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Pathogen research abs 1 || Pathogen research abs 2 || Pathogen research abs 3 || Pathogen research abs 4 || Pathogen research abs 5 || Hormone and endocrine research abs 1 || Hormone and endocrine research abs 2 || Hormone and endocrine research abs 3 || Hormone and endocrine research abs 4 || Hormone and endocrine research abs 5

Scand J Immunol. 2002 Nov;56(5):504-11.
Transcriptional regulation of serum amyloid A1 gene expression in human aortic smooth muscle cells involves CCAAT/enhancer binding proteins (C/EBP) and is distinct from HepG2 cells.

Kumon Y, Suehiro T, Faulkes DJ, Hosakawa T, Ikeda Y, Woo P, Sipe JD, Hashimoto K.

Second Department of Internal Medicine, Kochi Medical School, Kohasu Okoh-Cho, Nankoku, Kochi, Japan. kumonochi-ms.ac.jp

Regulation of acute-phase serum amyloid A (A-SAA) synthesis by proinflammatory cytokines and steroid hormones in human aortic smooth muscle cells (HASMCs) is distinct from that in HepG2 cells. To study the cis- and trans-activating promoter element involved in the SAA1 gene expression by HASMCs and HepG2 cells, we constructed plasmid vectors for luciferase reporter gene assay with varying lengths of SAA1 upstream regulatory region (up to 1431 bp), and examined their response to proinflammatory cytokines and/or steroid hormones. The corresponding vectors with the SAA4 upstream regulatory region served as controls. The presence of proposed transcriptional regulatory factors binding to these regions was confirmed immunohistochemically. The sequences of 1478 and 1836 bp of the SAA1 and SAA4 5'-flanking regions were determined, respectively. SAA1 promoter transcription in cultured HASMCs was upregulated not by proinflammatory cytokines, but rather by glucocorticoids. This differed from HepG2 cells, in which SAA1 promoter transcription was upregulated synergistically by proinflammatory cytokines and glucocorticoids. The promoter activity of a series of truncated SAA1 promoter constructs measured using the reporter gene assay showed that the 5'-region from -252 to -175, containing a consensus site for CCAAT/enhancer binding proteins alpha,beta (C/EBPalpha,beta), was essential for SAA1 induction in HASMCs. In HepG2 cells, the 5'-region from -119 to -79, containing a nuclear factor kappa-B (NFkappaB) consensus sequence, was essential for the induction. The functional significance of the C/EBP site as indicated by the immunohistochemical result was that in HASMCs anti-C/EBPbeta reactivity was shifted from the cytoplasm to the nuclei. We have, therefore, demonstrated that the region containing the C/EBPalpha,beta consensus binding site between the bases -252 and -175 is important for the glucocorticoid-induced SAA1 gene expression in HASMCs but not in HepG2 cells.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12410800&dopt=Abstract

Plant J. 2002 Nov;32(3):263-76.
Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90.

Kamphausen T, Fanghanel J, Neumann D, Schulz B, Rahfeld JU.

Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, Germany.

The twisted dwarf1 (twd1) mutant from Arabidopsis thaliana was identified in a screen for plant architecture mutants. The TWD1 gene encodes a 42 kDa FK506-binding protein (AtFKBP42) that possesses similarity to multidomain PPIases such as mammalian FKBP51 and FKBP52, which are known to be components of mammalian steroid hormone receptor complexes. We report here for the first time the stoichiometry and dissociation constant of a protein complex from Arabidopsis that consists of AtHsp90 and AtFKBP42. Recombinant AtFKBP42 prevents aggregation of citrate synthase in almost equimolar concentrations, and can be cross-linked to calmodulin. In comparison to one active and one inactive FKBP domain in FKBP52, AtFKBP42 lacks the PPIase active FKBP domain. While FKBP52 is found in the cytosol and translocates to the nucleus, AtFKBP42 was predicted to be membrane-localized, as shown by electron microscopy.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12410806&dopt=Abstract

Plant J. 2002 Nov;32(3):285-98.
Expression of the Arabidopsis histone H2A-1 gene correlates with susceptibility to Agrobacterium transformation.

Yi H, Mysore KS, Gelvin SB.

Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA.

Transformation of plant cells by Agrobacterium tumefaciens involves both bacterial virulence proteins and host proteins. We have previously shown that the Arabidopsis thaliana gene H2A-1 (RAT5), which encodes histone H2A-1, is involved in T-DNA integration into the plant genome. Mutation of RAT5 results in a severely decreased frequency of transformation, whereas overexpression of RAT5 enhances the transformation frequency (Mysore et al., 2000b). We show here that the expression pattern of RAT5 correlates with plant root cells most susceptible to transformation. As opposed to a cyclin-GUS fusion gene whose expression is limited to meristematic tissues, the H2A-1 gene is expressed in many non-dividing cells. Under normal circumstances, the H2A-1 gene is expressed in the elongation zone of the root, the region that is most susceptible to Agrobacterium transformation. In addition, when roots are incubated on medium containing phytohormones, a concomitant shift in H2A-1 expression and transformation susceptibility to the root base is observed. Inoculation of root segments with a transfer-competent, but not a transformation-deficient Agrobacterium strain induces H2A-1 expression. Furthermore, pre-treatment of Arabidopsis root segments with phytohormones both induces H2A-1 expression and increases the frequency of Agrobacterium transformation. Our results suggest that the expression of the H2A-1 gene is both a marker for, and a predictor of, plant cells most susceptible to Agrobacterium transformation.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12410808&dopt=Abstract

