A key role of PGC-1α
 transcriptional coactivator in production of VEGF by a novel angiogenic agent COA-Cl in cultured human fibroblasts

Abstract Skin fibroblasts were cultured from normal individuals, from patients with hemophilia, and from known and suspected carriers of hemophilia. All cell lysates studied had similar coagulant activity unaffected by incubation with a specific antibody to factor VIII and, therefore, presumably not factor VIII. Further investigation indicated that the coagulant had many properties indistinguishable from those associated with "tissue factor," including heat lability, sedimentation characteristics, and dependency on factor VII for expression of coagulant activity. The presence of tissue factor in skin fibroblasts is consistent with the wide distribution of this coagulant, and the ability to maintain this material in tissue culture provides an opportunity for further investigation of the role of tissue factor in normal and pathologic states.

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The role of cyclic-3′,5′-adenosine monophosphate in prostaglandin-mediated inhibition of basic calcium phosphate crystal-induced mitogenesis and collagenase induction in cultured human fibroblasts

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease ◽

10.1016/0925-4439(94)90064-7 ◽

1994 ◽

Vol 1226 (1) ◽

pp. 97-104 ◽

Cited By ~ 10

Author(s):

Geraldine M. McCarthy ◽

Herman S. Cheung

Keyword(s):

Calcium Phosphate ◽

Human Fibroblasts ◽

Adenosine Monophosphate ◽

Basic Calcium Phosphate ◽

Cultured Human Fibroblasts ◽

Calcium Phosphate Crystal ◽

Basic Calcium Phosphate Crystal

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Regulation of purine de novo synthesis in cultured human fibroblasts: The role of

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis ◽

10.1016/0005-2787(79)90135-7 ◽

1979 ◽

Vol 562 (1) ◽

pp. 162-176 ◽

Cited By ~ 19

Author(s):

Ross B. Gordon ◽

Lambert Thompson ◽

Lambro A. Johnson ◽

Bryan T. Emmerson

Keyword(s):

De Novo ◽

Human Fibroblasts ◽

De Novo Synthesis ◽

Cultured Human Fibroblasts

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Ceroid/lipofuscin formation in cultured human fibroblasts: the role of oxidative stress and lysosomal proteolysis

Mechanisms of Ageing and Development ◽

10.1016/s0047-6374(98)00073-6 ◽

1998 ◽

Vol 104 (3) ◽

pp. 277-291 ◽

Cited By ~ 85

Author(s):

Alexei Terman ◽

Ulf T. Brunk

Keyword(s):

Oxidative Stress ◽

Human Fibroblasts ◽

Cultured Human Fibroblasts ◽

Lysosomal Proteolysis ◽

Ceroid Lipofuscin

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Sumoylation of the major immediate-early IE2 protein of human cytomegalovirus Towne strain is not required for virus growth in cultured human fibroblasts

Journal of General Virology ◽

10.1099/vir.0.79954-0 ◽

2004 ◽

Vol 85 (8) ◽

pp. 2149-2154 ◽

Cited By ~ 17

Author(s):

Hye-Ra Lee ◽

Jin-Hyun Ahn

Keyword(s):

Human Cytomegalovirus ◽

Human Fibroblasts ◽

Artificial Chromosome ◽

Immediate Early ◽

Nuclear Antigen ◽

Virus Growth ◽

Cultured Human Fibroblasts ◽

Proliferating Cell ◽

Revertant Virus

Sumoylation of the major immediate-early IE2 protein of human cytomegalovirus has been shown to increase transactivation activity in target reporter gene assays. This study examined the role of IE2 sumoylation in viral infection. A Towne strain-based bacterial artificial chromosome clone was generated encoding a mutated form of the IE2 protein with Lys→Arg substitutions at positions 175 and 180, the two major sumoylation sites. When human fibroblast (HF) cells were infected with the reconstituted mutant virus, (i) viral growth kinetics, (ii) the accumulation of IE1 (UL123), IE2 (UL122), p52 (UL44) and pp65 (UL83) proteins and (iii) the relocalization of the cellular small ubiquitin-like modifier (SUMO)-1, p53 and proliferating cell nuclear antigen proteins into viral DNA replication compartments were comparable with those of the wild-type and the revertant virus. The data demonstrate that sumoylation of IE2 is not essential for virus growth in cultured HF cells.

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