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...

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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.

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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.

Transforming growth factors (TGFs) isolated from murine sarcoma virus-transformed 3T3 cells have been separated by high-pressure liquid chromatography into two subsets. One subset, called TGFα, competes with epidermal growth factor (EGF) for receptor sites, whereas the other, called TGFβ, does not. TGBβ, purified by high-pressure liquid chromatography, will not induce formation of large colonies of cells in soft agar in the absence of TGFα or EGF. However, the combined action of either TGFα or EGF (which by themselves are relatively ineffective in promoting growth of cells in soft agar) together with TGFβ results in a potent synergistic effect, with formation of large colonies. Chemically modified analogs of EGF also potentiate TGFβ activity to the extent that they bind to the EGF receptor. It is suggested that TGFβ may be an important mediator of the known effects of both TGFα and EGF on neoplastic transformation.

https://cancerres.aacrjournals.org/content/canres/42/11/4776.full.pdf

Synergistic interaction of two classes of transforming growth factors from murine sarcoma cells.

Transforming Growth Factor-@ in Human Platelets

A polypeptide having similar activity to that of EGF includes ten amino acids of the natural EGF polypeptide, in particular the sequence corresponding to the fragment from Cys (20) and Cys (31) of mEGF. The polypeptide may be formulated into a pharmaceutical or veterinary composition and be used, for example, in the treatment of gastric ulcers or for sheep shearing.

Akira Komoriya

Papers

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

Synergistic interaction of two classes of transforming growth factors from murine sarcoma cells.

Transforming Growth Factor-@ in Human Platelets

Synthetic peptides with egf like activity and pharmaceutical compositions and methods of use