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  • Aldosterone increases Na+ -K+ -ATPase activity in skeletal muscle of patients with Conn\'s syndrome. 21044117

    OBJECTIVE: In Conn\'s syndrome, hypokalaemia normally results from renal potassium loss because of the effect of excess aldosterone on Na(+) -K(+) -ATPase in principal cells. Little is known about the effect of aldosterone on cellular potassium redistribution in skeletal muscle. Our study determined the effect of aldosterone on muscle Na(+) -K(+) -ATPase.DESIGN: Muscle biopsies were taken from six patients immediately before and 1 month after adrenalectomy. Ten age-matched subjects with normal levels of circulating aldosterone served as controls.RESULTS:   Average plasma aldosterone was significantly higher in presurgery (235·0 ± 51·1 pg/ml) than postsurgery (64·5 ± 25·1 pg/ml) patients. Similarly, Na(+) -K(+) -ATPase activity, relative mRNA expression of α(2) (not α(1) or α(3) ) and β(1) (not β(2) or β(3) ), and protein abundance of α(2) and β(1) subunits were greater in pre- than postsurgery samples (128·7 ± 12·3 vs 79·4 ± 13·3 nmol·mg/protein/h, 2·45 ± 0·31 vs 1·04 ± 0·17, 1·92 ± 0·22 vs1·02 ± 0·14, 2·17 ± 0·33 vs 0·98 ± 0·09 and 1·70 ± 0·17 vs 0·90 ± 0·17, respectively, all P<0·05). The activity and mRNA expression of the α(2) and β(1) subunits correlated well with plasma aldosterone levels (r = 0·71, r = 0·75 and r = 0·78, respectively, all P < 0·01).CONCLUSIONS:   Our study provides the first evidence in human skeletal muscle that increased plasma aldosterone leads to increased Na(+) -K(+) -ATPase activity via increases in α(2) and β(1) subunit mRNAs and their protein expressions. The increased activity may contribute in part to the induction of hypokalaemia in patients with Conn\'s syndrome.© 2011 Blackwell Publishing Ltd.
    Document Type:
    Reference
    Product Catalog Number:
    AB9094

  • Intravascular injections of a conditional replicative adenovirus (adl118) prevent metastatic disease in human breast carcinoma xenografts. 11895001

    We describe a study showing that the adenovirus adl118, lacking both E1B proteins, very efficiently kills human malignant cells 'in vitro' and 'in vivo'. Since many breast cancer patients do not have metastasis at the time of diagnosis, but finally develop it, we planned to study whether intravascular injections of adl118 could prevent metastatic development. We studied the effects of this mutant adenovirus in an orthotopic model of human breast carcinoma xenografts with the breast MB435-lung 2 cell line, which is highly metastatic in the lungs. In this study, all primary tumors were excised when they reached 50-100 mm3 volume in the animals. After surgery, 10(10) p.f.u. of adl118 was intravenously injected into a random group of animals, either three times during the first week only, or once every week. At death, almost all the control animals showed numerous lung metastases of large size, which were present in only 15-40% of the treated animals, depending on the size of the primary tumor at the time of excision. Overall survival was 50-70 days in control mice, and over 120 days in mice injected with adl118. Concomitant treatment with adl118 and cisplatin did not enhance the antitumor effects of adl118. With these results, we conclude that intravenous injection of conditional replicative adenovirus, after excision of the primary tumor, induces a clear decrease in the metastatic disease, and could be a new strategy in preventing tumor metastasis of breast carcinomas.
    Document Type:
    Reference
    Product Catalog Number:
    MAB805
    Product Catalog Name:
    Anti-Adenovirus (Blend) Coating Antibody, clone 2/6, and 20/11

  • Augmented lipopolysaccharide-induced TNF-alpha production by peritoneal macrophages in type 2 diabetic mice is dependent on elevated glucose and requires p38 MAPK. 17202326

    Dysregulated inflammation is a complication of type 2 diabetes (T2D). In this study, we show that augmented LPS-induced TNF-alpha production by resident peritoneal macrophages (PerMphi) in type 2 diabetic (db/db) mice is dependent on elevated glucose and requires p38 MAPK. Intraperitoneal LPS administered to db/db and nondiabetic (db/+) mice induced 3- and 4-fold more TNF-alpha in the peritoneum and serum, respectively, of db/db mice as compared with db/+ mice. Examination of the TLR-4/MD2 complex and CD14 expression showed no difference between db/db and db/+ PerMphi. Ex vivo stimulation of PerMphi with LPS produced a similar 3-fold increase in TNF-alpha production in db/db PerMphi when compared with db/+ PerMphi. PerMphi isolated from db/+ mice incubated in high glucose (4 g/L) medium for 12 h produced nearly 2-fold more TNF-alpha in response to LPS than PerMphi incubated in normal glucose medium (1 g/L). LPS-dependent stimulation of PI3K activity, ERK1/2 activation, and p38 kinase activity was greater in PerMphi from db/db mice as compared with db/+ mice. Only inhibition of p38 kinase blocked LPS-induced TNF-alpha production in PerMphi from db/db mice. Taken together, these data indicate that augmented TNF-alpha production induced by LPS in macrophages during diabetes is due to hyperglycemia and increased LPS-dependent activation of p38 kinase.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple

