A cohort study of the service-users of online contraception.

BACKGROUND: In January 2017, the first free service providing oral contraceptive pills (OCPs) ordered online and posted home became available in the London boroughs of Lambeth and Southwark - ethnically and socioeconomically diverse areas with high rates of unplanned pregnancy. There are concerns that online services can increase health inequalities; therefore, we aimed to describe service-users according to age, ethnicity and Index of Multiple Deprivation (IMD) quintile of area of residence and to examine the association of these with repeated use. METHODS: We analysed routinely collected data from January 2017 to April 2018 and described service-users using available sociodemographic factors and information on patterns of use. Logistic regression analysis examined factors associated with repeat ordering of OCPs. RESULTS: The service was accessed by 726 individuals; most aged between 20 and 29 years (72.5%); self-identified as being of white ethnic group (58.8%); and residents of the first and second most deprived IMD quintiles (79.2%). Compared with those of white ethnic group, those of black ethnic group were significantly less likely to make repeat orders (adjusted OR 0.53, 95% CI 0.31 to 0.89; p=0.001), as were those of Asian and mixed ethnic groups. CONCLUSIONS: These are the first empirical findings on free, online contraception and suggest that early adopters broadly reflect the population of the local area in terms of ethnic diversity and deprivation as measured by IMD. Ongoing service development should prioritise the identification and removal of barriers which may inhibit repeat use for black and minority ethnic groups

Contraception in Person-Contraception Online (CiP-CO) cohort study.

BACKGROUND: Online contraception services increasingly provide information, clinical assessment and home-delivered oral contraceptives (OCs). Evidence is lacking on the effects of online contraceptive service use on short-term contraceptive continuation. METHODS: Cohort study comparing contraceptive continuation between new users of a free-to-access online OC service in South East London with those from other, face-to-face services in the same area. Online questionnaires collected data on participants' sociodemographic characteristics, motivations for OC access, service ratings, OC knowledge and contraceptive use. Contraceptive use in the 4-month study period was measured using health service records. Unadjusted and multivariable logistic regression models compared outcomes between the online service group and those using other services. RESULTS: Online service-users (n=138) were more likely to experience short-term continuation of OCs compared with participants using other services (n=98) after adjusting for sociodemographic and other characteristics (adjusted OR 2.94, 95% CI 1.52 to 5.70). Online service-users rated their service more highly (mean 25.22, SD 3.77) than the other services group (mean 22.70, SD 4.35; p<0.001), valuing convenience and speed of access. Among progestogen-only pill users, knowledge scores were higher for the online group (mean 4.83, SD 1.90) than the other services group (mean 3.87, SD 1.73; p=0.007). Among combined oral contraceptive users, knowledge scores were similar between groups. CONCLUSIONS: Free-to-access, online contraception has the potential to improve short-term continuation of OCs. Further research using a larger study population and analysis of longer-term outcomes are required to understand the impact of online services on unintended pregnancy

Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces

The acylation of sugars, most commonly via acetylation, is a widely used mechanism in bacteria that uses a simple chemical modification to confer useful traits. For structures like lipopolysaccharide, capsule and peptidoglycan, that function outside of the cytoplasm, their acylation during export or post-synthesis requires transport of an activated acyl group across the membrane. In bacteria this function is most commonly linked to a family of integral membrane proteins - acyltransferase-3 (AT3). Numerous studies examining production of diverse extracytoplasmic sugar-containing structures have identified roles for these proteins in O-acylation. Many of the phenotypes conferred by the action of AT3 proteins influence host colonisation and environmental survival, as well as controlling the properties of biotechnologically important polysaccharides and the modification of antibiotics and antitumour drugs by Actinobacteria. Herein we present the first systematic review, to our knowledge, of the functions of bacterial AT3 proteins, revealing an important protein family involved in a plethora of systems of importance to bacterial function that is still relatively poorly understood at the mechanistic level. By defining and comparing this set of functions we draw out common themes in the structure and mechanism of this fascinating family of membrane-bound enzymes, which, due to their role in host colonisation in many pathogens, could offer novel targets for the development of antimicrobials

