Hormonal proteins and peptides, vol. 13, corticotropin (ACTH)

Hormonal proteins and peptides, vol. 13, corticotropin (ACTH)

480 BOOK REVIEWS cedural aspects of research with the peptide growth factors. The principal factors that are considered here are platelet-derived gr...

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480

BOOK REVIEWS

cedural aspects of research with the peptide growth factors. The principal factors that are considered here are platelet-derived growth factor (PDGF), fibroblast growth factor (FGF), nerve growth factor (NGF), transferrin, and erythropoietin. The principal kinds of procedures that are described for each factor are chemical isolation and purification, assay by any of a number of types of procedures (e.g., RIA, radioreceptor assay, bioassay), preparation of antibodies, preparation of cDNA’s, culture of growth factor-producing cells, immunocytochemistry, etc. Obviously, anyone contemplating a research undertaking with the growth factors would find such a “how-to-do-it” compendium of great value. It should be available in any college or university library. Comparative endocrinologists have been slow to enter the growth factor field. With guides such as the “Methods in Enzymology” series available, we may hope that growth factors in lower vertebrates and invertebrates will soon be under active study. Hormonal Proteins and Peptides, Vol. 13, Corticotropin (ACTH). Edited by C. H. LI. Academic Press, San Diego, CA, 1987. 202 pp.

ACTH, a 39 amino acid peptide, is the smallest of the hormones of the pars distalis of the (“anterior”) pituitary and a fragment of the prohormone opiomelanocortin. It has received much attention in recent reviews. However, this volume is not only a valuable addition to the series edited by Professor Li, but also it has the merit of assembling all of the recent information about the physical, chemical, and biological properties of ACTH, as well as its secretory regulation and distribution in the vertebrate organism. Herbert et al. have supplied a particularly lucid and valuable chapter on the biosynthesis of ACTH, on the expression of the opiomelanocortin gene in various tissues, and the subsequent differential proteolytic processing of the prohormone. Two chapters deal with the details of con-

trol over adrenal steroidogenesis by ACTH. One chapter, by Sandman and Kastin, concerns the central nervous and behavioral actions of ACTH. This is of special interest because of the known distribution of ACTH in the brain and its generic and molecular relationship to the opioid peptides, the endorphins, and the enkephalins. Biochemical Actions of Hormones, Vol. 14. Edited by GERALD LITWACK. Academic Press, San Diego, CA, 1987. 372 pp.

In contrast to many recent published collections of papers given at a meeting, the nine chapters in this volume have the merit of having been invited by the editor to review an area that he considered to be of important recent interest. The first two chapters are general, and the remaining seven are more specific in their focus. The first chapter deals with the mechanisms by which steroid hormones initiate specific transcriptional events in hormonal target cells through their receptors. Those of us who have not followed this field closely, and who promptly become lost in the undefined acronyms that characterize this literature, can be grateful for the effort made in this chapter to lead the reader through this alphabetic maze. It appears that the steroid hormone receptors have three recognized molecular domans: one that binds the hormone, one that binds to a specific region of DNA, and a third that is less defined as to function, but which is necessary for the hormonal action. The DNA segment that binds receptor protein is near, but not necessarily close, to the promoter region of a particular gene. The hormone-receptor binding DNA region is known as the HRE (hormone regulatory element) since it activates the promoter and therefore leads to transcription. A major theme of this chapter is that the HREs of a number of transcriptional hormone responsive systems are all homologous in containing a characteristic 5’-TGTTCT-3’ nucleotide sequence. The second chapter deals with cel-