunoglobulin heavy-chain gene. The overall results indicate a clonal expansion of tumor cells with primitive plasma cell differentiation with the highly unusual feature of absent monotypic immunoglobulin. The study illustrates the need for a comprehensive array of techniques to distinguish such rare non-synthesizing and non-secretory plasmacytomas from lymphoma.

Aged↗

PubMed2002

Cell adhesion receptors - signaling capacity and exploitation by bacterial pathogens.

Cell adhesion receptors play an essential role in multicellular organisms by mediating the direct association of cells with each other and with proteins of the extracellular matrix. Members of different protein families such as integrins, cadherins, immunoglobulin superfamily cell adhesion molecules (IgCAMs), selectins, and syndecans not only support the structural integrity of cells and tissues, but also contribute to the transduction of signals. Interestingly, several of these molecules are exploited by bacterial pathogens to establish tight contact with eukaryotic cells. Using the example of integrins, cadherins, and IgCAMs, this review illustrates the signaling capacity of cell adhesion receptors and highlights a number of bacterial adhesins that are known to engage these receptors. Where applicable, the role of the receptor-adhesin interaction in the course of the infection is discussed.

Adhesins, Bacterial↗

PubMed2004

Expression of laminin and fibronectin in renal dysplasia.

The pathogenesis of renal dysplasia is a matter of debate. Recent theories have conceptualized the role of extracellular matrix proteins in the genesis of renal dysplasia. During normal nephrogenesis, collagen type I and III and fibronectins are lost and laminin and syndecan appear once proper induction has occurred. Any deviation from the normal pattern is said to lead to dysplasia. In this study, the expressions of adhesive glycoproteins, laminin, and fibronectin were studied immunohistochemically in 25 autopsy cases of renal dysplasia and normal age-matched control cases. These cases of renal dysplasia were categorized into 3 groups based on the period of gestation: 20 to 26 weeks, 27 to 33 weeks, and 34 to 40 weeks. The immunohistochemical findings were graded from 0 to 4+ based on the visual intensity. Chi-square analysis was used to calculate the difference in expressions of laminin and fibronectin in cases and controls as a whole and within and between age groups. Immunostaining for laminin in all age groups showed a significant difference in expression between dysplastic kidneys (less expression) and normal controls (greater expression). In the case of fibronectin expression, all but 1 group showed a significant difference, with dysplastic kidneys showing more and normal controls showing less expression. The inference derived is that laminin expression decreases and fibronectin expression increases in renal dysplasia compared with normal nephrogenesis.

Female↗

PubMed1999

Lipid mediators that modulate the extracellular matrix structure and function in vascular cells.

Treatment with moderate levels of albumin-bound, nonesterified fatty acids (NEFA) induce important alterations of the structure and functionality of proteoglycans secreted by endothelial cells and arterial smooth muscle cells. In endothelial cell monolayers, the reduction on relative amount and sulfation of heparan sulfate proteoglycans is associated with an increased permeability to albumin. In smooth muscle cells, NEFA-albumin complex increased the expression of the genes for the core proteins of the proteoglycans syndecan, decorin and perlecan. This effect appears mediated by peroxisome proliferator-activated receptor gamma (PPARg). The matrix produced by the cells treated with NEFA-albumin had a higher affinity with low-density lipoproteins (LDLs). We speculate about the possibility that under dyslipidemias associated with increased exposure of vascular cells to NEFA, like in type 2 diabetes, similar alterations may contribute to associated macrovascular and microvascular complications.

Animals↗

PubMed1994

Blimp-1, a novel zinc finger-containing protein that can drive the maturation of B lymphocytes into immunoglobulin-secreting cells.

