In nonprimate mammals, the material composing the microfistula implant and the implant itself do not induce significant inflammation or tissue reaction.
Purpose: Multiple glaucoma treatment modalities seek to lower IOP by bypassing or removing a portion of the juxtacanalicular trabecular meshwork. These procedures often require expensive implants or specialized surgical instruments. The authors developed a technique for ab interno goniectomy utilizing a standard disposable 25-gauge hypodermic needle. The surgical procedure—termed bent ab interno needle goniectomy (BANG)—and preliminary results are presented here.
Methods: A retrospective chart review was performed for all patients who underwent goniotomy using a modified hypodermic needle by one of the three authors between July 2017 and June 2018. The mean and standard deviation pre- and postoperative IOP and the number of glaucoma medications were calculated. The student paired t-test was used to compare pre- and postoperative data. A P-value of <0.05 was considered statistically significant.
Results: At postoperative month six, the mean IOP was 13.3 ± 2.5 mmHg (P = 3.6 × 10−7) on 0.5 ± 0.8 topical glaucoma medications (P = 0.01). A ≥20% reduction in IOP was achieved in 73% of patients. Seventy-three percent of patients required ≥1 fewer medication, while 73% of patients required no medications for IOP control. Forty-one percent of those treated achieved IOP ≤12 mmHg.
Conclusion: The BANG procedure is a low-cost MIGS technique available to surgeons around the world with preliminary outcomes similar to more expensive alternatives.
Most covalent protein labeling schemes require a choice between visual and affinity properties, requiring the use of multiple fusion systems where both attributes are needed. While not disruptive at the single experiment level, this detail becomes critical when addressing high-throughput experimentation. Here we develop a uniform site-specific protein tag for use in both fluorescent and affinity screening. Covalent protein tagging with a stilbene reporter via promiscuous phosphopantetheinyltransferase (PPTase) modification enables a switchable, antibody-elicited fluorescent response in solution or on affinity resin. For demonstration purposes, VibB, a natural fusion protein harboring a carrier protein domain, was labeled with a stilbene tag through PPTase modification with a stilbene-labeled coenzyme A analogue. Analysis of the resulting stilbene-tagged VibB was accomplished by fluorescent and Western blot analysis with anti-stilbene monoclonal antibody EP2-19G2. The illustration of this method for general application to fusion protein analysis offers a dual role in assisting both solution-based fluorescent analysis and surface-based affinity detection and purification.
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