Original articleHigh and low molecular weight kininogen and plasma prekallikrein/plasma kallikrein in villous capillaries of human term placenta
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Cited by (24)
Cysteine cathepsins as a prospective target for anticancer therapies—current progress and prospects
2018, BiochimieCitation Excerpt :HK and LK are precursors of potent peptide hormones, the kinins, which are released proteolytically by tissue and plasma kallikreins [231]. Mammalian kininogens occur predominantly in blood plasma [232], and they are also found in other body fluids and organs such as kidney as well as in cells such as neutrophils [233–235]. The interaction between cystatins and cysteine proteases has been elucidated as reversible binding in a substrate-competing mechanism, which forms an equimolar complex with Ki values that ranged from picomolar to nanomolar [222].
Utero-placental cellular and nuclear expression of bradykinin B2 receptors in normal and preeclamptic pregnancies
2016, Pregnancy HypertensionCitation Excerpt :The absence of the previously reported increase of B2R in EVTs according to immunohistochemistry and western blotting is likely due the reduced number of samples, and by the fact that tissue lysates include other cell types and variable amounts of extracellular matrix components. Bradykinin, the ligand of both the cell membrane and nuclear B2R, can be generated by the action of ubiquitous utero-placental tissue kallikrein on low molecular weight kininogen present in endothelial cells in placental villi, as well as in maternal and fetal blood [27]. The canonical effects of bradykinin acting on the cell membrane receptor can be extrapolated to the different cell types that express the B2R, as supported by the conserved expression in equivalent cell types in human, rat and guinea-pig utero-placental units [16,28–30].
The Contact Activation System (CAS) in cord blood: Measurement of CAS components and comparison with mother's blood. A pilot study
2015, Thrombosis ResearchCitation Excerpt :It seems, however, that the explanation can also be based on the novel study concerning CAS and kallikrein-kinin system (KKS) interactions [8,18]. Because the CAS is localized within the uteroplacental unit, it may play a role in regulating placental blood flow and transplacental transport of substances and metabolites [19]. Briefly, FXIIa activates PK; PK converts HMWK into kinins, which take part in many delivery processes, e.g. bradykinin exerts an effect on the in labor activity of myometrium and uteroplacental unit [20].
KLKB1 mRNA overexpression: A novel molecular biomarker for the diagnosis of chronic lymphocytic leukemia
2015, Clinical BiochemistryCitation Excerpt :The catalytic domain of the enzyme shows high homology to the trypsin family of serine peptidases. Although it was initially considered that plasma prekallikrein is solely synthesized by hepatocytes and secreted into circulation, Hermann et al. demonstrated the presence of KLKB1 mRNA and/or protein expression in other tissues too, including kidney, adrenal gland, pancreatic islet of Langerhans, prostate, breast, ovary, placenta, heart, lung, and trachea, as well as in endothelial cells, leukocytes, fibroblasts, epithelial cells, and interstitial Leydig cells of the testes [12,13]. Moreover, immunoreactive plasma kallikrein was also detected in blood vessels [14] and brain [15].
Kininogens: More than cysteine protease inhibitors and kinin precursors
2010, BiochimieCitation Excerpt :The precursors of kinins in mammals are HK (apparent molecular mass of 90–120 kDa) and LK (50–68 kDa). Mammalian kininogens are glycoproteins synthetized in liver that occur predominantly in blood plasma at respective concentrations of 170/220 μg/ml for LK and of 70/90 μg/ml for HK [15], but are also found in other body fluids and organs such as kidney and in cells such as neutrophils [16–18]. Early purification and partial characterization of human kininogens were initiated during the 1960s and 1970s [19–21].
Tissue kallikrein and kininogen levels in fetoplacental tissues from normotensive pregnant women and women with pregnancy-induced hypertension
2007, European Journal of Obstetrics and Gynecology and Reproductive BiologyCitation Excerpt :The reason for this difference in the distribution of total, active and inactive tissue kallikrein between the various fetoplacental tissues is yet to be discerned and may reflect the nature of their requirement and functions in these tissues. For instance, in the case of the placenta, these components of KKS may be needed for the establishment and maintenance of placental blood flow [8,11]. This is further supported by the finding of higher tissue kallikrein content in placenta during early pregnancy, when cytotrophoblast activity and placentation are at their peak, as compared to that of late pregnancy [9].