By H. Maurice Goodman
Easy clinical Endocrinology, 3rd version offers up to date assurance of speedily unfolding advances within the figuring out of hormones enthusiastic about regulating such a lot points of physically capabilities. The dialogue makes a speciality of molecular and mobile facets of hormone construction and motion firmly rooted within the context of integrative body structure. subject matters are approached from the point of view of a physiologist with 4 many years of educating experience.
This e-book is richly illustrated with either descriptive schematic diagrams and laboratory findings received in medical stories. all of the 13 in-depth chapters begins with an 'Overview' of the subject and ends with a 'Suggested interpreting' list.
* unmarried authorship offers continuity and consistency among chapters
* Richly illustrated with over 2 hundred illustrations
* IThirteen in-depth chapters incorporating the most recent insights gleaned from quickly increasing genetic stories of people and rodents
* writer has taught topic for over forty years
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Additional info for Basic Medical Endocrinology, Third Edition
In this process, storage vesicles are translocated to the cell surface, where they dock with specialized membrane proteins. Membranes of the vesicles then fuse with the plasma membrane, causing the vesicle to open and empty its contents into the extracellular fluid (Figure 9). Movement of the secretory vesicle to the cell surface and membrane fusion usually require transient increases in cytosolic calcium concentrations, brought about by release of calcium from internal organelles and from influx of extracellular calcium through activated membrane channels.
Heat shock proteins are abundant cellular proteins that are found in prokaryotes and all eukaryotic cells, and are so named because their synthesis abruptly increases when cells are exposed to high temperature or other stressful conditions. These proteins are thought to keep the receptor in a configuration that is favorable for binding the hormone and incapable of binding to DNA. Binding to its hormone causes the receptor to dissociate from Hsp 90 and the other proteins. The bound receptor then forms a homodimer with another liganded receptor molecule and undergoes a conformational change that increases its affinity for binding to DNA.
For the most part, protein phosphatases are constitutively active, but some specific protein phosphatases are directly or indirectly activated in response to hormonal stimulation. Unlike responses that require synthesis of new cellular proteins, responses that result from phosphorylation–dephosphorylation reactions occur very quickly, and therefore most second messenger-mediated responses are turned on and off without appreciable latency. These responses require the same time-consuming processes as are needed for nuclear receptormediated changes and are seen only after a delay.