Parathyroid hormone receptors in GtoPdb v.2021.3

The parathyroid hormone receptors (nomenclature as agreed by the NC-IUPHAR Subcommittee on Parathyroid Hormone Receptors [49]) are class B G protein-coupled receptors. The parathyroid hormone (PTH)/parathyroid hormone-related peptide (PTHrP) receptor (PTH1 receptor) is activated by precursor-derived peptides: PTH (84 amino acids), and PTHrP (141 amino-acids) and related peptides (PTH-(1-34), PTHrP-(1-36)). The parathyroid hormone 2 receptor (PTH2 receptor) is activated by the precursor-derived peptide TIP39 (39 amino acids). [125I]PTH may be used to label both PTH1 and PTH2 receptors. The structure of a long-active PTH analogue (LA-PTH, an hybrid of PTH-(1-13) and PTHrP-(14-36)) bound to the PTH1 receptor-Gs complex has been resolved by cryo-electron microscopy [147]. Another structure of a PTH-(1-34) analog bound to a thermostabilized inactive PTH1 receptor has been obtained with X-ray crytallography [34]

Parathyroid hormone receptors (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

The parathyroid hormone receptors (nomenclature as agreed by the NC-IUPHAR Subcommittee on Parathyroid Hormone Receptors [47]) are family B G protein-coupled receptors. The parathyroid hormone (PTH)/parathyroid hormone-related peptide (PTHrP) receptor (PTH1 receptor) is activated by precursor-derived peptides: PTH (84 amino acids), and PTHrP (141 amino-acids) and related peptides (PTH-(1-34), PTHrP-(1-36)). The parathyroid hormone 2 receptor (PTH2 receptor) is activated by the precursor-derived peptide TIP39 (39 amino acids). [125I]PTH may be used to label both PTH1 and PTH2 receptors

Metabolic activity throughout early development of dusky kob Argyrosomus japonicus (Sciaenidae)

Metabolism quantifies the energy-consuming activities of an organism (Nelson 2016) and is used as an indication of how organisms partition energy resources to activities that allow them to survive, grow and reproduce (Post and Lee 1996). The metabolic profile, which is a composition of the various metabolic rates of an individual, therefore gives an indication of the efficiency of energy transformation and allocation (Fry 1971; Brown et al. 2004). McKenzie et al. (2016) suggested that an organism’s physiology contributes towards its ability to survive under specific environmental conditions. As a result, physiological condition can be a reflection of the performance and fitness of an organism (Pörtner 2010). When combined with information on changing environmental conditions, physiological information can provide insight into species- and community-level responses (Pörtner and Farrell 2008). These kinds of data have served numerous ecological applications, including resource management, conservation (McKenzie et al. 2016) and climate-change assessments (Pörtner and Farrell 2008)

Parathyroid hormone receptors in GtoPdb v.2023.1

The parathyroid hormone receptors (nomenclature as agreed by the NC-IUPHAR Subcommittee on Parathyroid Hormone Receptors [50]) are class B G protein-coupled receptors. The parathyroid hormone (PTH)/parathyroid hormone-related peptide (PTHrP) receptor (PTH1 receptor) is activated by precursor-derived peptides: PTH (84 amino acids), and PTHrP (141 amino-acids) and related peptides (PTH-(1-34), PTHrP-(1-36)). The parathyroid hormone 2 receptor (PTH2 receptor) is activated by the precursor-derived peptide TIP39 (39 amino acids). [125I]PTH may be used to label both PTH1 and PTH2 receptors. The structure of a long-active PTH analogue (LA-PTH, an hybrid of PTH-(1-13) and PTHrP-(14-36)) bound to the PTH1 receptor-Gs complex has been resolved by cryo-electron microscopy [148]. Another structure of a PTH-(1-34) analog bound to a thermostabilized inactive PTH1 receptor has been obtained with X-ray crytallography [35]