Hormones water solubility

Solvent Evaporation. This encapsulation technology involves removing a volatile solvent from either an oil-in-water, oil-in-oil, or water-in-oH-in-water emulsion (19,20). In most cases, the shell material is dissolved in a volatile solvent such as methylene chloride or ethyl acetate. The active agent to be encapsulated is either dissolved, dispersed, or emulsified into this solution. Water-soluble core materials like hormonal polypeptides are dissolved in water that contains a thickening agent before dispersion in the volatile solvent phase that contains the shell material. This dispersed aqueous phase is gelled thermally to entrap the polypeptide in the dispersed aqueous phase before solvent evaporation occurs (21). 

Inhibin and Activin. Inhibin, a water-soluble, gonadal factor known for over 50 years to inhibit pituitary function, has been isolated and identified (127—130). Inhibin is a glycoprotein hormone that preferentially inhibits the secretion of FSH. It consists of an a-chain subunit, mol wt 14,000, linked by disulfide bonds to a P-chain subunit, mol wt 18,000. There exist two forms of the P-chain subunit, P-A and P-B. The smaller subunit combines with either the P-A or P-B subunit to form inhibin-A or inhibin-B, respectively. 

They are usually administered intramuscularly by Injection. Since they are not soluble in water they form a so-called depot that remains at or near the site of injection. As the esters slowly hydrolyze by exposure to body fluids, the relatively water-soluble estrone is released and finds its way into the bloodstream. In this way the patient is provided with a reasonably constant low-level dose of the hormone. 

Bilirubin is nonpolar and would persist in cells (eg, bound to lipids) if not rendered water-soluble. Hepatocytes convert bilirubin to a polar form, which is readily excreted in the bile, by adding glucuronic acid molecules to it. This process is called conjugation and can employ polar molecules other than glucuronic acid (eg, sulfate). Many steroid hormones and drugs are also... 

Their hydroxylated products are more water-soluble than their generally lipophilic substrates, facilitating excretion Liver contains highest amounts, but found In most If not all tissues. Including small Intestine, brain, and lung Located in the smooth endoplasmic reticulum or in mitochondria (steroidogenic hormones)... 

Protein/peptide hormones are derived from amino acids. These hormones are preformed and stored for future use in membrane-bound secretory granules. When needed, they are released by exocytosis. Protein/peptide hormones are water soluble, circulate in the blood predominantly in an unbound form, and thus tend to have short half-lives. Because these hormones are unable to cross the cell membranes of their target tissues, they bind to receptors... 

Steroid and thyroid hormones are minimally soluble in the blood. Binding to plasma proteins renders them water soluble and facilitates their transport. Protein binding also prolongs the circulating half-life of these hormones. Because they are lipid soluble, they cross cell membranes easily. As the blood flows through the kidney, these hormones would enter cells or be... 

Water soluble hormone release Transmitter release Vesicle trafficking proteins... 

Urea ((NH2)2CO), a small and highly water soluble molecule, is an end product of amine and ammonia nitrogen metabolism and as such represents an example of biodetoxification (Section 6.4). The process is discussed in this section because it illustrates a genuine de novo biosynthetic pathway rather than detoxification involving chemical modification, via phase I and phase II reactions, of a pre-existing molecule as is the case for haem or steroid hormones. 

Hormones are divided into two major categories, those that are water soluble (hydrophilic) and those that are lipid soluble (lipophilic, also known as hydrophobic). Important properties of these two classes are shown in Table 1-9-1,... 

Water-soluble hormones must transmit signals to affect metabolism and gene ejcpression without themselves entering the cytoplasm. They often do so via second messenger systems that, in turn, activate protein kinases. 

Some water-soluble hormones bind to receptors with intrinsic protein kinase activity (often tyrosine kinases). In this case, no second messenger is required for protein kinase activation. The insulin receptor is an example of a tyrosine kinase receptor. 

