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Identification in milk of a serum amyloid A peptide chemoattractant for B lymphoblasts
BACKGROUND: Normal mammary gland contains an extravascular population of B lymphoblasts, precursors of the immunoglobulin plasma cells that play a key role in the passive protection of neonates by secreting immunoglobulins to colostrum and milk. We investigated the presence of chemoattractants in th...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2637234/ https://www.ncbi.nlm.nih.gov/pubmed/19166592 http://dx.doi.org/10.1186/1471-2172-10-4 |
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author | de Jesus Rodriguez, Berardo Chevaleyre, Claire Henry, Gwénaële Mollé, Daniel Virlogeux-Payant, Isabelle Berri, Mustapha Boulay, François Léonil, Joëlle Meurens, François Salmon, Henri |
author_facet | de Jesus Rodriguez, Berardo Chevaleyre, Claire Henry, Gwénaële Mollé, Daniel Virlogeux-Payant, Isabelle Berri, Mustapha Boulay, François Léonil, Joëlle Meurens, François Salmon, Henri |
author_sort | de Jesus Rodriguez, Berardo |
collection | PubMed |
description | BACKGROUND: Normal mammary gland contains an extravascular population of B lymphoblasts, precursors of the immunoglobulin plasma cells that play a key role in the passive protection of neonates by secreting immunoglobulins to colostrum and milk. We investigated the presence of chemoattractants in the milk by analysing the chemoattractant activity of various fractions of this secretion. Milk chemoattractants are potentially involved in the recruitment of lymphocytes from the maternal bloodstream in lactating mammary glands. RESULTS: The dilution-related lymphoid cell chemoattraction of whey was associated with a < 10 kDa ultrafiltrate. Active fractions were purified by reverse-phase high performance liquid chromatography. Two peptides of 2.7 kDa (DMREANYKNSDKYFHARGNYDAA) and 1 kDa (RPPGLPDKY) were identified as fragments of the SAA protein family, tentatively identified as SAA2. Only the 2.7 kDa synthetic peptide displayed chemotactic activity, at two different optimal concentrations. At the lower concentration (3.7 nM), it attracted B-cell lymphoblasts, whereas at the higher (3.7 μM), it attracted B lymphocytes. Then, the SAA mRNA expression was analysed and we observed more SAA transcripts during lactation than gestation. CONCLUSION: These data are consistent with the SAA(23–45 )fragment being involved in preplasma B-cell recruitment to the mammary gland and resultant benefit to the neonate. |
format | Text |
id | pubmed-2637234 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-26372342009-02-07 Identification in milk of a serum amyloid A peptide chemoattractant for B lymphoblasts de Jesus Rodriguez, Berardo Chevaleyre, Claire Henry, Gwénaële Mollé, Daniel Virlogeux-Payant, Isabelle Berri, Mustapha Boulay, François Léonil, Joëlle Meurens, François Salmon, Henri BMC Immunol Research Article BACKGROUND: Normal mammary gland contains an extravascular population of B lymphoblasts, precursors of the immunoglobulin plasma cells that play a key role in the passive protection of neonates by secreting immunoglobulins to colostrum and milk. We investigated the presence of chemoattractants in the milk by analysing the chemoattractant activity of various fractions of this secretion. Milk chemoattractants are potentially involved in the recruitment of lymphocytes from the maternal bloodstream in lactating mammary glands. RESULTS: The dilution-related lymphoid cell chemoattraction of whey was associated with a < 10 kDa ultrafiltrate. Active fractions were purified by reverse-phase high performance liquid chromatography. Two peptides of 2.7 kDa (DMREANYKNSDKYFHARGNYDAA) and 1 kDa (RPPGLPDKY) were identified as fragments of the SAA protein family, tentatively identified as SAA2. Only the 2.7 kDa synthetic peptide displayed chemotactic activity, at two different optimal concentrations. At the lower concentration (3.7 nM), it attracted B-cell lymphoblasts, whereas at the higher (3.7 μM), it attracted B lymphocytes. Then, the SAA mRNA expression was analysed and we observed more SAA transcripts during lactation than gestation. CONCLUSION: These data are consistent with the SAA(23–45 )fragment being involved in preplasma B-cell recruitment to the mammary gland and resultant benefit to the neonate. BioMed Central 2009-01-23 /pmc/articles/PMC2637234/ /pubmed/19166592 http://dx.doi.org/10.1186/1471-2172-10-4 Text en Copyright © 2009 Rodriguez et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article de Jesus Rodriguez, Berardo Chevaleyre, Claire Henry, Gwénaële Mollé, Daniel Virlogeux-Payant, Isabelle Berri, Mustapha Boulay, François Léonil, Joëlle Meurens, François Salmon, Henri Identification in milk of a serum amyloid A peptide chemoattractant for B lymphoblasts |
title | Identification in milk of a serum amyloid A peptide chemoattractant for B lymphoblasts |
title_full | Identification in milk of a serum amyloid A peptide chemoattractant for B lymphoblasts |
title_fullStr | Identification in milk of a serum amyloid A peptide chemoattractant for B lymphoblasts |
title_full_unstemmed | Identification in milk of a serum amyloid A peptide chemoattractant for B lymphoblasts |
title_short | Identification in milk of a serum amyloid A peptide chemoattractant for B lymphoblasts |
title_sort | identification in milk of a serum amyloid a peptide chemoattractant for b lymphoblasts |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2637234/ https://www.ncbi.nlm.nih.gov/pubmed/19166592 http://dx.doi.org/10.1186/1471-2172-10-4 |
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