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Fibroids in Pregnancy
Published in Botros R.M.B. Rizk, Yakoub Khalaf, Mostafa A. Borahay, Fibroids and Reproduction, 2020
Various theories have been proposed to explain the biologic basis of preterm labor in the setting of uterine fibroids. As an example, it is possible that fibroid uteri are less distensible than nonfibrotic uteri, so that contractions occur when the uterus distends beyond a certain point [19]. Others have noted decreased oxytocinase activity in the gravid fibroid uterus, which may result in a localized increase in oxytocin levels, thereby predisposing to premature contractions [20].
Pregnancy-Related Proteins Detected by Their Biological Activities
Published in Gábor N. Than, Hans Bohn, Dénes G. Szabó, Advances in Pregnancy-Related Protein Research, 2020
Oxytocinase is formed in the syncytiotrophoblast layer of the placenta. During normal pregnancy, serum CAP activity increases progressively to a maximum at or about term. Measurement of CAP activity in serum of pregnant women can be used to assess placental and fetal weight.87 High CAP values have been detected in Rh incompatibility, and twin and diabetic pregnancies, whereas low CAP values are associated with threatened abortion and intrauterine growth retardation.87,88 The CAP activity in pregnancy serum was found to be well correlated with the plasma estriol levels.89 Determination of serum CAP activity, which is not affected by antibiotic treatment (as in the case with estriol levels), can be used as a satisfactory test for the assessment of fetal well-being.90 In patients with ovarian epithelial cancer, the serum CAP activity correlates with the tumor mass.91 Its measurement can be used for the early primary diagnosis and in the follow-up of such tumors.
Puerperal Psychosis
Published in Diana Riley, Perinatal Mental Health, 2018
There is a single report of high serum oxytocinase levels in late pregnancy in a woman who later became psychotic78. This enzyme degrades oxytocin and may also have an effect on other peptides.
ERAP1: a potential therapeutic target for a myriad of diseases
Published in Expert Opinion on Therapeutic Targets, 2020
Emma Reeves, Yasmin Islam, Edward James
The peptide trimming function of ERAP1 has been demonstrated by multiple groups and confirmed in a number of cell lines and animal models, and is responsible for the primary peptide processing event in the ER [7–12]. ERAP1, ERAP2 and insulin-regulated aminopeptidase (IRAP), an enzyme expressed in endosomes with analogous peptide trimming function with ERAP1/2, are members of the M1 zinc metalloproteases, specifically the oxytocinase subfamily, all of which are characterized by the presence of two key motifs in the active site; GXMEN substrate binding site and HEXXH-X18E zinc binding motif [13–15]. ERAP2 and IRAP share 49% and 43% sequence homology with ERAP1, mostly within the conserved active site domains. Interestingly, mice only express ERAP1 (ERAAP in mice) and IRAP, with no ERAP2 gene.