Insulin-like growth factor binding protein production by bovine and human vascular smooth muscle cells: production of insulin-like growth factor binding protein-6 by human smooth muscle
Autor: | Brian L. Dake, David R. Moser, Mary Boes, Robert S. Bar, Barbara A. Booth |
---|---|
Rok vydání: | 1996 |
Předmět: |
Insulin-Like Growth Factor Binding Protein 6
medicine.medical_specialty Proteases Vascular smooth muscle Transcription Genetic medicine.medical_treatment Pulmonary Artery Biology Polymerase Chain Reaction Muscle Smooth Vascular Insulin-like growth factor-binding protein Endocrinology Species Specificity Internal medicine medicine Animals Humans RNA Messenger Aorta Cells Cultured Messenger RNA Growth factor Binding protein Proteolytic enzymes Arteries Coronary Vessels Insulin-Like Growth Factor Binding Proteins Molecular Weight biology.protein Cattle hormones hormone substitutes and hormone antagonists |
Zdroj: | Endocrinology. 137:5357-5363 |
ISSN: | 1945-7170 0013-7227 |
Popis: | Insulin-like growth factor binding protein (IGFBP) secretory profiles were determined for vascular smooth muscle cells (VSMC) derived from bovine aorta and human aorta, pulmonary artery, and coronary artery. The bovine cells produced IGFBP-4, IGFBP-3, and an IGFBP-3 protease. IGF-I stimulated messenger RNA (mRNA) and media levels of IGFBP-3. The human cells produced IGFBP-3, IGFBP-4, and IGFBP-3 and IGFBP-4 proteases. The three human cells also produced a 30K IGFBP, shown to be IGFBP-6, based on increased affinity for IGF-II vs. IGF-I, size decrease when treated with O-glycanase, but not N-glycanase, reactivity with IGFBP-6 antiserum, presence of a 1.3-kilobase pair mRNA that hybridized to IGFBP-6 specific complementary DNA, and N-terminal amino acid sequence corresponding to IGFBP-6. In the human cells, IGF-I increased media levels of IGFBP-3 through stimulation of IGFBP-3 mRNA and dissociation of cell bound IGFBP-3, and decreased IGFBP-4 via potentiation of IGFBP-4 proteolysis. Neither the bovine nor the human aorta VSMC produced sufficient IGFBP-2 or IGFBP-2 mRNA to be detected by ligand blot and Northern analysis, as previously reported for porcine and rat aorta smooth muscle cells. The variable expression of IGFBPs and IGFBP proteases by VSMC are likely to contribute to differential vascular reactivity to the IGFs in larger arterial blood vessels. |
Databáze: | OpenAIRE |
Externí odkaz: |