Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Epidermal growth factor-urogastrone (EGF) caused a concentration-dependent contractile response in porcine ocular ciliary muscle preparations. The half-maximal contraction was observed at 23 ng/ml EGF (4 nM). The contractile action of EGF, which was not abolished by the removal of extracellular calcium, was not affected by atropine, tetrodotoxin, phentolamine and indomethacin. In addition to causing contractions on its own, the contractile action of EGF was potentiated in the presence of prostaglandin E1 and vasopressin. Our data point to a potential role for EGF in the regulation of ciliary muscle tension.
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PMID:Contraction of porcine ocular ciliary muscle by epidermal growth factor-urogastrone. 208 43

Two tetrapeptide sequence homologies between mouse epidermal growth factor precursor (mEGFP) and human follitropin (FSH) were revealed by a computer program that identifies identical residues among polypeptide sequences. The two tetrapeptides, Lys-Thr-Cys-Thr (KTCT) and Thr-Arg-Asp-Leu (TRDL), are present in the hormone-specific beta subunit of FSH from all species studied. These tetrapeptides are not present in the alpha subunit, which is common to all pituitary glycoprotein hormones. Both tetrapeptides are also found in mEGFP, and one tetrapeptide, TRDL, is located within the 53-residue form of mEGF purified from mouse submaxillary glands. Computer-generated hydropathy profiles predicted that both tetrapeptides are located in hydrophilic portions of the FSH beta subunit and that TRDL is in a hydrophilic portion of commercially available mEGF. Therefore, the tetrapeptides might be accessible to receptor binding sites for FSH. We report that mEGF inhibits binding of 125I-labeled human FSH to receptors in testis by 50% (I50) at a concentration of 1.8 X 10(-5) M. No binding inhibition was observed by GnRH or arginine-vasopressin at 10(-4) M, neither of which contain the tetrapeptide sequences. FSH beta subunit, which contains both tetrapeptides, also inhibited binding (I50 = 9 X 10(-8) M) of 125I-labeled human FSH to testis receptor. Thus, it appears that FSH beta subunit and mEGF are capable of inhibiting binding of FSH to testicular FSH receptors, presumably through interactions that include the homologous tetrapeptides. This presumption was supported by the observation that the synthetic tetrapeptides (KTCT or TRDL) were also active in inhibiting binding of 125I-labeled human FSH to testis receptor.
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PMID:Inhibition of iodine-125-labeled human follitropin binding to testicular receptor by epidermal growth factor and synthetic peptides. 301 10

Work over the past six to eight years has established that mitogenic polypeptides such as epidermal growth factor-urogastrone (EGF-URO) or platelet-derived growth factor (PDGF), commonly referred to as 'growth factors', can have rapid (seconds to minutes) regulatory actions in a variety of smooth muscle systems. With EGF-URO as a prototype example, this article describes three distinct smooth muscle response paradigms, two of which (type A and type B) comprise a rapid (seconds to minutes) increase in muscle tension) and one of which (type C) is characterized by an EGF-URO-mediated reduction in sensitivity to other agonists. The quite distinct signal transduction pathways for the three types of response paradigms are outlined, and the marked tissue and species variation in the types of smooth muscle responses that can be observed, even for a single growth factor agonist, are summarized. The article also illustrates that G-protein-coupled vasoactive agents such as angiotensin-II and vasopressin, which can act as 'growth factors' in cultured cell systems, can also work via tyrosine kinase pathways to cause contraction in some of the same intact smooth muscle preparations that contract in response to growth factors such as EGF-URO. Attention is drawn to the fact that many so-called 'growth factors', quite apart from stimulating cell division and differentiation, may in many instances act as rapid localized paracrine/autocrine regulators of tissues such as smooth muscle. It is also pointed out that some of the tyrosine kinase-modulated signal pathways usually associated with the mitogenic action of 'growth factors' may be involved not only in the rapid effects of agents such as EGF-URO in smooth muscle but also in the contractile actions of G-protein-linked agonists.
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PMID:The acute actions of growth factors in smooth muscle systems. 828 82