TY - JOUR
T1 - Gel-free shotgun proteomic analysis of human milk
AU - Picariello, Gianluca
AU - Ferranti, Pasquale
AU - Mamone, Gianfranco
AU - Klouckova, Iveta
AU - Mechref, Yehia
AU - Novotny, Milos V.
AU - Addeo, Francesco
N1 - Copyright:
Copyright 2012 Elsevier B.V., All rights reserved.
PY - 2012/3/2
Y1 - 2012/3/2
N2 - The composition of milk has adapted during the evolution of the species to fulfill the specific nutritional needs of the offspring. Currently, it is widely recognized that milk benefits go beyond mere nutrition and serve as a source of a number of functional components to the newborn, particularly host defense effectors. However, the human milk proteome description is still incomplete, primarily because the detection of low-abundance proteins remains challenging. To overcome the limitations of the classical electrophoresis-based approach, previously separated milk fat globule membrane (MFGM) and whey protein fractions were analyzed by nanoflow-high performance liquid chromatography (HPLC)/Fourier Transform-Ion Cyclotron Resonance (FT-ICR) mass spectrometry (MS). This shotgun strategy showed an as yet unmatched potential to profile low-abundance proteins in human milk. Proteins associated with 301 different gene products were identified, some of which could be clustered into subsets of protein isoforms, thus providing one of the largest protein inventories of human milk. The identified proteins, which were derived from multiple metabolic pathways, are involved in different physiological functions, such as membrane trafficking, cell signaling, fat metabolism and transport, metabolite delivery, protein synthesis/proteolysis or folding, and immunity-related actions. Nevertheless, it appears clear from this study that the overall picture of the human milk proteome is still incomplete, although several protein signatures of milk evolution are emerging.
AB - The composition of milk has adapted during the evolution of the species to fulfill the specific nutritional needs of the offspring. Currently, it is widely recognized that milk benefits go beyond mere nutrition and serve as a source of a number of functional components to the newborn, particularly host defense effectors. However, the human milk proteome description is still incomplete, primarily because the detection of low-abundance proteins remains challenging. To overcome the limitations of the classical electrophoresis-based approach, previously separated milk fat globule membrane (MFGM) and whey protein fractions were analyzed by nanoflow-high performance liquid chromatography (HPLC)/Fourier Transform-Ion Cyclotron Resonance (FT-ICR) mass spectrometry (MS). This shotgun strategy showed an as yet unmatched potential to profile low-abundance proteins in human milk. Proteins associated with 301 different gene products were identified, some of which could be clustered into subsets of protein isoforms, thus providing one of the largest protein inventories of human milk. The identified proteins, which were derived from multiple metabolic pathways, are involved in different physiological functions, such as membrane trafficking, cell signaling, fat metabolism and transport, metabolite delivery, protein synthesis/proteolysis or folding, and immunity-related actions. Nevertheless, it appears clear from this study that the overall picture of the human milk proteome is still incomplete, although several protein signatures of milk evolution are emerging.
KW - Fourier Transform-Ion Cyclotron Resonance mass spectrometry
KW - Host defense proteins
KW - Human milk
KW - Lipid droplet proteins
KW - Milk fat globule membrane proteins
KW - Shotgun proteomics
UR - http://www.scopus.com/inward/record.url?scp=84856621853&partnerID=8YFLogxK
U2 - 10.1016/j.chroma.2012.01.014
DO - 10.1016/j.chroma.2012.01.014
M3 - Article
C2 - 22277183
AN - SCOPUS:84856621853
VL - 1227
SP - 219
EP - 233
JO - Journal of Chromatography A
JF - Journal of Chromatography A
SN - 0021-9673
ER -