CARDIOVASCULAR disease remains the chief cause of death in the United States and Western Europe, and atherosclerosis, the principal cause of myocardial and cerebral infarction, accounts for the majority of these deaths.1 This review, like its predecessor,2 will not attempt to cover all literature on atherosclerosis. In a previous review of the pathogenesis of atherosclerosis,2 Glomset and I discussed various hypotheses of atherogenesis2 3 4 5 6 7 and emphasized the importance of intimal smooth-muscle proliferation as the key event in the development of the advanced lesions of atherosclerosis. The response-to-injury hypothesis of atherogenesis2 3 4 5 6 proposes that "injury" to the endothelium is the initiating event in . . .

The Pathogenesis of Atherosclerosis — An Update

Werner, Sabine, and Richard Grose. Regulation of Wound Healing by Growth Factors and Cytokines. Physiol Rev 83: 835–870, 2003; 10.1152/physrev.00032.2002.—Cutaneous wound healing is a complex proce...

/pdf/regulation-of-wound-healing-by-growth-factors-and-cytokines-2zk7orhjdk.pdf

Regulation of Wound Healing by Growth Factors and Cytokines

Transforming growth factor-beta stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix.

The biology of platelet-derived growth factor

The partial amino-acid sequence of purified human transforming growth factor-beta (TGF-beta) was used to identify a series of cDNA clones encoding the protein. The cDNA sequence indicates that the 112-amino acid monomeric form of the natural TGF-beta homodimer is derived proteolytically from a much longer precursor polypeptide which may be secreted. TGF-beta messenger RNA is synthesized in various normal and transformed cells.

/pdf/human-transforming-growth-factor-beta-complementary-dna-16zn58cf34.pdf

Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells.

Transforming growth factor-beta in human platelets. Identification of a major storage site, purification, and characterization.

Platelet-derived growth factor (PDGF) is known to be involved in regulating the mitosis of connective tissue cells, and recent studies have also shown that it may function in mediating cellular transformation. The oncogene carried by simian sarcoma virus, sis, is homologous to one chain of PDGF, and treatment of non-neoplastic cells with this growth factor results in increased transcription of another oncogene, myc (ref. 9). PDGF also stimulates the synthesis of proteins that are characteristic of transformed cells. However, phenotypic transformation does not appear to result from the action of PDGF alone. For example, expression of myc does not transform cells in the absence of other oncogene expression. We have recently shown that platelets contain another peptide growth factor, transforming growth factor-beta (TGF-beta)12,13, in addition to PDGF. We report here that extracts of human platelets can induce anchorage-independent growth of nonneoplastic rat kidney (NRK) fibroblasts, but that purified PDGF alone does not elicit this effect. Rather, the transforming activity of the platelet extract is due to a concerted action of three distinct peptides: PDGF, TGF-ss and a newly identified analogue of epidermal growth factor (EGF).

Cellular transformation by coordinated action of three peptide growth factors from human platelets

Transforming growth factor-β controls receptor levels for epidermal growth factor in NRK fibroblasts

Transforming Growth Factor-@ in Human Platelets

This article was the result of collaboration between various members of Anfinsen's lab at the NIAMD with Hunkapiller and
 Hood at Caltech. In it, they addressed the difficult problem of determining the amino acid sequence of Human Lymphoblastoid
 Interferon (HuIFN-alpha). Earlier attempts to sequence the amino-terminal portion of this molecule using conventional methods
 failed due to insufficient quantities of interferon. Through this collaboration, Anfinsen's lab developed a microsequencer,
 a technology that allowed them to obtain amino acid sequence data on 10 to 20 picomoles of protein. Because of this, they
 were able to successfully determine the amino-terminal amino acid sequence of the major component of human lymphoblastoid
 interferon (HuIFN-alpha).

Dorothea M. Miller

Papers

Transforming growth factor-beta in human platelets. Identification of a major storage site, purification, and characterization.

Cellular transformation by coordinated action of three peptide growth factors from human platelets

Transforming growth factor-β controls receptor levels for epidermal growth factor in NRK fibroblasts

Transforming Growth Factor-@ in Human Platelets

Human lymphoblastoid interferon: purification, amino acid composition, and amino-terminal sequence