By M. A. Lehrman, H. H. Hobbs, M. S. Brown, J. L. Goldstein, D. W. Russell (auth.), Professor Dr. Dres. h. c. Gotthard Schettler (eds.)
The impressive contributions to this quantity are designed to make clear a few fields of cellphone biology and mobile pathology, together with newly saw phenomena of cell-cell interactions, that can be acceptable in learning the pathological means of atherosclerosis. the themes integrated hide: lipoproteins and lipoprotein receptors; development components; endocytosis and exocytosis; ONC Genes and proliferative affliction; white blood cells; prostaglandins and leukotrienes; and the biology of gentle muscle and endothelium. the quantity offers a whole precis of crucial advancements within the box with nice impression for arteriosclerosis research.
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Extra info for Molecular Biology of the Arterial Wall
1986). SUMMARY POGF is a ubiquitous growth factor that can be formed by macrophages, endothelial cells, and smooth muscle cells, and is carried in and released from a storage granule in the platelet. PDGF may playa number of roles in embryogenesis and development, wound repair, atherosclerosis, liver cirrhosis, pulmonary fibrosis, and rheumatoid arthritis. This growth factor may also be important in various aspects of neoplasia. It may be formed by neoplastically transformed cells which can respond in an autocrine fashion, or it may stimulate other cells in a paracrine fashion, causing them to respond by forming connective tissue or by forming substances that will further stimulate the neoplastically transformed cells.
Liver Uptake of I-acetyl-LDL and I-Mal-BSA When 1311-acetyl-LDL and 1311-Mal-BSA were administered intraffiously into rats, hepatic uptake was saturable. Saturation occurred with 400 pMol I-acetyl-LDL and U1500 pMol Mal-BSA. Maximal uptake was 58 pMol/min acetyl-LDL and 862 pMol/min I-Mal-BSA, 1-3 min after injection of the radioligand. Binding Characteristics of 1311-acetyl-LDL and 1311-Mal-BSA in vitro 1) The hepatic scavenger receptor was 1450-fold purified by phase separation with Triton X-114, ion exchange chromatography with polyethylenimin cellulose, and 23 HPLC on TSK G 4000.
Endothelial cells lack receptors for PDGF and hence do not respond to the PDGF they produce. Recently we have shown that the synthesis of PDGFlike peptides by endothelial cells is a highly regulated process. For example, in endothelial cells, thrombin stimulates the exprgssion of the c-sis gene that encodes one polypeptide chain of PDGF. Transforming growth factor-s, a growth factor known to be in platelets, also enhances c-sis gene expression in these cells. Thus both thrombin and transforming growth factor-s could potentially playa role in stimulating production of PDGF-like peptides by endothelial cells in response to platelet aggregation and thrombosis at sites of vascular injury.