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Coagulopathies
Published in Victor A. Bernstam, Pocket Guide to GENE LEVEL DIAGNOSTICS in Clinical Practice, 2019
RFLP analysis, in evaluating the carrier state, uses probes within the FVIII gene and restriction enzymes (BcII, XbaI, and BgII)extragenic probes (BgIII/DX13, and TaqI/St14)
Hair dysplasias
Published in Pierre Bouhanna, Eric Bouhanna, The Alopecias, 2015
Juan Ferrando, L. Alheli Niebla, Gerardo A. Moreno-Arias
In those cases associated with type 2 congenital pachionychia, a structural alteration of keratin 17 has been observed.28 Mutation of the ST14 gene (Cr 11q24.3-q.25) that encodes a protease (type II transmembrane serine protease matriptase) has been identified in cases of pili torti associated with hypotrichosis and ichthyosis.29 When associated with congenital hypotrichosis and juvenile macular dystrophy mutation has been identified in 16q22.1.30,31 Other mutations have also been identified in CDH3.
Higher rates of cefiderocol resistance among NDM producing Klebsiella bloodstream isolates applying EUCAST over CLSI breakpoints
Published in Infectious Diseases, 2023
Burcu Isler, Cansel Vatansever, Berna Özer, Güle Çınar, Abdullah Tarık Aslan, Caitlin Falconer, Michelle J. Bauer, Brian Forde, Funda Şimşek, Necla Tülek, Hamiyet Demirkaya, Şirin Menekşe, Halis Akalin, İlker İnanç Balkan, Mehtap Aydın, Elif Tükenmez Tigen, Safiye Koçulu Demir, Mahir Kapmaz, Şiran Keske, Özlem Doğan, Çiğdem Arabacı, Serap Yağcı, Gülşen Hazırolan, Veli Oğuzalp Bakır, Mehmet Gönen, Neşe Saltoğlu, Alpay Azap, Özlem Azap, Murat Akova, Önder Ergönül, Füsun Can, David L. Paterson, Patrick N. A. Harris
Elevated cefiderocol MICs for NDM producers were previously demonstrated in in vitro surveillance studies and the co-presence of an ESBL, particularly CTX-M, was found to be more frequent among cefiderocol-resistant metallo-beta-lactamase producers [3]. In this study, copresence of an ESBL, particularly SHV, was more frequent among cefiderocol-resistant metallo-beta-lactamase producers. We also observed an association between the MLST type and cefiderocol resistance, such that all except one of the ST14 isolates and all except one of the ST101 isolates were cefiderocol resistant and susceptible, respectively. This may partially be explained by the carbapenemase types, as 75% of the isolates in the ST14 group harboured a metallo-beta-lactamase, whereas only 5% of the ST101 isolates harboured a metallo-beta-lactamase.
The role of kallikreins in inflammatory skin disorders and their potential as therapeutic targets
Published in Critical Reviews in Clinical Laboratory Sciences, 2021
Caitlin T. Di Paolo, Eleftherios P. Diamandis, Ioannis Prassas
Of the aspartic proteases in the skin, cathepsin D is the primary protease responsible for the final stages of desquamation. Its involvement with regulating levels of CE proteins, involucrin and loricrin, is thought to contribute to dry skin and hyperkeratosis [69]. Caspases are a family of cysteine-dependent aspartate-directed proteases also found in the epidermis. Within the family of caspases, caspase-14 is the most unique as it shares very little sequence homology with fellow caspases and its expression is mainly localized to the cornified layer of the epidermis [70–72]. Caspase-14 has been shown to be involved in the processing of proFLG into FLG, with caspase-14 knockout mice displaying abnormal accumulation of FLG fragments in the SC as a result of decreased breakdown of FLG into NMF [51]. Expression of caspase-14 is thought to be associated with inflammatory cytokines, suggesting a possible link between the skin barrier function and inflammation [73]. Matriptase and prostasin, like KLKs, are also serine proteases involved in desquamation and the processing of proFLG, however, they are both membrane bound [74]. Mutations in the matriptase gene ST14 leads to ichthyosis due to impaired degradation of corneodesmosomes [75,76]. It is evident that dysregulation of epidermal proteases underlies many of the features associated with inflammatory skin disorders.
Inhibitors of type II transmembrane serine proteases in the treatment of diseases of the respiratory tract – A review of patent literature
Published in Expert Opinion on Therapeutic Patents, 2020
Alexandre Murza, Sébastien P. Dion, Pierre-Luc Boudreault, Antoine Désilets, Richard Leduc, Éric Marsault
TTSP expression is widely spread across the human body, being enriched in epithelial tissues of various origins [2,5]. The respiratory tract, where airflow from the nasal cavity to the lungs enables respiration, can be divided in two main compartments, i.e. the upper respiratory tract (from nasal cavity to larynx) and the lower respiratory tract (trachea and lungs). According to the GTEx RNA-seq database [21], three TTSPs: HPN (hepsin), TMPRSS2, and ST14 (matriptase) are expressed at high levels in healthy human lungs, while TMPRSS3 and TMPRSS13 are expressed at lower levels, in agreement with several publications Figure 1B [22–26]. Furthermore, other reports show low expression of TMPRSS11E (DESC1) in the lungs [27] and predominant expression of TMPRSS11D (HAT, human airway trypsin) and TMPRSS11A (HATL1, human airway trypsin like 1) in the human trachea [28,29]. Finally, both TMPRSS4 and ST14 were also found to be overexpressed in lungs affected by idiopathic pulmonary fibrosis (IPF) [30,31]. These nine TTSPs are thus expressed at different levels in the human airway in normal and/or pathological contexts. For some, their biological role in the lung needs to be better defined, yet their involvement as determinants of respiratory viral infection [32,33], respiratory system-associated diseases, and other pathologies [2,34,35] makes them attractive therapeutic targets.