Christelle Cebo - Academia.edu (original) (raw)

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Papers by Christelle Cebo

Proteomics, 2013

Camel milk has been widely characterized with regards to casein and whey proteins. However, in ca... more Camel milk has been widely characterized with regards to casein and whey proteins. However, in camelids, almost nothing is known about the milk fat globule membrane (MFGM), the membrane surrounding fat globules in milk. The purpose of this study was thus to identify MFGM proteins from Camelus dromedarius milk. Major MFGM proteins (namely, fatty acid synthase, xanthine oxidase, butyrophilin, lactadherin, and adipophilin) already evidenced in cow milk were identified in camel milk using MS. In addition, a 1D-LC-MS/MS approach led us to identify 322 functional groups of proteins associated with the camel MFGM. Dromedary MFGM proteins were then classified into functional categories using DAVID (the Database for Annotation, Visualization, and Integrated Discovery) bioinformatics resources. More than 50% of MFGM proteins from camel milk were found to be integral membrane proteins (mostly belonging to the plasma membrane), or proteins associated to the membrane. Enriched GO terms associated with MFGM proteins from camel milk were protein transport (p-value = 1.73 × 10 −14 ), translation (p-value = 1.08 × 10 −11 ), lipid biosynthetic process (p-value = 6.72 × 10 −10 ), hexose metabolic process (p-value = 1.89 × 10 −04 ), and actin cytoskeleton organization (p-value = 2.72 × 10 −04 ). These findings will help to contribute to a better characterization of camel milk. Identified MFGM proteins from camel milk may also provide new insight into lipid droplet formation in the mammary epithelial cell.

Proteomics, 2013

Camel milk has been widely characterized with regards to casein and whey proteins. However, in ca... more Camel milk has been widely characterized with regards to casein and whey proteins. However, in camelids, almost nothing is known about the milk fat globule membrane (MFGM), the membrane surrounding fat globules in milk. The purpose of this study was thus to identify MFGM proteins from Camelus dromedarius milk. Major MFGM proteins (namely, fatty acid synthase, xanthine oxidase, butyrophilin, lactadherin, and adipophilin) already evidenced in cow milk were identified in camel milk using MS. In addition, a 1D-LC-MS/MS approach led us to identify 322 functional groups of proteins associated with the camel MFGM. Dromedary MFGM proteins were then classified into functional categories using DAVID (the Database for Annotation, Visualization, and Integrated Discovery) bioinformatics resources. More than 50% of MFGM proteins from camel milk were found to be integral membrane proteins (mostly belonging to the plasma membrane), or proteins associated to the membrane. Enriched GO terms associated with MFGM proteins from camel milk were protein transport (p-value = 1.73 × 10 −14 ), translation (p-value = 1.08 × 10 −11 ), lipid biosynthetic process (p-value = 6.72 × 10 −10 ), hexose metabolic process (p-value = 1.89 × 10 −04 ), and actin cytoskeleton organization (p-value = 2.72 × 10 −04 ). These findings will help to contribute to a better characterization of camel milk. Identified MFGM proteins from camel milk may also provide new insight into lipid droplet formation in the mammary epithelial cell.