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Cancer Res. 2002 Nov 15;62(22):6639-44.
Methylthioadenosine phosphorylase, a gene frequently codeleted with p16(cdkN2a/ARF), acts as a tumor suppressor in a breast cancer cell line.
Christopher SA, Diegelman P, Porter CW, Kruger WD.
Fox Chase Cancer Center, Division of Population Science, Philadelphia, Pennsylvania 19111, USA.
The human methylthioadenosine phosphorylase (MTAP) gene is located on 9p21 and is frequently homozygously deleted, along with p16(cdkN2a/ARF), in a wide variety of human tumors and human tumor-derived cell lines. The function of MTAP is to salvage methylthioadenosine, which is produced as a byproduct of polyamine metabolism. We have reintroduced MTAP into MCF-7 breast adenocarcinoma cells and have examined its effect on the tumorigenic properties of these cells. MTAP expression does not affect the growth rate of cells in standard tissue culture conditions but severely inhibits their ability to form colonies in soft agar or collagen. In addition, MTAP-expressing cells are suppressed for tumor formation when implanted into SCID mice. This suppression of anchorage-independent growth appears to be because of the enzymatic activity of MTAP, as a protein with a missense mutation in the active site does not exhibit this phenotype. MTAP expression causes a significant decrease in intracellular polyamine levels and alters the ratio of putrescine to total polyamines. Consistent with this observation, the polyamine biosynthesis inhibitor alpha-difluoromethylornithine inhibits the ability of MTAP-deficient cells to form colonies in soft agar, whereas addition of the polyamine putrescine stimulates colony formation in MTAP-expressing cells. These results indicate that MTAP has tumor suppressor activity and suggest that its effects may be mediated by altering intracellular polyamine pools.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12438261&dopt=Abstract
Ann Rheum Dis. 2000 Dec;59(12):959-65.
Apoptosis in normal and osteoarthritic human articular cartilage.
Heraud F, Heraud A, Harmand MF.
INSERM U443, Victor Segalen University, Bordeaux, France.
OBJECTIVES: To investigate whether apoptosis occurs in osteoarthritis (OA), and if this phenomenon is modulated by human recombinant interleukin 1beta (hrIL1beta). METHODS: Human articular cartilage samples were obtained at the time of hip arthroplasty because of femoral neck fracture (normal cartilage) (n=4) or advanced coxarthrosis (OA cartilage) (n=14). Apoptotic chondrocytes, isolated by collagenase digestion and cultivated for 24 hours, or present in situ in frozen cartilage sections, were quantified by fluorescent microscopy using two apoptosis markers: the TUNEL reaction, which detects nuclear DNA fragmentation, and Annexin-V-fluos, which labels at the membrane level the externalisation of phosphatidylserine. RESULTS: In OA cartilage 18-21% of chondrocytes showed apoptotic features, compared with 2-5% in normal cartilage. The results were similar for the two comparative studies (in situ and in vitro) and for both apoptosis markers. Moreover, hrIL1beta increased the apoptosis rate in vitro in a dose dependent manner in OA and normal chondrocytes. CONCLUSION: These results suggest that apoptosis may be an important factor in the evolution of OA and may be a new target for treatment of OA.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11087699&dopt=Abstract
Ann Rheum Dis. 2000 Dec;59(12):982-4.
Procollagen IIC-peptide as a marker for assessing mechanical risk factors of knee osteoarthritis: effect of obesity and varus alignment.
Kobayashi T, Yoshihara Y, Yamada H, Fujikawa K.
