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  • 1.
    Krettek, Alexandra
    et al.
    The Wallenberg Laboratory for Cardiovascular Research, Göteborg University, Sahlgrenska University Hospital, Göteborg, Sweden.
    Fager, G.
    The Wallenberg Laboratory for Cardiovascular Research, Göteborg University, Sweden.
    Jernberg, P.
    The Wallenberg Laboratory for Cardiovascular Research, Göteborg University, Sweden.
    Östergren-Lundén, G.
    The Wallenberg Laboratory for Cardiovascular Research, Göteborg University, Sweden.
    Lustig, F.
    The Wallenberg Laboratory for Cardiovascular Research, Göteborg University, Sweden.
    Quantitation of platelet-derived growth factor receptors in human arterial smooth muscle cells in vitro1997In: Arteriosclerosis, Thrombosis and Vascular Biology, ISSN 1079-5642, E-ISSN 1524-4636, Vol. 17, no 11, p. 2395-2404Article in journal (Refereed)
    Abstract [en]

    Platelet-derived growth factor (PDGF) is suggested to play an important role in the development of atherosclerosis as a migratory and mitogenic stimulus to arterial smooth muscle cells (ASMCs). Stimulated and unstimulated ASMCs were studied with respect to PDGF receptor (PDGF-R) mRNA and protein expression. Quantitative RT-PCR was developed for simultaneous evaluation of both PDGF-R alpha and -R beta mRNA expression and a quantitative ELISA for estimation of corresponding PDGF-R subunits. On the mRNA level, the overall PDGF-R beta expression was approximately 100 times lower than that of PDGF-R alpha. Furthermore, although PDGF-R alpha mRNA levels were high irrespective of hASMC phenotype, PDGF-R beta mRNA was influenced by serum stimulation with lower copy numbers in proliferating and confluent cells compared with quiescent cells. On the protein level, quiescent hASMCs expressed 10 times more PDGF-R beta than PDGF-R alpha. Serum stimulation decreased cell surface PDGF-Rs, with most prominent loss of PDGF-R alpha (ELISA and immunohistochemistry). Our results suggest a differential regulatory pattern for PDGF-R alpha and -R beta and are compatible with the usage of alternative promoters for regulation of -R alpha expression. Further, it seems that the number of available receptor subunits is not the only determinant of variations in cell stimulation with different PDGF isoforms.

  • 2.
    Krettek, Alexandra
    et al.
    Wellenberg Lab. for Cardiovasc. Res., Göteborg University, Sahlgrenska University Hospital, Göteborg, Sweden / Wallenberg Lab. for Cardiovasc. Res., Göteborg University, Sahlgrenska University Hospital, Göteborg, Sweden.
    Fager, G.
    Wellenberg Lab. for Cardiovasc. Res., Göteborg University, Sahlgrenska University Hospital, Göteborg, Sweden.
    Lindmark, H.
    Wellenberg Lab. for Cardiovasc. Res., Göteborg University, Sahlgrenska University Hospital, Göteborg, Sweden.
    Simonson, C.
    Wellenberg Lab. for Cardiovasc. Res., Göteborg University, Sahlgrenska University Hospital, Göteborg, Sweden.
    Lustig, F.
    Wellenberg Lab. for Cardiovasc. Res., Göteborg University, Sahlgrenska University Hospital, Göteborg, Sweden.
    Effect of phenotype on the transcription of the genes for platelet-derived growth factor (PDGF) isoforms in human smooth muscle cells, monocyte-derived macrophages, and endothelial cells in vitro1997In: Arteriosclerosis, Thrombosis and Vascular Biology, ISSN 1079-5642, E-ISSN 1524-4636, Vol. 17, no 11, p. 2897-2903Article in journal (Refereed)
    Abstract [en]

    Proliferation of arterial smooth muscle cells (ASMCs) contributes considerably to enlargement of the arterial wall during atherosclerosis. The platelet-derived growth factor (PDGF) is a well-known mitogen and chemoattractant for ASMCs. Quantitative reverse transcription-polymerase chain reaction showed that cells appearing in atherosclerotic lesions, such as ASMCs, endothelial cells, and monocytes/macrophages, expressed mRNAs for both PDGF A and B chains in vitro, with the highest expression in endothelial cells. On proliferation, ASMCs and endothelial cells upregulated PDGF A mRNA. Differentiation of macrophages increased the amount of both mRNAs. Thus, the regulation of PDGF A- and B-chain expression depends on cell types and phenotypic states of the cells, which have also been found in vivo in human atherosclerotic lesions. PDGF A can be produced as short and long isoforms. The latter binds with high affinity to glycosaminoglycans. Irrespective of phenotype, only the minor part of total PDGF A mRNA consisted of the long variant in ASMCs, while endothelial cells produced 40% of total PDGF A as the long form. The differentiation of macrophages increased the production of the long PDGF A mRNA from 10% to 40%. Thus, increasing numbers of stimulated cells in the atherosclerotic lesion may increase the transcription of PDGF isoforms, and particularly of the long PDGF A isoform. Together with increasing amounts of ASMC-derived proteoglycans in developing lesions, this may contribute to accumulation of PDGF in the arterial wall matrix, resulting in prolonged stimulation of ASMCs.