We describe a novel gene, Blimp-1 (for B lymphocyte-induced maturation protein), transcripts of which are rapidly induced during the differentiation of B lymphocytes into immunoglobulin secretory cells and whose expression is characteristic of late B and plasma cell lines. The 856 amino acid open reading frame contains five Krüppel-type zinc finger motifs and proline-rich and acidic regions similar to those of known transcription factors. Serological studies show an approximately 100 kd protein that localizes to the nucleus. Stable or transient transfection of Blimp-1 into B cell lymphoma lines leads to the expression of many of the phenotypic changes associated with B cell differentiation into an early plasma cell stage, including induction of J chain message and immunoglobulin secretion, up-regulation of Syndecan-1, and increased cell size and granularity. Thus, Blimp-1 appears to be a pleiotropic regulatory factor capable of at least partially driving the terminal differentiation of B cells.

Amino Acid Sequence↗

PubMed2006

Protein kinase Calpha can undergo membrane localization via an alternative phosphatidylinositol 4,5-bisphosphate-dependent pathway.

Protein kinase Calpha (PKCalpha) activation is known to be dependent on the metabolic product of phosphatidylinositol 4,5-bisphosphate (PIP2) by phospholipase C (PLC). Here we report that fibroblasts may have an additional PIP2-dependent mechanism for membrane localization of PKCalpha. We observed PKCalpha membrane localization in both wild type and PLCgamma1 -/- mouse embryonic fibroblasts. Treatment of cells with a specific PLC inhibitor U73122 resulted in increased PIP2 levels and enhanced membrane localization of PKCalpha. PKCalpha levels in the membrane fraction decreased following incubation with PLCgamma, but increased following treatment with U73122 or addition of exogenous PIP2 in vitro. In addition, PKCalpha interacted with PIP2-conjugate bead and mixed micelles containing PIP2. Finally, we found that PIP2 is involved in syndecan-4-mediated membrane localization of PKCalpha. Taken together, these data suggest that PIP2 might contribute to directly regulating the membrane localization of PKCalpha.

Animals↗

PubMed2004

Phenytoin treatment reduces atherosclerosis in mice through mechanisms independent of plasma HDL-cholesterol concentration.

Phenytoin (PHT) increases high density lipoprotein cholesterol (HDL-C) and reduces coronary artery disease mortality in humans. We report the results of PHT treatment on atherosclerosis susceptibility and lipid profile in four different types of mouse: control C57BL/6 mice and cholesteryl ester transfer protein transgenic mice as models of fatty streak, and LDL receptor-deficient mice and apolipoprotein E-deficient mice as models of mature atherosclerosis. Each mouse type was fed an appropriate diet to induce atherosclerosis and prevent liver toxicity. PHT treatment demonstrated a protective effect in all models. Reduction in aortic atherosclerotic area by PHT treatment was more evident in early atherosclerosis (2.3-fold) than in mature atherosclerosis (decreases of 40 and 23%, respectively, but only in mice in the upper 50% percentile of plasma PHT concentration). Atherosclerosis prevention was not concomitant with a consistent increase in HDL-C or any other protective change in the lipid profile. Different analyses of potential antiatherogenic HDL functions did not provide additional information. Microarray liver gene expression analyses identified a potential atheroprotective mechanism characterized by decreased expression of syndecan-4, RhoA2, double LIM protein-1, zeta-chain-associated protein kinase-70 and interleukin 6 receptor-alpha. However, to demonstrate that these changes are part of a PHT-antiatherogenic effect, they will need to be found also in arteries, maintained at protein level and proved to be causal rather than reactive.

Analysis of Variance↗

PubMed2004

Induction of synthesis of a large heparan sulfate proteoglycan, perlecan, by thrombin in cultured human coronary smooth muscle cells.