Table 1-9-2 is a summary of the major components of water-soluble hormone pathways reviewed in this section. There are several different G proteins (GTP-binding) involved. Tfimeric G pro- teins include G, Gj, G, and in the photoreceptor pathway reviewed in Chapter 10, G (trans- ducin). Receptors that engage these aU have the 7-helix membrane-spanning structure. Receptor stimulation causes the Ga subunit to bind GTP and become active. The Ga subunit subsequently hydrolyzes the GTP to GDP, terminating the signal. The p21 G protein is monomeric. 

The natural hormones are unsuitable for oral application because they are subject to presystemic hepatic elimination. Estradiol is converted via estrone to estriol by conjugation, all three can be rendered water soluble and amenable to renal excretion. The major metabolite of progesterone is pregnandiol, which is also conjugated and eliminated renally. 

Insulin suspensions. When the hormone is injected as a suspension of insulin-containing particles, its dissolution and release in subcutaneous tissue are retarded (rapid, intermediate, and slow insulins). Suitable particles can be obtained by precipitation of apolar, poorly water-soluble complexes consisting of anionic insulin and cationic partners, e.g the polycationic protein protamine or the compound aminoqui-nuride (Surfen). In the presence of zinc and acetate ions, insulin crystallizes crystal size determines the rate of dissolution. Intermediate insulin preparations (NPH or isophane, lente or zinc insulin) act for 18 to 26 h, slow preparations (protamine zinc insulin, ultralente or extended zinc insulin) for up to 36 h. 

The kidneys main function is excretion of water and water-soluble substances (1). This is closely associated with their role in regulating the body s electrolyte and acid-base balance (homeostasis, 2 see pp.326 and 328). Both excretion and homeostasis are subject to hormonal control. The kidneys are also involved in synthesizing several hormones (3 see p. 315). Finally, the kidneys also play a role in the intermediary metabolism (4), particularly in amino acid degradation and gluconeo-genesis (see p. 154). 

Each hormone is the center of a hormonal regulation system. Specialized glandular cells synthesize the hormone from precursors, store it in many cases, and release it into the bloodstream when needed (biosynthesis). For transport, the poorly water-soluble lipophilic hormones are bound to plasma proteins known as hormone carriers. To stop the effects of the hormone again, it is inactivated by enzymatic reactions, most of which take place in the liver (metabolism). Finally, the hormone and its metabolites are expelled via the excretory system, usually in the kidney (excretion). All of these processes affect the concentration of the hormone and thus contribute to regulation of the hormonal signal. 

Hydrophilic hormones and other water-soluble signaling substances have a variety of biosynthetic pathways. Amino acid derivatives arise in special metabolic pathways (see p. 352) or through post-translational modification (see p. 374). Proteohormones, like all proteins, result from translation in the ribosome (see p. 250). Small peptide hormones and neuropeptides, most of which only consist of 3-30 amino acids, are released from precursor proteins by proteolytic degradation. 

Sulfotransferases (SULTs) are important for the metabolism of a number of drugs, neurotransmitters, and hormones, especially the steroid hormones. The cosubstrate for these reactions is 3 -phosphoadenosine 5 -phosphosulfate (PAPS) (Fig. 4.1). Like the aforementioned enzymes, sulfate conjugation typically renders the compound inactive and more water soluble. However, this process can also result in the activation of certain compounds, such as the antihypertensive minoxidil and several of the steroid hormones. Seven SULT isoforms identified in humans, including SULTs lAl to 1A3, possess activity toward phenolic substrates such as dopamine, estradiol, and acetaminophen. SULTIBI possesses activity toward such endogenous substrates as dopamine and triiodothyronine. SULTIEI has substantial activity toward steroid hormones, especially estradiol and dehydroepiandrosterone, and toward the anti-... 

Early investigations of peptides in membrane model systems included studies of mel-letin 124,125 220 221 spectra and polarization properties. This water-soluble peptide is found to be structureless in solution at neutral pH but was sensitive to environmental change. The undecapeptide hormone, substance P, a member of the tackykinin family, was also found by Choo et a].1222 to be unstructured in solution at physiological pH and to aggregate at high pH or on interaction with charged lipids. These data were used as counter-evidence to a hypothesis that the membrane surface structured the peptide to facilitate interaction with the receptor. 

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