Thursday, April 17th, 2014

Meetings

Notices

1.April 14, 2014 Meeting in Columbia; Speaker: Dr. Maureen Kane, University of Maryland; Topic: The Use of Fast HPLC and Multiplexing MRM3 for Retinoic Acid Quantitation in Complex Matrices

1. 2014 Washington-Baltimore MSDG Young Investigator Travel Awards

Read more of this article

April Meeting: Co-sponsored with Washington Chromatography Discussion Group

Speaker: Dr. Maureen Kane, University of Maryland

Topic: The Use of Fast HPLC Multiplexing MRM3 for Retinoic Acid Quantitation in Complex Matrices

Date: Monday, April 14, 2014

Time: 6:15 pm: Dinner and Social Hour; 7:15 pm: Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)

Dinner and Social Hour Please RSVP to Christopher Crutchfield (Crutchfield@jhmi.edu) if you will be attending dinner.

Abstract:

Vitamin A is essential to numerous physiological processes including cell proliferation, differentiation, immune response, development, reproduction, cellular metabolism, and nervous system function. Metabolism activates vitamin A into an active metabolite, retinoic acid (RA), which controls gene transcription through activating nuclear receptors and can also function via non-genomic mechanisms. Because the action of RA is amplified through its signaling mechanisms and represents a key signaling node, the abundance of endogenous RA is strictly controlled. Quantification of endogenous RA is essential to understanding its biological actions and the consequences of disruption to the retinoid pathway. Additionally, there are endogenous RA isomers with distinct biological actions must be resolved to achieve accurate quantification and a full understanding of RA function. Here we describe a Fast HPLC multiplexing MRM3 assay that was developed, characterized, and applied to the detection and quantitation of RA isomers from complex matrices in order to remove interfering signal that is observed with MRM detection during some chromatographic separation systems. The combined integration of Fast HPLC using fused-core particles with an embedded polar group C18 stationary phase, LC multiplexing, and MRM3 detection is a novel combination of analysis methodology which resulted in resolution of endogenous (isobaric) RA isomers, rapid analytical throughput and enhanced specificity without compromising assay sensitivity.

Read more of this article

March Meeting

Speaker: Professor Donald Hunt, Ph.D. University of Virginia

Topic: Innovative Instrumentation and Technology for (A) characterization of intact proteins on a chromatographic time-scale and (B) Identification of Class I MHC Phosphopeptides for Immunotherapy of Cancer

Date: Monday, March 10, 2014

Time: 6:15 pm: Dinner and Social Hour; 7:15 pm: Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)

Dinner and Social Hour Please RSVP to Christopher Crutchfield (Crutchfield@jhmi.edu) if you will be attending dinner.

Abstract:

This lecture will focus on data generated with a new ion source that facilitates simultaneous generation of positively charged sample ions by electrospray ionization and negatively charged reagent ions for both electron transfer dissociation (ETD) and ion-ion proton transfer (IIPT) reactions on Orbitrap mass spectrometers. Implementation of multiple C-trap fills for enhanced sensitivity will be discussed and both peak parking, and ion ejection strategies to facilitate protein separation and enhanced sequence coverage of intact proteins will be described. Use of IIPT/ETD facilitates near complete sequence coverage on many intact proteins and is ideally suited for locating multiple posttranslational modifications on the same protein molecule. A novel approach for sequence analysis of antibodies will also be presented.

Cells in the human body communicate their health status to the immune system by degrading cellular proteins and by presenting fragments of each on the cell surface in association class I MHC proteins. Appropriately educated, cytotoxic T-lymphocytes (CTL) (CD8+ T-cells) bind to the class I MHC molecules on the cell surface, sample the protein fragments (peptides) being presented and kill those cells that express new peptides as a result of viral, bacterial and parasitic infection, tissue transplantation and cellular transformation. Since dysregulation of cell signaling pathways is a hallmark of cancer, we hypothesized that class I MHC phosphopeptides that result from these pathways should be excellent candidates for use in the immunotherapy of cancer. Recent results will be discussed.

Read more of this article

Read More Posts in Meetings