Proteome Mapping of Human Skim Milk Proteins in Term and Preterm Milk

Molinari, Claire E.; Casadio, Ylenia S.; Hartmann, Ben; Livk, Andreja; Bringans, Scott; Arthur, Peter G.; Hartmann, Peter

doi:10.1021/pr2008797

Cited by 110 publications

(99 citation statements)

References 67 publications

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“…The discovery of these EV proteins could be because milk-derived EV are underrepresented in this database, because only few studies have characterized human milkderived EV (12,13,41), contributing only 81 proteins to Vesiclepedia. Indeed, some of the proteins we identified in milk-derived EV that are not listed in Vesiclepedia, OLAH, and PTHLH, have been described in milk proteomics studies on whole milk or skim milk (22,(42)(43)(44). These proteins are thus specific to EV derived from milk (and have not been identified in other EV preparations).…”

Section: Discussionmentioning

confidence: 89%

Comprehensive Proteomic Analysis of Human Milk-derived Extracellular Vesicles Unveils a Novel Functional Proteome Distinct from Other Milk Components

Herwijnen

Zonneveld

Goerdayal³

et al. 2016

Molecular & Cellular Proteomics

146

158

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Section: Discussionmentioning

confidence: 89%

Comprehensive Proteomic Analysis of Human Milk-derived Extracellular Vesicles Unveils a Novel Functional Proteome Distinct from Other Milk Components

Herwijnen

Zonneveld

Goerdayal³

et al. 2016

Molecular & Cellular Proteomics

146

158

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“…Peptide identification was accomplished using the database searcher X! Tandem included on GMP Manager 2.2.1 (42) against a human milk protein library composed of 975 entries constructed on the basis of previous proteomic studies ( [43][44][45] and compiled from UniProt. Masses were allowed 60 ppm error.…”

Section: Discussionmentioning

confidence: 99%

Mechanistic Peptidomics: Factors That Dictate Specificity in the Formation of Endogenous Peptides in Human Milk

Guerrero

Dallas

Contreras

et al. 2014

Molecular & Cellular Proteomics

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An extensive mass spectrometry analysis of the human milk peptidome has revealed almost 700 endogenous peptides from 30 different proteins. Two in-house computational tools were created and used to visualize and interpret the data through both alignment of the peptide quasi-molecular ion intensities and estimation of the differential enzyme participation. These results reveal that the endogenous proteolytic activity in the mammary gland is remarkably specific and well conserved. Certain proteins-not necessarily the most abundant ones-are digested by the proteases present in milk, yielding endogenous peptides from selected regions. Our results strongly suggest that factors such as the presence of specific proteases, the position and concentration of cleavage sites, and, more important, the intrinsic disorder of segments of the protein drive this proteolytic specificity in the mammary gland. As a consequence of this selective hydrolysis, proteins that typically need to be cleaved at specific positions in order to exert their activity are properly digested, and bioactive peptides encoded in certain protein sequences are released. Proteins that must remain intact in order to maintain their activity in the mammary gland or in the neonatal gastrointestinal tract are unaffected by the hydrolytic environment present in milk. These results provide insight into the intrinsic structural mechanisms that facilitate the selectivity of the endogenous milk protease activity and might be useful to those studying the peptidomes of other biofluids. Molecular &

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“…En contraste con esto, las concentraciones de las caseínas α s1 y β son más bajas en la leche de las madres cuyos hijos nacieron antes de término. Esto sugiere en la leche de las madres de prematuros se produce un mayor grado de hidrólisis de sus proteínas que cuando el niño nace a término 37,38 . Esto es evidente para la actividad de la plasmina, que sería mayor en la leche en el pretérmino que en la leche de embarazos de término 7 .…”

Section: Hidrólisis De Las Proteínas De La Leche Materna Y Madurez Fetalunclassified

Avances en el conocimiento de las proteínas de la leche materna

Brunser

2018

Rev. chil. pediatr.

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Recibido el 25 de abril de 2017; aceptado el 12 de octubre de 2017 Palabras clave: Leche materna; enzimas; péptidos; tripsina; plasmina ResumenLa glándula mamaria y la leche materna son el resultado de millones de años de una evolución que llevó a una composición óptima para el crecimiento y desarrollo de recién nacidos y lactantes; la leche materna favorece el crecimiento, la adaptación y la supervivencia de su organismo y de sus órganos inmaduros. Análisis recientes han demostrado en ella la presencia de 1606 proteínas que en su mayoría son sintetizadas en los acinos de la glándula mamaria aunque otras proteínas y péptidos provienen de órganos como el sistema linfático y el aparato digestivo. La composición de la leche materna incluye enzimas que modifican sus proteínas y originan péptidos antimicrobianos, antihipertensivos y estimuladores del metabolismo. Esta actividad proteolítica actúa en sitios específicos de las cadenas peptídicas de la proteína de la leche. La activación extemporánea de estos enzimas en los acinos es regulada por péptidos inhibidores y activadores que previenen procesos inflamatorios. Algunos enzimas de la leche actúan en el tubo digestivo de recién nacidos y lactantes y complementan la menor concentración y actividad de sus propios enzimas digestivos. Así, la enteroquinasa de la leche estimula la liberación de enzimas pancreáticos (mediada por el estímulo de la colecistoquininapancreozimina); la lipasa activada por las sales biliares complementa la baja producción de lipasa pancreática. Estas actividades probablemente facilitan la nutrición de los prematuros, cuyo tubo digestivo es más permeable a las proteínas parcialmente hidrolizadas y cuyas actividades enzimáticas y factores defensivos locales no han alcanzado su plena madurez. Esto también puede estimular en ellos la tolerancia inmunológica. En este artículo se presentan los aspectos fisiológicos relevantes de la leche materna, y los avances en el conocimiento de su composición, para el cabal conocimiento del pediatra de esta importante materia. Keywords:Breast milk; enzymes; peptides; trypsin; plasmin AbstractThe mammary gland and maternal milk are the product of millions of years of evolution that resulted in an optimal composition that sustains the growth and development of newborns and infants. Maternal milk supports the growth, adaptation and survival of this immature organism. Recent studies have detected 1606 different proteins in human milk, most of them synthesized in the acini of the glandular tissue while others originate from distant organs such as the lymphoid tissue and the digestive tract. Maternal milk enzymes modify its proteins and liberate peptides with antimicrobial, antihypertensive or stimulatory activities. This proteolytic activity occurs at specific sites in peptide Correspondencia: obrunser@icloud.com

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Proteome Mapping of Human Skim Milk Proteins in Term and Preterm Milk

Cited by 110 publications

References 67 publications

Comprehensive Proteomic Analysis of Human Milk-derived Extracellular Vesicles Unveils a Novel Functional Proteome Distinct from Other Milk Components

Comprehensive Proteomic Analysis of Human Milk-derived Extracellular Vesicles Unveils a Novel Functional Proteome Distinct from Other Milk Components

Mechanistic Peptidomics: Factors That Dictate Specificity in the Formation of Endogenous Peptides in Human Milk

Avances en el conocimiento de las proteínas de la leche materna

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