  • 3.
    Krettek, Alexandra
    et al.
    Brigham and Women's Hospital, Harvard Medical School, Boston, United States.
    Sukhova, Galina K.
    Brigham and Women's Hospital, Harvard Medical School, Boston, United States.
    Libby, Peter
    Brigham and Women's Hospital, Harvard Medical School, Boston, United States.
    Elastogenesis in human arterial disease: A role for macrophages in disordered elastin synthesis2003In: Arteriosclerosis, Thrombosis and Vascular Biology, ISSN 1079-5642, E-ISSN 1524-4636, Vol. 23, no 4, p. 582-587Article in journal (Refereed)
    Abstract [en]

    OBJECTIVE: Elastin, an extracellular matrix protein, constitutes about 30% of the dry weight of the arteries. Elastolysis induced by inflammatory processes is active in chronic arterial diseases. However, elastogenesis in arterial diseases has received little attention. In this work we hypothesized that disordered elastogenesis is active in matrix remodeling in atheroma and abdominal aortic aneurysm (AAA).

    METHODS AND RESULTS: Human AAA and atheroma have 4- to 6-fold more tropoelastin protein than nondiseased arteries. The smooth muscle cell-containing media and fibrous cap of atherosclerotic arteries contain ordered mature elastin, whereas macrophage (MPhi)-rich regions often have disorganized elastic fibers. Surprisingly, in addition to smooth muscle cells, MPhis in diseased arteries also produce the elastin precursor tropoelastin, as shown by double immunostaining, in situ hybridization, and reverse transcription-polymerase chain reaction for tropoelastin mRNA. Cultured monocyte-derived MPhis can express the elastin gene. AAA have 9-fold but atheroma only 1.6-fold lower levels of desmosine, a marker for mature cross-linked elastin, than normal arteries.

    CONCLUSIONS: This study demonstrates ongoing but often ineffective elastogenesis in arterial disease and establishes human macrophages as a novel source for this important matrix protein. These results have considerable import for understanding mechanisms of extracellular matrix remodeling in arterial diseases.

  • 4.
    Rydberg, Ellen Knutsen
    et al.
    Wallenberg Lab. for Cardiovasc. Res., Sahlgrenska University Hospital, Göteborg, Sweden.
    Krettek, Alexandra
    Wallenberg Lab. for Cardiovasc. Res., Sahlgrenska University Hospital, Göteborg, Sweden.
    Ullström, Christina
    Wallenberg Lab. for Cardiovasc. Res., Sahlgrenska University Hospital, Göteborg, Sweden.
    Ekström, Karin
    Wallenberg Lab. for Cardiovasc. Res., Sahlgrenska University Hospital, Göteborg, Sweden.
    Svensson, Per-Arne
    Res. Ctr. for Endocrinol./Metabolism, Sahlgrenska Univ. Hospital, Göteborg, Sweden.
    Carlsson, Lena M. S.
    Res. Ctr. for Endocrinol./Metabolism, Sahlgrenska Univ. Hospital, Göteborg, Sweden.
    Jönsson-Rylander, Ann-Cathrine
    Molecular Pharmacology and DMPK, AstraZeneca R and D, Mölndal, Sweden.
    Hansson, Göran I.
    Bioanalytical Chemistry, AstraZeneca R and D, Mölndal, Sweden.
    McPheat, William
    Molecular Pharmacology and DMPK, AstraZeneca R and D, Mölndal, Sweden.
    Wiklund, Olov
    Wallenberg Lab. for Cardiovasc. Res., Sahlgrenska University Hospital, Göteborg, Sweden.
    Ohlsson, Bertil G.
    Wallenberg Lab. for Cardiovasc. Res., Sahlgrenska University Hospital, Göteborg, Sweden.
    Hultén, Lillemor Mattsson
    Wallenberg Lab. for Cardiovasc. Res., Sahlgrenska University Hospital, Göteborg, Sweden.
    Hypoxia increases LDL oxidation and expression of 15-lipoxygenase-2 in human macrophages2004In: Arteriosclerosis, Thrombosis and Vascular Biology, ISSN 1079-5642, E-ISSN 1524-4636, Vol. 24, no 11, p. 2040-2045Article in journal (Refereed)
    Abstract [en]

    OBJECTIVE: Macrophage-mediated oxidation of low-density lipoprotein (LDL) by enzymes, such as the lipoxygenases, is considered of major importance for the formation of oxidized LDL during atherogenesis. Macrophages have been identified in hypoxic areas in atherosclerotic plaques.

    METHODS AND RESULTS: To investigate the role of hypoxia in macrophage-mediated LDL oxidation, we incubated human monocyte-derived macrophages with LDL under normoxic (21% O2) or hypoxic (0% O2) conditions. The results showed that hypoxic macrophages oxidized LDL to a significantly higher extent than normoxic cells. Interestingly, the mRNA and protein expression of 15-lipoxygenase-2 (15-LOX-2) as well as the activity of this enzyme are elevated in macrophages incubated at hypoxia. Both the unspliced 15-LOX-2 and the spliced variant 15-LOX-2sv-a are found in macrophages. In addition, 15-LOX-2 was identified in carotid plaques in some macrophage-rich areas but was only expressed at low levels in nondiseased arteries.

    CONCLUSIONS: In summary, these observations show for the first time that 15-LOX-2 is expressed in hypoxic macrophages and in atherosclerotic plaques and suggest that 15-LOX-2 may be one of the factors involved in macrophage-mediated LDL oxidation at hypoxia.

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