The proteomic approach to analysis of human milk fat globule membrane

被引：57

作者：

Cavaletto, M

Giuffrida, MG

Conti, A

机构：

[1] Univ Piemonte Orientale, Dept Environm & Life Sci, I-15100 Alessandria, Italy

[2] CNR, Inst Sci Food Prod, I-10126 Turin, Italy

来源：

CLINICA CHIMICA ACTA | 2004年 / 347卷 / 1-2期

关键词：

human milk; mass spectrometry; milk fat globule membrane; proteome; two-dimensional electrophoresis;

D O I：

10.1016/j.cccn.2004.04.026

中图分类号：

R446 [实验室诊断]; R-33 [实验医学、医学实验];

学科分类号：

1001 ;

摘要：

Lactating mammary epithelial cells do not adhere to the classical rule of lipid secretion since lipids are secreted enveloped by the milk fat globule membrane (MFGM) via a budding process. Historically, biochemical studies of MFGM proteins focused on the analysis of single molecules. Today, thanks to proteomic technologies, it is now possible to comprehensively analyse the protein component of MFGM. Questions concerning: (1) protein organization within the MFGM structure; (2) correlation to the intracellular secretion pathway; and (3) display of multiple specialized functions, can now be addressed. Proteomics allows for rapid identification of the total MFGM proteins thereby providing a global functional screen of the lactating cell. In addition to their nutritional value, human MFGM proteins have important protective functions against bacteria, viruses and protozoa. Identifying the complex nature of protein-protein interactions would further enhance our present knowledge of MFGM function. A speculative molecular architecture of the human MFGM is proposed. (C) 2004 Elsevier B.V. All rights reserved.

引用

页码：41 / 48

页数：8

共 48 条

[1] Butyrophilin is expressed in mammary epithelial cells from a single-sized messenger RNA as a type I membrane glycoprotein [J].