Department of Orthopaedic Surgery, National Defence Medical College, 3-2, Namiki, Tokorozawa, Saitama, Japan. kyusee.ndmc.ac.jp
OBJECTIVE: To ascertain by cross sectional examination whether the concentration of procollagen IIC-peptide in joint fluid significantly correlates with mechanical risk factors of knee osteoarthritis (OA), such as obesity (body mass index) and varus alignment (lateral femorotibial angle). METHODS: The concentrations of procollagen IIC-propeptide in synovial fluid were measured by a sandwich enzyme immunoassay of 65 patients with the same radiological stage of primary knee OA-that is, Ahlbak stage I. The relations between procollagen IIC-peptide and body mass index and lateral femorotibial angle were examined using simple regression analysis and multiple regression analysis. RESULTS: Significant positive correlations were found between procollagen IIC-propeptide concentrations and body mass index (r=0.479, p<0.0001), and between procollagen IIC-propeptide concentrations and lateral femorotibial angle (r=0.375, p=0.0021). Significant correlations were also found by multiple regression analysis. The multiple correlation coefficient of body mass index and femorotibial lateral angle to the procollagen IIC-propeptide concentrations was 0.547 (p<0.0001). CONCLUSIONS: The findings suggest that synthesis of type II collagen by chondrocytes is enhanced by abnormal mechanical stress, in this case obesity and varus alignment. It is concluded that procollagen IIC-propeptide concentrations in joint fluid are a useful marker of early OA.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11087702&dopt=Abstract
Glycobiology. 2000 Nov;10(11):1201-8.
Molecular modeling and mutagenesis studies of the N-terminal domains of galectin-3: evidence for participation with the C-terminal carbohydrate recognition domain in oligosaccharide binding.
Barboni EA, Bawumia S, Henrick K, Hughes RC.
National Institute for Medical Research, Mill Hill, London NW7 1AA, UK.
A model structure (Henrick,K., Bawumia,S., Barboni,E.A.M., Mehul,B. and Hughes, R.C. (1998) Glycobiology:, 8, 45-57) of the carbohydrate recognition domain (CRD, amino acid residues 114-245) of hamster galectin-3 has been extended to include N-terminal domain amino acid residues 91-113 containing one of the nine proline-rich motifs present in full-length hamster galectin-3. The modeling predicts two configurations of the N-terminal tail: in one the tail turns toward the first (SI) and last (S12) beta-strands of the CRD and lies at the apolar dimer interface observed for galectins -1 and -2. In the second folding arrangement the N-terminal tail lies across the carbohydrate-binding pocket of the CRD where it could participate in sugar-binding: in particular tyrosine 102 and adjacent residues may interact with the partly solvent exposed nonreducing N-acetylgalactosamine and fucose substituents of the A-blood group structure GalNAcalpha1,3 [Fucalpha1,2]Galbeta1,4GlcNAc-R. Binding studies using surface plasmon resonance of a recombinant fragment Delta1-93 protein containing residues 94-245 of hamster galectin-3 and a collagenase-derived fragment Delta1-103 containing residues 104-245, as well as alanine mutagenesis of residues 101-105 in Delta1-93 protein, support the prediction that Tyr102 and adjacent residues make significant contributions to oligosaccharide binding.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11087712&dopt=Abstract
J Biol Chem. 2001 Feb 23;276(8):6046-55. Epub 2000 Nov 21.
Cartilage oligomeric matrix protein interacts with type IX collagen, and disruptions to these interactions identify a pathogenetic mechanism in a bone dysplasia family.
Holden P, Meadows RS, Chapman KL, Grant ME, Kadler KE, Briggs MD.
Wellcome Trust Centre for Cell-Matrix Research, School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road., Manchester M13 9PT, United Kingdom.
Cartilage oligomeric matrix protein (COMP) and type IX collagen are key structural components of the cartilage extracellular matrix and have important roles in tissue development and homeostasis. Mutations in the genes encoding these glycoproteins result in two related human bone dysplasias, pseudoachondroplasia and multiple epiphyseal dysplasia, which together comprise a "bone dysplasia family." It has been proposed that these diseases have a similar pathophysiology, which is highlighted by the fact that mutations in either the COMP or the type IX collagen genes produce multiple epiphyseal dysplasia, suggesting that their gene products interact. To investigate the interactions between COMP and type IX collagen, we have used rotary shadowing electron microscopy and real time biomolecular (BIAcore) analysis. Analysis of COMP-type IX collagen complexes demonstrated that COMP interacts with type IX collagen through the noncollagenous domains of type IX collagen and the C-terminal domain of COMP. Furthermore, peptide mapping identified a putative collagen-binding site that is associated with known human mutations. These data provide evidence that disruptions to COMP-type IX collagen interactions define a pathogenetic mechanism in a bone dysplasia family.
online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11087755&dopt=Abstract
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