Receptor-Mediated Endocytosis and Intracellular Trafficking of Lipoproteins

Heeren, Joerg; Beisiegel, Ulrike

doi:10.1007/978-3-642-00300-4_8

Cited by 3 publications

(2 citation statements)

References 109 publications

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“…The depletion of TG and enrichment of CE convert VLDL to IDL, and further to LDL. This conversion also reduces the binding affinity of apolipoprotein E (apoE) and other apolipoproteins, resulting in LDL particles with a single copy of the non-exchangeable apoB100 [ 43 ]. Angiopoietin-related protein 4 (ANGPTL4) plays an important role in regulating lipid metabolism in that it inhibits directly the lipolysis activity of LPL [ 44 ].…”

Section: Resultsmentioning

confidence: 99%

Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation

et al. 2013

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In-depth understanding of the changing functions of human milk (HM) proteins and the corresponding physiological adaptions of the lactating mammary gland has been inhibited by incomplete knowledge of the HM proteome. We analyzed the HM whey proteome (n = 10 women with samples at 1 week and 1, 3, 6, 9 and 12 months) using a quantitative proteomic approach. One thousand three hundred and thirty three proteins were identified with 615 being quantified. Principal component analysis revealed a transition in the HM whey proteome-throughout the first year of lactation. Abundance changes in IgG, sIgA and sIgM display distinct features during the first year. Complement components and other acute-phase proteins are generally at higher levels in early lactation. Proteomic analysis further suggests that the sources of milk fatty acids (FA) shift from more direct blood influx to more de novo mammary synthesis over lactation. The abundances of the majority of glycoproteins decline over lactation, which is consistent with increased enzyme expression in glycoprotein degradation and decreased enzyme expression in glycoprotein synthesis. Cellular detoxification machinery may be transformed as well, thereby accommodating increased metabolic activities in late lactation. The multiple developing functions of HM proteins and the corresponding mammary adaption become more apparent from this study.

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Section: Resultsmentioning

confidence: 99%

Quantitative Analysis of the Human Milk Whey Proteome Reveals Developing Milk and Mammary-Gland Functions across the First Year of Lactation

et al. 2013

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“…Apolipoprotein B (ApoB) differs from other apolipoproteins in that it binds strongly to and cannot be exchanged from the lipid droplets where it was originated . Other apolipoproteins, for example, ApoA1 and ApoA2, have lower fat affinities and can be released during the conversion of very low-density lipoprotein (VLDL) to intermediate/low-density lipoprotein (IDL/LDL) and further to high-density lipoprotein (HDL) . The levels of ApoB in whey increase steadily during the first 48 min of digestion and are 4 and 5 times as abundant at 36 and 48 min, respectively, as at t = 0 min (Figure A).…”

Section: Results and Discussionmentioning

confidence: 99%

Differential Digestion of Human Milk Proteins in a Simulated Stomach Model

et al. 2013

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A key element in understanding how human milk proteins support the health and development of the neonate is to understand how individual proteins are affected during digestion. In the present study, a dynamic gastric model was used to simulate infant gastric digestion of human milk, and a subsequent proteomic approach was applied to study the behavior of individual proteins. A total of 413 human milk proteins were quantified in this study. This approach demonstrated a high degree of variability in the susceptibility of human milk proteins to gastric digestion. Specifically this study reports that lipoproteins are among the class of slowly digested proteins during gastric processes. The levels of integral lysozyme C and partial lactadherin in milk whey increase over digestion. Mucins, ribonuclease 4, and macrophage mannose receptor 1 are also resistant to gastric digestion. The retention or enhancement in whey protein abundance can be ascribed to the digestive release of milk-fat-globule-membrane or immune-cell enclosed proteins that are not initially accessible in milk. Immunoglobulins are more resistant to digestion compared to total milk proteins, and within the immunoglobulin class IgA and IgM are more resistant to digestion compared to IgG. The gastric digestion of milk proteins becomes more apparent from this study.

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