ABSTRACT
BACKGROUND: A cervical cerclage is often placed for women with cervical shortening or insufficiency. There are early and late complications of cervical cerclage placement, but they rarely involve the lower urinary tract. We present a case of a lower urinary tract complication from this procedure presenting as recurrent urinary tract infections. CASE: A 43-year-old woman with a history of cerclage placement during her second pregnancy (10 years prior) presented with recurrent urinary tract infections and hematuria. Radiologic imaging and cystoscopy revealed a 2-cm bladder stone attached to suture that was subsequently removed during cystoscopy. CONCLUSION: Retained suture from a cervical cerclage can act as a nidus for bladder stone formation.
Subject(s)
Cerclage, Cervical/adverse effects , Urinary Bladder Calculi/diagnosis , Urinary Bladder Calculi/etiology , Urinary Tract Infections , Adult , Diagnosis, Differential , Female , Foreign Bodies/surgery , Humans , Pregnancy , Recurrence , Sutures , Ultrasonography , Urinary Bladder Calculi/diagnostic imagingABSTRACT
Endothelial dysfunction is an important component in the pathogenesis of atherosclerosis. The ability to assess the endothelium in a meaningful manner has been the subject of intense investigation over decades. Since the function of endothelial cells is a gauge of vascular health, assessment of vascular function is emerging as a useful tool for predicting cardiovascular risk and as a surrogate outcome measure for cardiovascular reduction intervention studies. This review highlights techniques for assessing endothelial function, focusing on a novel method of determining peripheral vascular reactivity via arterial tonometry.
Subject(s)
Arteries/physiopathology , Endothelium, Vascular/physiopathology , Fingers/blood supply , Manometry/methods , Pulsatile Flow , Atherosclerosis/diagnosis , Equipment Design , Humans , Manometry/instrumentation , Manometry/trends , VasodilationABSTRACT
A-kinase anchoring proteins (AKAPs) bind to protein kinase A (PKA) via an amphipathic helix domain that interacts with a dimerization/docking domain on the regulatory (R) subunit of PKA. Four other mammalian proteins (ROPN1, ASP, SP17, and CABYR) also contain a highly conserved RII dimerization/docking (R2D2) domain, suggesting all four proteins may interact with all AKAPs in a manner similar to RII. All four of these proteins were originally detected in the flagellum of mammalian sperm. In this report, we demonstrate that all four R2D2 proteins are expressed in a wide variety of tissues and three of the proteins SP17, CABYR, and ASP are located in motile cilia of human bronchus and fallopian tubes. In addition, we detect SP17 in primary cilia. We also provide evidence that ROPN1 and ASP bind to a variety of AKAPs and this interaction can be disrupted with anchoring inhibitor peptides. The interaction of SP17 and CABYR with AKAPs appears to be much more limited. None of the R2D2 proteins appears to bind cAMP, a fundamental characteristic of the regulatory subunits of PKA. These observations suggest that R2D2 proteins utilize docking interactions with AKAPs to accomplish their function of regulating cilia and flagella. Based on location, affinity for AKAPs and lack of affinity for cAMP, it appears that each R2D2 protein has a unique role in this process.