The accumulation of extracellular matrix components such as proteoglycans is a hallmark of an atherosclerotic lesion. A large heparan sulfate proteoglycan, perlecan, dramatically increases in the advanced lesion, and vascular smooth muscle cells are the cell type responsible for the accumulation. In this study, we investigated the effects of thrombin on the proteoglycan synthesis in cultured human coronary smooth muscle cells to determine the interrelationship between the accumulation of proteoglycans and the procoagulant state of blood in atherosclerosis. The cells were metabolically labeled with [(35)S]sulfate or (35)S-labeled amino acids in the presence of thrombin, and the labeled proteoglycans were characterized by Sepharose CL-4B molecular sieve chromatography and DEAE-Sephacel ion-exchange chromatography. The glycosaminoglycan M(r) and composition were analyzed by Sepharose CL-6B chromatography, and the core protein M(r) was determined by SDS-polyacrylamide gel electrophoresis before and after digestion with chondroitinase ABC or papain. The results indicate that thrombin increases the cell layer-associated heparan sulfate proteoglycan with a core protein size of approximately 400 kDa without any change in the length of the glycosaminoglycan chains when the cell density is high. The heparan sulfate proteoglycan was identified as perlecan by Western blot analysis. In addition, quantitative reverse transcription-polymerase chain reaction showed that thrombin elevated the steady-state level of perlecan mRNA but not that of versican, decorin, and syndecan-1 mRNAs, although that of biglycan mRNA was moderately elevated. Furthermore, the percentage of disaccharide units that compose perlecan heparan sulfate chains remained unaffected by thrombin. Therefore, it is suggested that thrombin induces the perlecan core protein synthesis without influencing the formation of the heparan sulfate chains in human coronary smooth muscle cells at a high cell density. The regulation of proteoglycan synthesis by thrombin may be involved in the accumulation of perlecan in advanced lesions of atherosclerosis.

Arteriosclerosis↗

PubMed2004

Catabolism of heparan sulfate proteoglycans in Drosophila cell lines.

We have studied intracellular catabolism of heparan sulfate proteoglycans (HSPGs) in Drosophila cell lines, Kc and S2, by a series of pulse-chase experiments using [(35)S]sulfate as a precursor in metabolic labeling experiments. HSPGs in culture medium and cell layer were separately purified by serial chromatographic procedures using Q-Sepharose and Superose 6 for characterization. Analysis of intact HSPG on Superose 6 chromatography revealed that Kc and S2 cells synthesize one major molecular species with slightly differing in sizes (estimated to be 54kDa in Kc and 78kDa in S2 cells). Analysis of glycosaminoglycans for (35)S-labeled macromolecules showed that the majority of (35)S-labeled macromolecules in Kc and S2 cells are HSPGs ( approximately 60% and approximately 80%, respectively). Results from continuous labeling and 2h pulse labeling-chase experiments revealed that, in both cell lines, the intact HSPGs were degraded in multiple phases; the degradation of HSPG was rapid in the early phase (with half-lives of approximately 6h in Kc and approximately 3h in S2 cells) and slow in the later phase (with half-lives >80h in both Kc and S2 cells). The rapid degradation appeared similar to that observed for glycosylphosphatidylinositol-anchored HSPGs (glypicans) in mammalian cell cultures. While the slow degradation appeared similar to that observed for transmembrane HSPGs (syndecans) in mammalian cell cultures. These experiments suggested that vertebrates and invertebrates shared common mechanisms for intracellular HSPG catabolism.

Animals↗

PubMed2004

Connective tissues: signalling by tenascins.

