Serum amyloid A1 (SAA1) protein in human colostrum

Proteins of the serum amyloid A (SAA) family have been remarkably conserved in evolution. Their biologic function(s) are not fully defined but they are likely to be a part of primordial host defense. We have detected a ∼ 12‐kDa protein reacting with antibodies against serum amyloid A (SAA) in human...

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Main Authors: George H. Sack Jr, Natasha Zachara, Nadine Rosenblum, C. Conover Talbot Jr, Simion Kreimer, Robert Cole, Thomas L. McDonald
Format: Article
Language:English
Published: Wiley 2018-03-01
Series:FEBS Open Bio
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Online Access:https://doi.org/10.1002/2211-5463.12383
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author George H. Sack Jr
Natasha Zachara
Nadine Rosenblum
C. Conover Talbot Jr
Simion Kreimer
Robert Cole
Thomas L. McDonald
author_facet George H. Sack Jr
Natasha Zachara
Nadine Rosenblum
C. Conover Talbot Jr
Simion Kreimer
Robert Cole
Thomas L. McDonald
author_sort George H. Sack Jr
collection DOAJ
description Proteins of the serum amyloid A (SAA) family have been remarkably conserved in evolution. Their biologic function(s) are not fully defined but they are likely to be a part of primordial host defense. We have detected a ∼ 12‐kDa protein reacting with antibodies against serum amyloid A (SAA) in human colostrum by western blotting. Mass spectrometry identified the reactive species as SAA1, previously identified as a prominent member of the acute‐phase response in serum. Our finding SAA1 in human colostrum contrasts with bovine, caprine and ovine colostrum where a species corresponding to putative SAA3 is uniformly present. SAA1 protein in human colostrum presumably contributes to neonatal protection.
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spelling doaj-art-ed38f28fe8264c4eb8de67b3b53797d42024-12-26T06:31:12ZengWileyFEBS Open Bio2211-54632018-03-018343544110.1002/2211-5463.12383Serum amyloid A1 (SAA1) protein in human colostrumGeorge H. Sack Jr0Natasha Zachara1Nadine Rosenblum2C. Conover Talbot Jr3Simion Kreimer4Robert Cole5Thomas L. McDonald6Department of Biological Chemistry Johns Hopkins University School of Medicine Baltimore MD USADepartment of Biological Chemistry Johns Hopkins University School of Medicine Baltimore MD USADepartment of Obstetrics and Gynecology Johns Hopkins University School of Medicine Baltimore MD USAInstitute for Basic Biomedical Sciences Johns Hopkins University School of Medicine Baltimore MD USAInstitute for Basic Biomedical Sciences Johns Hopkins University School of Medicine Baltimore MD USADepartment of Biological Chemistry Johns Hopkins University School of Medicine Baltimore MD USADepartment of Pathology University of Nebraska Medical Center Omaha NE USAProteins of the serum amyloid A (SAA) family have been remarkably conserved in evolution. Their biologic function(s) are not fully defined but they are likely to be a part of primordial host defense. We have detected a ∼ 12‐kDa protein reacting with antibodies against serum amyloid A (SAA) in human colostrum by western blotting. Mass spectrometry identified the reactive species as SAA1, previously identified as a prominent member of the acute‐phase response in serum. Our finding SAA1 in human colostrum contrasts with bovine, caprine and ovine colostrum where a species corresponding to putative SAA3 is uniformly present. SAA1 protein in human colostrum presumably contributes to neonatal protection.https://doi.org/10.1002/2211-5463.12383acute‐phaseamyloidcolostrumserum amyloid A
spellingShingle George H. Sack Jr
Natasha Zachara
Nadine Rosenblum
C. Conover Talbot Jr
Simion Kreimer
Robert Cole
Thomas L. McDonald
Serum amyloid A1 (SAA1) protein in human colostrum
FEBS Open Bio
acute‐phase
amyloid
colostrum
serum amyloid A
title Serum amyloid A1 (SAA1) protein in human colostrum
title_full Serum amyloid A1 (SAA1) protein in human colostrum
title_fullStr Serum amyloid A1 (SAA1) protein in human colostrum
title_full_unstemmed Serum amyloid A1 (SAA1) protein in human colostrum
title_short Serum amyloid A1 (SAA1) protein in human colostrum
title_sort serum amyloid a1 saa1 protein in human colostrum
topic acute‐phase
amyloid
colostrum
serum amyloid A
url https://doi.org/10.1002/2211-5463.12383
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