Federal funding of nursing research by the National Institutes of Health (NIH): 1993 to 2017.

BACKGROUND: There has been a dramatic increase in the number of doctoral programs (PhD and DNP) that prepare nurse research scientists and advanced practitioners since establishment of the National Institute of Nursing Research (NINR) at the National Institutes of Health (NIH) in 1985. PURPOSE: The purpose of this report is to examine the historical context of federal research funding to schools/colleges of nursing to determine if the NINR/NIH budget is adequate. METHOD: Data were extracted from the NIH RePORT/ER database from 1993 to 2017. Additional data were obtained from the American Association of Colleges of Nursing. A return on investment analysis for four landmark nursing studies is included. FINDINGS: The percent of the NINR budget awarded to schools/colleges of nursing peaked in 2005; since 2011, more funding to schools/colleges of nursing was received from all other NIH institutes combined, compared to NINR. The return on investment for four nursing research studies, ranged from $1:$202 to $1:$1,206, and far exceeds the Standard and Poor's 500 Index (S&P 500) of 10%. DISCUSSION: Federal funding of nursing research is inadequate and a chokepoint relative to the number of doctoral programs. We suggest the NINR budget would need to increase at least fivefold to over $763 million to adequately fund nursing science. The impact of inadequate funding on the discipline is discussed.

Proteolytic activity by multiple bacterial species isolated from chronic venous leg ulcers degrades matrix substrates.

BACKGROUND: A major feature of chronic wounds is the loss of tissue, with the exposure of dermal components preventing primary closure and leading to bacterial colonization. Bacterial colonization has been proposed as one of the common underlying pathologies present in chronic wounds. The objective of this exploratory study was to identify bacteria cultured from chronic venous leg ulcers and test for proteolytic activity that degrades matrix substrates. METHOD: Bacteria were isolated, cultured, and identified from six subjects (average age = 62.8 years) over 2-10 months under an approved protocol using swabs and microbiological culture media. Proteolytic activity against (a) gelatin, (b) an elastin substrate, and (c) a serine/trypsin-sensitive substrate was determined using a colorimetric plate assay with an ELISA plate reader and zymography. RESULTS: We identified 13 bacteria that expressed proteolytic activity against one or more of the tested substrates. Of these, six were Gram-positive (Staphylococcus aureus, Enterococcus faecalis, Staphylococcus epidermidis, Streptococcus agalactiae, Corynebacterium, and Streptococcus bovis) and seven were Gram-negative (Pseudomonas aeruginosa, Escherichia coli, Proteus mirabilis, Morganella morganii, Klebsiella pneumoniae, Bacteroides fragilis, and Serratia marcescens) organisms. Two of these, S. aureus and P. aeruginosa, are recognized wound pathogens. CONCLUSIONS: Multiple bacteria species isolated from colonized venous leg ulcers have the capacity to secrete proteases capable of degrading components of the extracellular matrix important for wound healing. Matrix degradation by bacteria may contribute to delays in tissue deposition and repair, suggesting that treatment of chronic wounds should include appropriate management of colonizing bacteria.

Effect of Dakin's solution on components of a dermal equivalent.

BACKGROUND: The use of Dakin's solution on open wounds remains controversial in clinical practice. Here we investigated the effect of Dakin's solution on collagen degradation and fibroblast migration using a dermal equivalent. MATERIALS AND METHODS: Acid solubilized or neutralized collagen was combined with four dilutions of Dakin's solution (0.5%, 0.25%, 0.125%, 0.0125%), with and without serum, at room temperature and 37 degrees C. Collagen degradation was examined at 0, 1, and 24 h using 8% SDS-page gels. Cell migration was determined using dermal equivalents where fibroblasts were incorporated into 3D collagen gels and exposed to Dakin's solution with and without serum. The cells were assessed for viability and cell migration at 24 and 48 h. RESULTS: Dakin's at 0.0125% resulted in little or no collagen degradation compared with a higher concentration of 0.5%, where collagen was either partially or completely degraded. Likewise, cell migration was completely inhibited at higher concentrations, while fibroblasts in a 3D matrix at 0.0125% were still able to migrate at 24 and 48 h, albeit in fewer numbers compared with controls. Serum had a protective effect for both collagen degradation and cell migration when added together with the Dakin's solutions. A time and temperature dependent effect was also noted, with longer contact and higher temperatures being more detrimental. CONCLUSIONS: Collagen degradation and fibroblast migration is affected by the concentration of Dakin's solution, the presence or absence of serum, time exposure and temperature. Use of Dakin's solution in clinical settings should take these findings into consideration in clinical practice.

Angiogenic laminin-derived peptides stimulate wound healing.

Acceleration of the wound healing process by using angiogenic peptides has been demonstrated previously. Here we used select laminin-111 peptides, A13 and C16, from the laminin alpha1 and gamma1 chain, respectively, to test whether they are able to stimulate wound healing in a rat full thickness wound model. The 12-mer peptides C16 and A13 are highly angiogenic and bind to integrins alphavbeta3 and alpha5beta1. We show that A13 increases wound re-epithelialization as much as 17% over controls by day 4 and C16 increases coverage by 11%. Contraction of the treated wounds was increased as much as 11% for A13 and 8% for C16 at day 4. No differences were observed at day 7 with either peptide. The peptides also stimulated fibroblast migration in Boyden chamber assays. A13 increased cell migration as much as 2.4-fold on uncoated filters and as much as 16-fold on collagen type IV-coated filters over negative controls. Similarly, C16 also stimulated migration 1.8-fold on uncoated filters and as much as 12-fold on collagen-coated filters. A13 and C16 significantly decreased expression of the pro and active forms of matrix metalloproteinase 2 in foreskin fibroblasts indicating their role in collagen accumulation. We conclude that small bioactive angiogenic peptides can promote dermal wound healing and may offer a new class of stable and chemically manipulable therapeutics for wound healing.

Evaluating and managing open skin wounds: colonization versus infection.

Open skin wounds are colonized with bacteria, and optimal wound care is required to prevent progression to infection. Intact skin normally provides protection from external environmental assaults. Disruption of the skin or tissue creating an open skin wound can result in infection, dehydration, hypothermia, scarring, compromised immunity, and changes in body image. Biofilms and bacterial genomics are areas of intense scientific investigation in the face of the emerging threat of bacterial resistance. Optimal wound care to prevent progression from colonization to infection remains the foundation of good clinical practice. On the basis of wound conditions, cleansing, debridement, measures to increase oxygenation and perfusion, adequate nutrition, and appropriate use of topical agents and antibiotics, when indicated, are the keys to managing open skin wounds. This article provides a targeted review of normal skin flora, wound healing, prevention of skin infection, colonization versus infection, biofilms, genomics and infectious disease, and management of open skin wounds.