Kidney Int. 2002 Dec;62 Suppl 82:36-41.
Angiotensin II type 1 receptor blockade to control blood pressure in postmenopausal women: Influence of hormone replacement therapy.

Fernandez-Vega F, Abellan J, Vegazo O, De Vinuesa SG, Rodriguez JC, Maceira B, De Castro SS, Nicolas RR, Luno J.

Department of Nephrology-I, Hospital Central de Asturias; Health Centre of San Andres, Murcia; Medical Department, AstraZeneca Farmaceutica Spain, S.A.; Department of Nephrology, Hospital Gregorio Maranon, Madrid; Department of Nephrology, Hospital Doctor Negrin, Las Palmas; Department of Nephrology, Hospital Universitario de Canarias, Tenerife; Department of Nephrology, Hospital Marques de Valdecilla, Santander; and Department of Nephrology, Hospital Infanta Cristina, Badajoz, Spain.

Angiotensin II type 1 receptor blockade to control blood pressure in postmenopausal women: Influence of hormone replacement. BACKGROUND: Hypertension is twice as common in postmenopausal than in premenopausal women. This study evaluated the effectiveness of a blockade of the renin-angiotensin-aldosterone system (RAAS) with candesartan cilexetil (CC) to control blood pressure (BP) in hypertensive menopausal women, and the influence of hormone replacement therapy (HRT). METHODS: This was designed as a prospective, open-label and non-comparative study. Included were 618 hypertensive menopausal women grade I/II according to the Sixth Report of the Joint National Committee (VI-JNC), with an average age 52 +/- 4.7 years (95% CI 52.3-53.0) and with a last menstrual period (LMP) at least one year before. BP was determined by measurement in four visits during six months of follow-up, according to the recommendations of the OMS/SIH. Optimal control of BP was considered as BP <140/90 mm Hg. RESULTS: A statistically significant decrease in systolic (SBP; 19.9 +/- 11.2) and diastolic (DBP; 11.5 +/- 7.3) blood pressure mm Hg values was observed (P < 0.01). The control of BP increased significantly over time to 61.2% (P < 0.01). In multivariate analysis, only age was associated with control of BP (beta = -0.062; P = 0.004). Of the women not controlled in the second visit, 12.5 mg of hydrochlorothiazide (HCTZ) were added to 31.5% (N = 122), with 80% more BP control achieved in visit 3 than in the non-supplement group (OR = 1.8; 95% CI 1.04-3.05; P < 0.03). One hundred and three (16.7%) patients were receiving HRT for 2.01 +/- 2.23 years (95% CI 1.55-2.46). HRT did not affect the control of BP. No severe adverse reactions were reported. CONCLUSIONS: Candesartan cilexetil significantly reduced SBP and DBP and increased control (61.2%) of BP in hypertensive menopausal women. Only age had an inverse association with control of BP. In this study, HRT did not affect the control of BP.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12410853&dopt=Abstract [PubMed - as supplied by publisher]

Plant Physiol. 1999 Apr;119(4):1209-16.
Chloroplast-targeted ERD1 protein declines but its mRNA increases during senescence in Arabidopsis.

Weaver LM, Froehlich JE, Amasino RM.

Department of Biochemistry, University of Wisconsin, 433 Babcock Drive, Madison, Wisconsin 53706, USA.

Arabidopsis ERD1 is a ClpC-like protein that sequence analysis suggests may interact with the chloroplast-localized ClpP protease to facilitate proteolysis. The mRNA encoded by the ERD1 gene has previously been shown to accumulate in response to senescence and to a variety of stresses and hormones. Here we show that the ERD1 protein, in contrast to the ERD1 mRNA, strongly declines in abundance with age, becoming undetectable in fully expanded leaves. Sequence analysis also suggests that ERD1 is chloroplast targeted, and we show in an in vitro system that the native protein is properly imported, processed, and present within the soluble fraction of the chloroplast, presumably the stroma. We show that ClpP protein, which is also present in the stroma, declines with age in parallel with ERD1. These results are consistent with the interaction of ERD1 and ClpP, but they suggest that it is unlikely that either plays a major role during senescence. Certain other chloroplast proteins decline with age coordinately with ERD1 and ClpP, suggesting that these declines are markers of an early age-mediated change that occurs within the chloroplast.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10198079&dopt=Abstract

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