  • The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. 1322798

    A cDNA clone encoding a novel, widely expressed protein (called growth factor receptor-bound protein 2 or GRB2) containing one src homology 2 (SH2) domain and two SH3 domains was isolated. Immunoblotting experiments indicate that GRB2 associates with tyrosine-phosphorylated epidermal growth factor receptors (EGFRs) and platelet-derived growth factor receptors (PDGFRs) via its SH2 domain. Interestingly, GRB2 exhibits striking structural and functional homology to the C. elegans protein sem-5. It has been shown that sem-5 and two other genes called let-23 (EGFR like) and let-60 (ras like) lie along the same signal transduction pathway controlling C. elegans vulval induction. To examine whether GRB2 is also a component of ras signaling in mammalian cells, microinjection studies were performed. While injection of GRB2 or H-ras proteins alone into quiescent rat fibroblasts did not have mitogenic effect, microinjection of GRB2 together with H-ras protein stimulated DNA synthesis. These results suggest that GRB2/sem-5 plays a crucial role in a highly conserved mechanism for growth factor control of ras signaling.
    Document Type:
    Reference
    Product Catalog Number:
    Multiple
    Product Catalog Name:
    Multiple

  • Broadly expressed SNT-like proteins link FGF receptor stimulation to activators of Ras. 8761293

    SNT was originally described as a approximately 90 kilodalton protein in neuronal precursor cells which bears affinity for the yeast cell cycle protein p13sucl and which undergoes rapid tyrosine phosphorylation following stimulation with growth factors which trigger terminal differentiation, but not by other growth factors which promote proliferation (Rabin et al., 1993). We show here that similarly sized SNT-like proteins (SLPs) are expressed in fibroblast, myoblast, and lymphoid cell lines, and undergo robust tyrosine phosphorylation in response to several mitogenic ligands, including fibroblast growth factors (FGFs). SLPs are tyrosine phosphorylated within 15 s of FGF stimulation, are predominantly membrane-associated, and are weakly associated with activated FGF receptor-1, suggesting that these proteins may be direct targets of the receptor kinase. Kinetic analysis of SLP phosphorylation and studies with serine/threonine kinase and phosphatase inhibitors suggest that SLPs are no larger than 70 000 kilodaltons, and that serine/threonine phosphorylation follows tyrosine phosphorylation to substantially retard gel electrophoretic mobility. SLPs are associated with the Grb-2 adaptor and are the major tyrosine phosphorylated proteins associated with the Ras guanine nucleotide exchange factor Sos in FGF-stimulated fibroblasts, suggesting that SLP-Grb2-Sos complexes modulate the activity of Ras proteins.
    Document Type:
    Reference
    Product Catalog Number:
    14-122

  • Endothelial cell apoptosis in capillary network remodeling. 9989782

    We hypothesized that the regulation of apoptosis is an important determinant of capillary network structure. Using human umbilical vein endothelial cells (HUVEC) in in vitro model systems of capillary tube formation, we initially documented that apoptosis is a prominent feature of network formation. Perturbations of integrin-matrix signaling by the administration of either colchicine or an anti-alpha(v)beta3 antibody resulted in the dissolution of the tubular network in association with increased apoptosis. The activation of the alpha(v)beta3 integrin induced increased expression of the anti-apoptotic gene bcl-2 and conferred resistance to the proapoptotic effect of TGF-beta1. In contrast to the stable networks formed by HUVEC, bovine aortic endothelial cells (BAEC) exhibited a more dynamic process of network formation and spontaneous involution. The inhibition of BAEC apoptosis by stable transfection of bcl-2 prevented the involution of the network. We hypothesized that TGF-beta1 present within the model system mediated network involution by inducing BAEC death. Indeed, blockade of TGF-beta1 with neutralizing antibodies reduced BAEC apoptosis and preserved the network structure. As observed with HUVEC networks, stable BAEC networks formed during blockade of TGF-beta1 were also dependent on the survival-promoting effects of matrixintegrin interactions. This study suggests that capillary network structure is determined by the balance of proapoptotic vs. anti-apoptotic signals mediated by the engagement of cytokine and integrin receptors within the milieu.
    Document Type:
    Reference
    Product Catalog Number:
    MAB1961
    Product Catalog Name:
    Anti-Integrin αVβ5 Antibody, clone P1F6