Different connective tissue cells secrete different types of tenascins. These glycoproteins contribute to extracellular matrix (ECM) structure and influence the physiology of the cells in contact with the tenascin containing environment. Tenascin-C expression is regulated by mechanical stress. It shows highest expression in connective tissue surrounding tumors, in wounds and in inflamed tissues where it may regulate cell morphology, growth, and migration by activating diverse intracellular signalling pathways. Thus, integrin and syndecan signalling is influenced by tenascin-C and the levels and/or activies of several proteins involved in intracellular signalling pathways are regulated by its presence. Tenascin-X is important for the proper deposition of collagen fibers in dermis and patients with a tenascin-X deficiency suffer from Ehlers Danlos syndrome. Tenascin-R (and -C) is prominent in the nervous system and has an impact on neurite outgrowth and synaptic functions, and tenascin-W is found in the extracellular matrix of bone, muscle, and kidney. Cell facts:bone: osteoblasts produce tenascin-C, -W cartilage: perichondrial cells produce tenascin-C tendon: fibroblasts produce tenascin-C smooth muscle cells produce tenascin-W, -C skeletal muscle: endo-, peri-, and epimysial fibroblasts produce tenascin-X dermal fibroblasts produce tenascin-X tumors: stromal fibroblasts produce tenascin-C wounds: fibroblasts produce tenascin-C nervous system: glial cells produce tenascin-R, -C, -X.

Cell Shape↗

PubMed2004

Heparan sulfate proteoglycans and heparanase--partners in osteolytic tumor growth and metastasis.

This review summarizes a series of studies demonstrating that heparan sulfate proteoglycans act to promote the growth and metastasis of myeloma and breast tumors, two tumors that home to, and grow within, bone. Much of the growth-promoting effect of proteoglycans in these tumors may reside in the shed form of syndecan-1 that acts to favorably condition the tumor microenvironment. Moreover, the interplay between heparan sulfate and the extracellular enzyme heparanase-1 also has important regulatory implications. Recent studies indicate that the activity of heparanase, which likely releases heparin sulfate-bound growth factors and generates highly active heparan sulfate fragments, also promotes growth and metastasis of myeloma and breast tumors. Understanding the role of heparan sulfate and heparanase in the regulation of tumor behavior may lead to new therapeutic approaches for treating cancer.

Animals↗

PubMed2004

mda-9/syntenin: recent insights into a novel cell signaling and metastasis-associated gene.

PDZ (an acronym representing three proteins--postsynaptic density protein PSD95/SAP90, drosophila tumor suppressor DLGA, and tight junction protein ZO-1) domain containing proteins are adapter proteins that play indispensable roles in regulating cell growth, development, and differentiation, predominantly through their capacity to serve as central organizers of protein complexes at the plasma membrane. A recently identified member of this protein family is melanoma differentiation associated gene-9 (mda-9), also known as syntenin, which was first identified as a gene down-regulated during human melanoma differentiation as mda-9 and subsequently recognized as an interacting partner of the cell-surface heparan sulfate syndecans, syntenin. Interest in mda-9/syntenin is intensifying because of its involvement in organization of protein complexes in the plasma membranes, regulation of B cell development, intracellular trafficking and cell surface targeting, cancer metastasis, synaptic transmission, and axonal outgrowth. In this review, we discuss the identification, structure and function of mda-9/syntenin and delineate future studies to address its role in regulating key physiological and pathological processes.

Amino Acid Sequence↗

PubMedDate not supplied

The endothelium and early immune activation: new perspective and interactions.

Far from being just a membrane for the passive transport of cells, molecules, and water between blood vessels and their interstitium or a passive target for humoral immunological reactions, the endothelium is now being viewed as an active modulator of both normal physiological homeostasis and the early inflammatory response. The repertoire of receptors and mediators produced by endothelial cells overlap those traditionally assigned to the immune system. This new paradigm together with the changes caused by brain death in the cadaver donor have far-reaching repercussions on how rejection is conceived, while opening new venues for its prevention. The respective theoretical roles of the neuro-endocrine-immunological axis and of syndecans are highlighted.

Angiogenesis Inducing Agents↗

PubMed2005

Plasmacytoid transitional cell carcinoma of the urinary bladder.

A case of rare plasmacytoid transitional cell carcinoma of the urinary bladder in a 60-year old man is described. The presence of end-stage disease did not allow for any efficacious therapy. Immunohistochemistry showed the tumor cells to be reactive for epithelial markers and syndecan-1 (CD138).

Carcinoma, Transitional Cell↗