Cervical Cancer and a History of Incarceration: Examining a Social Determinant of Health.

Females who are incarcerated are disproportionately burdened by cancer, particularly cervical cancer. We measured the odds of cervical cancer compared with nonscreenable cancers for females who were incarcerated before diagnosis. By comparing a cancer for which screening and vaccination are available with cancers for which neither are available, we aimed to assess the relationship of incarceration with diseases for which preventive care mitigates risk. We created a novel data set combining cancer data from a large cancer center with incarceration data from the state department of corrections. We then estimated the odds of cervical cancer relative to nonscreenable cancers for those with and without a history of incarceration. Females with a history of incarceration had greater odds of being diagnosed with cervical cancer compared with nonscreenable cancers (odds ratio = 7.04; 95% confidence interval [CI]: 4.4-11.0) relative to those who had not been incarcerated. Adjusting for race and age, the odds of cervical cancer remained significantly greater for those with a history of incarceration (adjusted odds ratio = 3.86; 95% CI: 2.3-6.3). Our findings support the need for expanded cervical cancer screening and vaccination opportunities for incarcerated females and increased access to preventive health care after release.

Intramolecular interactions in the N-domain of cardiac troponin C are important determinants of calcium sensitivity of force development.

Myocardial contraction is initiated when Ca2+ binds to site II of cardiac troponin C. This 12-residue EF-hand loop (NH2-DEDGSGTVDFDE-COOH) contains six residues (bold) that coordinate Ca2+ binding and six residues that do not appear to influence Ca2+ binding directly. We have introduced six single-cysteine substitutions (italics) within site II of cTnC to investigate whether these residues are essential for Ca2+ binding affinity in isolation and Ca2+ sensitivity of force development in single muscle fibers. Ca2+ binding properties of mutant proteins were examined in solution and after substitution into rat skinned soleus fibers. Except for the serine mutation, cysteine substitution had no effect on Ca2+ binding on cTnC in solution. However, as part of the myofilament, the threonine mutation reduced Ca2+ sensitivity while the phenylalanine mutation increased Ca2+ sensitivity. Analysis of the available crystal and NMR structures reveals specific structural mechanisms for these effects.