6 results match your criteria: "Massachusetts General Hospital and Shriners Burns Hospital[Affiliation]"

Magnetization transfer contrast MRI in GFP‑tagged live bacteria.

Mol Med Rep

January 2019

NMR Surgical Laboratory, Department of Surgery, Massachusetts General Hospital and Shriners Burns Hospital, Harvard Medical School, Boston, MA 02114, USA.

Green fluorescent protein (GFP) is a widely utilized molecular reporter of gene expression. However, its use in in vivo imaging has been restricted to transparent tissue mainly due to the tissue penetrance limitation of optical imaging. Magnetization transfer contrast (MTC) is a magnetic resonance imaging (MRI) methodology currently utilized to detect macromolecule changes such as decrease in myelin and increase in collagen content.

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Effects of Exendin-4 on pancreatic islets function in treating hyperglycemia post severe scald injury in rats.

J Trauma Acute Care Surg

December 2018

From the Department of Burns and Plastic Surgery (D.L., Y.S., C.S., L.L., D.Z., L.M.), the First Affiliated Hospital of Chinese PLA General Hospital, Beijing, China; Anesthesia, Critical Care and Pain Medicine (L.M.), Massachusetts General Hospital and Shriners Burns Hospital-Boston; and Burn Unit, Department of Surgery (Y.Y.), Massachusetts General Hospital and Shriners Burns Hospital-Boston, Boston, Massachusetts.

Background: It has been established that glucagon-like peptide 1 (GLP 1) inhibits pancreatic β-cell apoptosis, increases insulin secretion, and improves glucose tolerance in scald injury. However, the effects of Exendin-4, a long-acting incretin similar to GLP 1, remained unclear in severe scald injury. Hence, this study attempted to investigate whether Exendin-4 had similar effects by protecting the histology of pancreas in severely scalded rats.

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Pressure ulcers (PUs) are common debilitating complications of traumatic spinal cord injury (SCI) and tend to occur in soft tissues around bony prominences. There is, however, little known about the impact of SCI on skin wound healing because of the lack of suitable animal models for studies in controlled experimental settings. Herein, we describe a reproducible and clinically relevant mouse model of PUs in the context of complete SCI.

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In previous work, we demonstrated the development of a novel fusion protein containing stromal cell-derived growth factor-1 alpha juxtaposed to an elastin-like peptide (SDF1-ELP), which has similar bioactivity, but is more stable in elastase than SDF1. Herein, we compare the ability of a single topical application of SDF1-ELP to that of SDF1 in healing 1 × 1 cm excisional wounds in diabetic mice. Human Leukemia-60 cells were used to demonstrate the chemotactic potential of SDF1-ELP versus SDF1 .

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Elastin-like polypeptides: A strategic fusion partner for biologics.

Biotechnol Bioeng

August 2016

Department of Biomedical Engineering, Rutgers University, 599 Taylor Road, Piscataway 08854, New Jersey.

Elastin-like peptides (ELPs) are derivatives of tropoelastin with a unique property that allows them to stay soluble below a certain critical temperature but reversibly form aggregates above that temperature. Since they are derived from tropoelastin, ELPs are biocompatible, non-toxic, and non-immunogenic. The unique properties of ELPs have made them a desirable class of fusion tags used in several biomedical applications including targeted drug delivery and enhancing the half-life of protein drugs.

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The development and characterization of SDF1α-elastin-like-peptide nanoparticles for wound healing.

J Control Release

June 2016

Department of Biomedical Engineering, Rutgers University, 599 Taylor Road, Piscataway, NJ 08854, USA. Electronic address:

Chronic skin wounds are characterized by poor re-epithelialization, angiogenesis and granulation. Previous work has demonstrated that topical stromal cell-derived growth factor-1 (SDF1) promotes neovascularization, resulting in faster re-epithelialization of skin wounds in diabetic mice. However, the clinical usefulness of such bioactive peptides is limited because they are rapidly degraded in the wound environment due to high levels of proteases.

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