Use of Proteomic Methodology for the Characterization of Human Milk Fat Globular Membrane Proteins

Charlwood, Joanne; Hanrahan, Sarah; Tyldesley, Richard; Langridge, James; Dwek, Miriam; Camilleri, Patrick

doi:10.1006/abio.2001.5498

Cited by 79 publications

(69 citation statements)

References 25 publications

(28 reference statements)

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“…The spatial and temporal distributions of isoforms can play a critical role in determining functionality whether in the context of development, maintenance of homeostasis or progression of allergic disease. From a health perspective, there have been a number of reports on proteomic characterization of milk fat globule membrane-associated proteins (MFGMPs) [13,14], otherwise difficult to study due to their hydrophobic nature. The MFGMPs, mostly post-translationally modified in glycoproteins, are thought to act as specific viral and bacterial ligands that prevent (or contribute to the prevention of) the attachment of pathogenic organisms to the intestinal mucosa of the infant [15].…”

Section: Discussionmentioning

confidence: 99%

Cow's milk allergens identification by two‐dimensional immunoblotting and mass spectrometry

Natale

Bisson

Monti

et al. 2004

Molecular Nutrition Food Res

166

123

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Cow's milk allergy (CMA) has become a common disease in early childhood, its prevalence ranging from 1.6% to 2.8% among children younger than 2 years of age. The role of different cow's milk protein (CMP) in the pathogenesis of CMA is still controversial. Even if the proteins most frequently and most intensively recognized by immunoglobulin E (IgE) seem to be the most abundant in milk (caseins and beta-lactoglobulin), with an although great variability all milk proteins appear to be potential allergens, even those that are present in trace amounts (i.e., lactoferrin, IgG, and BSA). In this work proteomics techniques have been applied for CMP allergens analysis. Allergens have been identified by immunoblotting following resolution of CMP components by two-dimensional electrophoresis. Sera from 20 milk-allergic subjects, as proven by oral provocation test, CAP-RAST and skin prick test, have been used for cow's milk major allergen identification. Cow's milk proteins and their isoforms were identified by matrix assisted laser desorption/ionization-time of flight (MALDI-TOF)-mass spectrometry. In our group of patients, the prevalence of CMP allergens, i.e., the total number of subjects sensitized to CMP divided by the total number of the subjects enrolled in the study, was: 55% alpha(s1)-casein, 90% alpha(s2)-casein, 15% beta-casein, 50% kappa-casein, 45% beta-lactoglobulin, 45% BSA, 95% IgG-heavy chain, 50% lactoferrin, and 0% alpha-lactalbumin.

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Section: Discussionmentioning

confidence: 99%

Cow's milk allergens identification by two‐dimensional immunoblotting and mass spectrometry

Natale

Bisson

Monti

et al. 2004

Molecular Nutrition Food Res

166

123

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“…Published works on milk proteomics range from the most basic whole proteome analysis with limited or no pre-MS separation (Catinella, Traldi, Pinelli, Dallaturca, & Marsilio, 1996;Sabbadin, Sergalia, Allegri, Bertazzo, & Traldi, 1999) to more complex studies involving multiple separation techniques in combination with detailed MS/MS analysis (Yamada et al, 2002;Charlwood et al, 2002;Cavaletto et al, 2002). On the whole, however, the majority of these analyses utilize only one-stage separation and limited MS analysis.…”

Section: Milk Proteomicsmentioning

confidence: 98%

Milk proteomics

O’Donnell

Holland

Deeth

et al. 2004

International Dairy Journal

129

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Milk proteins have been studied continuously for over 50 years. Knowledge of this complex protein system has evolved incrementally in recent decades, largely coinciding with advances in technology. Proteomics and associated technologies have the potential to facilitate further advances in our knowledge of milk proteins. Proteomics allows for the detection, identification and characterization of milk proteins. More importantly, proteomics facilitates the analysis of large numbers of milk proteins simultaneously.In the first part of this review we provide a description of the key techniques used within proteomic methodologies, with an emphasis on their general uses within proteomics. In the second part we summarize recent applications of proteomics to milk proteins and highlight the potential for new and rapid advances in the analysis of milk proteins. In particular, we emphasise the effectiveness of two-dimensional gel electrophoresis in combination with various mass spectrometry techniques for the detailed characterization of milk proteins. r

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“…Charlwood et al (2002) have used proteomics technology to identify glycoproteins and their constituent N-linked glycans from human milk fat globular membrane proteins. The glycans were removed from the 2D gel-separated glycoproteins with PNGase, derivatized with 3-acetamido-6-aminoacridine (AA-Ac) and identified by MS/MS using a MALDI-Q-TOF instrument.…”

Section: Proteomicsmentioning

confidence: 99%

“…Several investigators have obtained high-quality CID spectra from N-linked glycans (Charlwood et al, 2002;Harvey et al, 2000;Saba et al, 2002) and glycosphingolipids with MALDI ion sources interfaced to Q-TOF mass spectrometers. Collisional cooling of the ion beam is necessary to modulate the pulsed nature of the ion source.…”

Section: Instrumentationmentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update covering the period 2001–2002

Harvey¹

2008

Mass Spectrometry Reviews

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This review is the second update of the original review on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates that was published in 1999. It covers fundamental aspects of the technique as applied to carbohydrates, fragmentation of carbohydrates, studies of specific carbohydrate types such as those from plant cell walls and those attached to proteins and lipids, studies of glycosyl-transferases and glycosidases, and studies where MALDI has been used to monitor products of chemical synthesis. Use of the technique shows a steady annual increase at the expense of older techniques such as FAB. There is an increasing emphasis on its use for examination of biological systems rather than on studies of fundamental aspects and method development and this is reflected by much of the work on applications appearing in tabular form.

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Use of Proteomic Methodology for the Characterization of Human Milk Fat Globular Membrane Proteins

Cited by 79 publications

References 25 publications

Cow's milk allergens identification by two‐dimensional immunoblotting and mass spectrometry

Cow's milk allergens identification by two‐dimensional immunoblotting and mass spectrometry

Milk proteomics

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update covering the period 2001–2002

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