Exploring How Public Health Partnerships with Community-Based Organizations (CBOs) can be Leveraged for Health Promotion and Community Health.

The Academic Public Health Corps (APHC) works to support local public health in Massachusetts through varying models of collaboration. In the setting of the COVID-19 pandemic, one initiative of the APHC has been to partner with community-based organizations (CBOs) to address vaccine hesitancy and improve overall community health. The purpose of this article is to share how the APHC partnered with CBOs in Massachusetts to address COVID-19 concerns within their respective communities, and present strategies to empower communities, share resources, and increase health promotion. The APHC partnered with 2 CBOs who received the Massachusetts COVID-19 Community Grants distributed by Health Resources in Action (HRiA). These CBOs include the Association of Islamic Charitable Projects Massachusetts (AICP) and the Somali Parents Advocacy Center for Education (SPACE). Culturally relevant educational and promotional materials were created and tailored toward the communities of interest within the CBOs. Additionally, in response to the community's desire for more informational events, the APHC hosted a virtual COVID-19 Q&A panel with Muslim health care professionals that included live Arabic translation. The model of outreach that the APHC has employed illustrates an intentional way of addressing key public health issues within local communities. The success of these partnerships highlights the importance of including CBOs in conversations about public health and health equity.

Rotational thromboelastometry and standard coagulation tests for live liver donors.

PURPOSE: To study coagulation of live liver donors with standard coagulation tests (SCT) and rotational thromboelastometry (ROTEM) and investigate their relationship. METHODS: A descriptive prospective study involving 50 right hepatotomy donors with epidural catheters. ROTEM (EXTEM, INTEM, and FIBTEM represent extrinsic and intrinsic pathways of coagulation and fibrinogen activity, respectively) was measured perioperatively and on days 1, 3, 5, 10, and 30. SCTs include prothrombin time (PT), international normalized ratio (INR) of PT, activated partial thromboplastin time (aPPT), fibrinogen, and platelets. RESULTS: PT and INR reflect hypocoagulability reaching maximum on day one (16.9 ± 2.5 s, 1.4 ± 0.2, p < 0.05 compared with baseline). ROTEM was in normal ranges till day 30 with no hypercoagulability. Fibrinogen showed no correlation with maximum clot firmness (MCF) of FIBTEM (r = 0.35, p > 0.05). CFT of EXTEM was not in significant correlation with PT and INR (r = 0.16, 0.19, p > 0.05), respectively. Significant correlation between platelets and both MCF (EXTEM; r = 0.59, p = 0.004) and MCF (INTEM; r = 0.48, p = 0.027). CONCLUSION: ROTEM disagreed with SCTs and did not show the temporary hypocoagulability suggested by SCTs. Both ROTEM and SCTs showed no signs of hypercoagulability. Future studies involving ROTEM could help develop new guidelines for coagulation monitoring.

A study of 36 unrelated cases with pure erythrocytosis revealed three new mutations in the erythropoietin receptor gene.

Thirty-six unrelated cases with erythrocytosis of unknown origin were investigated. Exons 5-8 of the erythropoietin receptor gene (EPOR), the von Hippel-Lindau gene, and the prolyl hydroxylase domain protein 2 gene (PHD2) were screened by direct DNA sequencing. The Janus kinase 2 mutation, JAK2 (Val617Phe), was screened by allele specific PCR. In this study, three new mutations of EPOR causing deletions in exon 8 were found: the first led directly to a stop codon [g.5957_5958delTT (p.Phe424X)], the second to a stop codon after one residue [g.5828_5829delCC (p.Pro381GlnfsX1)] and the third to a stop codon following a frameshift sequence of 23 residues [g.5971delC (p.Leu429TrpfsX23)]. One patient had a previously reported EPOR mutation [g.6146A>G (p.Asn487Ser)] and another, a silent one (g.5799G>A). All were heterozygotes. In addition, 2 patients were positive for JAK2 (Val617Phe), and 2 reported elsewhere, were mutated in the PHD2 gene [c.606delG (p.Met202IlefsX71).

Disturbance in the HIF-1alpha pathway associated with erythrocytosis: further evidences brought by frameshift and nonsense mutations in the prolyl hydroxylase domain protein 2 (PHD2) gene.

The hypoxia-inducible factor HIF-1 is the key regulator in cellular adaptation to hypoxia. Acting through a complex pathway, interconnected with VHL and kinases, it regulates a large number of genes, such as those involved in erythropoiesis, glycolysis, pH regulation, and angiogenesis. Recently, a missense mutation [c.950C>G (p.Pro317Arg)] in the prolyl hydroxylase domain protein 2 (PHD2) gene, whose encoded protein has HIF-1alpha as a substrate, provided evidence of the PHD2 role in a case of familial erythrocytosis. In this study, we looked for mutations in the PHD2 gene, in 74 patients with unidentified erythrocytosis. We found two heterozygous carriers of frameshift mutations [c.606delG (p.Met202IlefsX71) and c.840_841insA (p.Arg281ThrfsX3)]; both located in exon 1 and a heterozygous carrier of a nonsense mutation [c.1129C>T (p. Gln377X)] in exon 3. As a result of these mutations the encoded PHD2, if synthesized, would lose its catalytic activity. The genetic defects herein described are the first frameshift and nonsense mutations reported in the PHD2 gene and, as the previous missense mutation described, suggest that a decreased prolyl hydroxylase activity disturbing the oxygen-sensing pathway might be the cause of erythrocytosis. In addition to erythrocytosis, other complications, such as inflammatory arthromyalgia, have been observed in one case.

Two French Caucasian families with dominant thalassemia-like phenotypes due to hyper unstable hemoglobin variants: Hb Sainte Seve [codon 118 (-T)] and codon 127 [CAG-->TAG (Gln-->stop]).

We report two French Caucasian families suffering from dominant thalassemia-like phenotypes due to hyper unstable hemoglobin (Hb) variants. In both cases, molecular analysis revealed a defect localized in the third exon of the beta-globin gene, resulting in dramatic changes of the Hb structure. The first one is a new variant, Hb Sainte Seve, that is associated with a frameshift mutation at codon 118 (-T). In the second family, the disease resulted from a truncated protein due to a stop mutation at codon 127 [CAG-->TAG (Gln-->Stop)]. These two observations are additional evidences of the important role played by helix H in Hb stability: its partial absence, or a large structural modification, seems to be the major reason for the hyper instability of such molecules.