Search

A maternal diagnosis of chorioamnionitis, based on maternal peripartum fever of 100.4°F alone, is commonly used as an indication for blood work and antibiotic treatment in newborns. New strategies such as the Kaiser Permanente early-onset sepsis (EOS) calculator have proven effective in identifying high-risk newborns and reducing unnecessary antibiotic administration.Retrospective data from October 2017 to September 2018 from 297 well-appearing newborns ≥35 weeks' gestational age (GA) with maternal chorioamnionitis showed that 93.6% had blood work and 90.2% were treated with antibiotics. This was despite no culture-positive cases of sepsis. Our aim was to reduce by 50% blood work evaluation and antibiotic treatment within a 6-month period.Using plan-do-study-act (PDSA) cycles, we adopted the Kaiser Permanente EOS calculator. We collected longitudinal data to track the outcomes after its implementation.In 423 newborns with maternal chorioamnionitis triaged with the EOS calculator from October 2018 to July 2020, the rates of blood culture and antibiotic treatment decreased from 93.6% to 26.7% and 90.2% to 12.3% (P.0001). In the larger population of 6426 newborns ≥35 weeks' GA, the rate of blood culture and antibiotic treatment decreased from 12.8% to 5.8% and 9.9% to 2.5% (P.0001).The EOS calculator substantially and safely decreases blood work and antibiotic administration in asymptomatic newborns with maternal chorioamnionitis.Our findings provide further evidence for the effectiveness and safety of the EOS calculator.Video abstract available athttps://journals.lww.com/advancesinneonatalcare/Pages/videogallery.aspx.

Microtubule associated proteins MAP1B and MAP2 are important components of the neuronal cytoskeleton. During early development of the brain, MAP1B (340 kDa) is present as two isoforms that differ in their level of phosphorylation, while MAP2 is expressed as a single high molecular weight isoform (MAP2B, 280 kDa) and a low molecular weight form (MAP2C, 70 kDa). In this study we examined and compared the sensitivities of MAP1B and MAP2, obtained from MT preparations and brain homogenates of young rats, to degradation by calcium-activated neutral protease, calpain II. We found that in MAPs prepared from microtubules the two isoforms of MAP1B had comparable sensitivity to calpain-mediated proteolysis. Similarly, the high and low molecular weight forms of MAP2 were equally sensitive to digestion by calpain. However, although both MAPs were very susceptible to calpain-mediated proteolysis, MAP1B was more resistant to degradation by calpain than MAP2. Furthermore, the endogenous degradation of MAPs in neonate brain homogenates was calcium-dependent and inhibited by leupeptin, and the pattern of degradation products for MAP1B and MAP2 was similar to that of calpain-mediated proteolysis. These data suggest that calpain can play a role in the regulation of MAPs levels during brain development, in relation to normal neuronal differentiation and disorders associated with neurodegeneration.

Plasmolipin is a plasma membrane proteolipid which has recently been described as a component of myelin (Cochary et al.: Journal of Neurochemistry 55:602-610, 1990). The present study reports the expression and localization of plasmolipin in primary glial cultures and secondary oligodendrocyte cultures. Double-label immunofluorescence showed that plasmolipin was expressed by galactocerebroside (GC)-positive oligodendrocytes, but was absent from astrocytes, characterized by their positive staining for glial fibrillary acidic protein (GFAP). At 1 week in culture plasmolipin staining was relatively weak in the cell body of some of the GC-positive cells. During the following 3 weeks in culture plasmolipin staining of oligodendrocytes gradually increased and was present in the cell body, its plasma membrane, and all the processes. However, the plasmolipin antibodies did not stain regions of the flat membrane sheets. Western blot analysis of homogenates from primary glial cultures showed that plasmolipin levels gradually increased during the first 5 weeks in culture. We conclude that the presence of plasmolipin in myelin is a result of its expression by oligodendrocytes.

Microtubule-associated protein MAP1B from neonatal rat brain was separated on sodium dodecyl sulfate-containing polyacrylamide gels into two isoforms (high and low MAP1B), both of which were recognized by a panel of monoclonal and polyclonal antibodies against MAP1B. In addition, SMI31, a monoclonal antibody directed against phosphorylated epitopes of the neurofilament proteins, showed phosphatase-sensitive reactivity against the high isoform of MAP1B. The antigenic relationship between the phosphorylated isoform of MAP1B and neurofilaments was confirmed by the reactivity of SMI31 with the immunoprecipitated MAP1B protein. After dephosphorylation of MAP1B with alkaline phosphatase, the higher-molecular-weight isoform of MAP1B was no longer detectable with phosphate-insensitive anti-MAP1B antibodies, whereas there was a significant increase in the immunoreactivity of the lower-molecular-weight MAP1B isoform. These data suggest that the structural microheterogeneity of MAP1B is due to differences in phosphorylation. The two isoforms were present in all brain regions of the young rat. During brain development, the general decrease in MAP1B levels was accompanied by changes in the relative amount of the two isoforms. In particular, the phosphorylated isoform of MAP1B decreased dramatically to almost undetectable levels in adult brain. This conclusion was further supported by immunoblotting analysis that showed the disappearance of phosphorylated epitopes of MAP1B early during brain development. In addition, dephosphorylation experiments demonstrated the phosphatase sensitivity of the phosphorylated isoform throughout development.

Microtubule-associated protein 1B (MAP1B) is a major constituent of the neuronal cytoskeleton early in development. This protein is present in embryonic brain and is composed of two isoforms that are the result of differential phosphorylation. We examined the distribution of MAP1B during the differentiation of cultured hippocampal neurons and compared it to that of MAP2 and tubulin. We demonstrated by immunofluorescent doublestaining that MAP1B and MAP2 are colocalized in cell bodies and the minor processes of hippocampal neurons during the early stages of development, before the establishment of neuronal polarity. Later, when neurons acquire axonal and dendritic characteristics, MAP1B is sorted into growing axons, including the growth cone, whereas MAP2 is restricted to dendrites and cell bodies. Unlike tubulin, the localization of MAP1B in growing axons is not uniform. Rather, the protein is found concentrated in the distal portion. During later stages of development, the neurons extend a network of fasciculating axonal and dendritic neurites in which the segregation of MAP1B and MAP2 is maintained. However, the staining of MAP1B in mature neuronal cultures decreases in a pattern that resembles the decline of this protein during brain development. These results support the association of MAP1B with growing axons and its correct developmental regulation in the hippocampal culture system.