The Impact of Hospital/University Affiliation on Research Productivity Among US-Based Authors in the Fields of Trauma, Surgical Critical Care, Acute Care, and Emergency General Surgery.

BACKGROUND: Research productivity is critical to academic surgery and essential for advancing surgical knowledge and evidence-based practice. We aim to determine if surgeon affiliation with top US universities/hospitals (TOPS) is associated with increased research productivity measured by numbers of peer-reviewed publications in PubMed (PMIDs). METHODS: A bibliometric analysis was performed for PMIDs. Affiliated authors who published in trauma surgery (TS), surgical critical care (SCC), acute care surgery (ACS), and emergency general surgery (EGS) were evaluated for publications between 2015 and 2019, and lifetime productivity. Our analysis included 3443 authors from 443 different institutions. Our main outcome was PMIDs of first author (FA) and senior author (SA) in each field (2015-2019) and total lifetime publications. RESULTS: Significant differences exist between PMIDs from TOPS vs non-TOPS in FA-TS (1.34 vs 1.23, P = .001), SA-TS (1.71 vs 1.46, P < .001), total SA-PMIDs (44.10 vs 26.61, P < .001), and SA-lifetime PMIDs (90.55 vs 59.03, P < .001). There were no significant differences in PMIDs for FA or SA-SCC, FA or SA-ACS, FA or SA-EGS, FA-total PMIDs 2015-2019, or FA-lifetime PMIDs (P > .05 for all). CONCLUSION: There were significantly higher TS PMIDs among FAs and SAs affiliated with top US institutions in 2015-2019, along with higher total PMIDs (2015-2019) and lifetime PMIDs. These findings are of significance to future graduate medical applicants and academic surgeons who need to make decisions about training and future career opportunities.

Endothelial Cell Autophagy Maintains Shear Stress-Induced Nitric Oxide Generation via Glycolysis-Dependent Purinergic Signaling to Endothelial Nitric Oxide Synthase.

OBJECTIVE: Impaired endothelial cell (EC) autophagy compromises shear stress-induced nitric oxide (NO) generation. We determined the responsible mechanism. APPROACH AND RESULTS: On autophagy compromise in bovine aortic ECs exposed to shear stress, a decrease in glucose uptake and EC glycolysis attenuated ATP production. We hypothesized that decreased glycolysis-dependent purinergic signaling via P2Y1 (P2Y purinoceptor 1) receptors, secondary to impaired autophagy in ECs, prevents shear-induced phosphorylation of eNOS (endothelial nitric oxide synthase) at its positive regulatory site S1117 (p-eNOSS1177) and NO generation. Maneuvers that restore glucose transport and glycolysis (eg, overexpression of GLUT1 [glucose transporter 1]) or purinergic signaling (eg, addition of exogenous ADP) rescue shear-induced p-eNOSS1177 and NO production in ECs with impaired autophagy. Conversely, inhibiting glucose transport via GLUT1 small interfering RNA, blocking purinergic signaling via ectonucleotidase-mediated ATP/ADP degradation (eg, apyrase), or inhibiting P2Y1 receptors using pharmacological (eg, MRS2179 [2'-deoxy-N6-methyladenosine 3',5'-bisphosphate tetrasodium salt]) or genetic (eg, P2Y1-receptor small interfering RNA) procedures inhibit shear-induced p-eNOSS1177 and NO generation in ECs with intact autophagy. Supporting a central role for PKCδT505 (protein kinase C delta T505) in relaying the autophagy-dependent purinergic-mediated signal to eNOS, we find that (1) shear stress-induced activating phosphorylation of PKCδT505 is negated by inhibiting autophagy, (2) shear-induced p-eNOSS1177 and NO generation are restored in autophagy-impaired ECs via pharmacological (eg, bryostatin) or genetic (eg, constitutively active PKCδ) activation of PKCδT505, and (3) pharmacological (eg, rottlerin) and genetic (eg, PKCδ small interfering RNA) PKCδ inhibition prevents shear-induced p-eNOSS1177 and NO generation in ECs with intact autophagy. Key nodes of dysregulation in this pathway on autophagy compromise were revealed in human arterial ECs. CONCLUSIONS: Targeted reactivation of purinergic signaling and PKCδ has strategic potential to restore compromised NO generation in pathologies associated with suppressed EC autophagy.