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Inhibition of Phospholipase A2 by Uteroglobin and Antiflammin Peptides

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 279))

Abstract

Blastokinin (1) or uteroglobin (UG; 2) is a secretory protein with a low molecular mass (15.8 kDa). This protein was originally discovered in the rabbit uterine fluid during early pregnancy (1, 2). Its synthesis and secretion in the endometrium are stimulated by progesterone (2–5). Since its discovery in 1967, UG has been one of the most thoroughly studied markers of progesterone action in the rabbit endometrium. In addition to the uterus, UG has been found in several other organs of rabbits, namely, the oviduct, the male genital tract and the tracheobronchial tree of both male and female animals (4–9). More recently, we detected UG in the circulation of the rabbit (10). The source of this protein in circulation seems to be the tracheobronchial epithelium and/or the progesterone-induced uterine endometrium (10).

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Miele, L., Cordella-Miele, E., Facchiano, A., Mukherjee, A.B. (1990). Inhibition of Phospholipase A2 by Uteroglobin and Antiflammin Peptides. In: Mukherjee, A.B. (eds) Biochemistry, Molecular Biology, and Physiology of Phospholipase A2 and Its Regulatory Factors. Advances in Experimental Medicine and Biology, vol 279. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0651-1_9

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