Chapter Seven
Life Flow One
The Solution For Heart Disease
by
Karl Loren
Heart Disease
Cholesterol & Cell Membranes
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Search Results
- Results for your query on June 29, 1999:
- Search all fields for: cell membrane And cholesterol And thick
- Published in 1966 through 1999
- Only select references with abstracts available
- Show references published in English only
- Show references pertaining to humans
Documents: 1 to 5 of 5
NLM Database Documents
Record 1 from database: MEDLINE
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- Title
- Structure of erythrocyte membrane and its transport functions.
- Author
- Ballas SK; Krasnow SH
- Address
-
- Source
- Ann Clin Lab Sci, 1980 May, 10:3, 209-19
- Abstract
- The red cell membrane contains approximately equal amounts of lipids and
proteins. Membrane lipids are either phospholipids or neutral lipids, mostly
unesterified cholesterol. Membrane phospholipids are asymmetrically arranged
into a lipid bilayer two molecules thick. Choline phospholipids are more
abundant in the extracellular surface whereas amino phospholipids are more
concentrated on the inner leaflet of the bilayer. Cholesterol is
intercalated between the phospholipid molecules. The relative amounts of
cholesterol and phospholipids are responsible for the fluid properties of
the erythrocyte membrane. Alterations in the membrane cholesterol-phospholipid
ratio result in morphologically abnormal erythrocytes with decreased life
span. Membrane proteins are also asymmetrically oriented within the lipid
bilayer and can be divided into three functional sets: structural, catalytic
and receptor proteins. Sprectrin and actin are the two main structural
proteins that together form a submembranous cytoskeletal meshwork that is
responsible for the viscoelastic properties of the erythrocyte membrane.
Band 3, or the anion channel, is a major transmembranous protein involved in
the transport of water and anions and is a carrier of the blood-group-I
antigen. Glycophorin A, a sialic-acid-rich glycoprotein, is the major
contact or receptor membrane polypeptide that also spans the lipid bilayer.
The MN blood group determinants and possibly other biologic receptor sites
have been localized on the extracellular portion of glycophorin A. At least
35 to 40 enzymes are confined to the membrane and, undoubtedly, play a vital
role in the maintenance of normal structure and function of the erythrocyte.
- Language of Publication
- English
- Unique Identifier
- 80240578
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- MeSH Heading (Major)
- Erythrocyte Membrane|*PH/UL; Erythrocytes|*PH
- MeSH Heading
- Biological Transport; Blood Groups|IM; Glycophorin|PH; Human; Membrane
Fluidity; Membrane Lipids|PH; Membrane Proteins|PH; Na(+)-K(+)-Exchanging
ATPase|PH; Peptides|PH
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0091-7370
- Country of Publication
- UNITED STATES
Record 2 from database: MEDLINE
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- Title
- Lipids of the Golgi membrane.
- Author
- van Meer G
- Address
- Academic Medical Center, University of Amsterdam, Dept of Cell Biology and
Histology, The Netherlands. G.vanMeer@AMC.UvA.NL
- Source
- Trends Cell Biol, 1998 Jan, 8:1, 29-33
- Abstract
- The thin membrane of the endoplasmic reticulum matures into the thick
plasma membrane in the Golgi apparatus. Along the way, the concentrations of
cholesterol and sphingolipids increase. Here, Gerrit van Meer discusses how
this phenomenon may reflect an intricate lipid-protein sorting machinery.
Synthesis of sphingolipids, translocation across the Golgi membrane and
lateral segregation into lumenal domains seem to be key events. In addition,
signalling lipids indicate the lipid status of the Golgi and interact with
proteins of the transport machinery to regulate membrane flux.
- Language of Publication
- English
- Unique Identifier
- 98360918
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- MeSH Heading (Major)
- Golgi Apparatus|CH/*ME/PH; Intracellular Membranes|CH/*ME/PH; Membrane
Lipids|*/BI/CH/ME/PH
- MeSH Heading
- Animal; Biological Transport; Human; Models, Biological; Signal
Transduction
- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0962-8924
- Country of Publication
- ENGLAND
Record 3 from database: MEDLINE
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- Title
- Histochemical aspects concerning the synthesis and the fate of cholesterol
into the epidermis.
- Author
- Silveira SR; Hadler WA
- Address
-
- Source
- Acta Histochem, 1984, 74:2, 145-55
- Abstract
- By means of a suitable histochemical method free cholesterol and its
esters could be detected into the epidermis layers. The results show that in
the stratum spinosum keratinocytes free cholesterol appears as an amorphous
or granular structure apparently protein unbound; into the stratum
granulosum keratinocytes the cholesterol becomes protein-bound and its most
part undergoes esterified. The extracellular compartment nearly the stratum
granulosum contains a little amount of cholesterol esters loosely bound to
proteins. The results suggest that free cholesterol after being synthesized
into the cytoplasm of the stratum spinosum and granulosum keratinocytes, it
is partially esterified and becomes protein-bound, appearing as fine
granules within the cytoplasm of the granulous cells. From this site it
takes to fates:1. Its most part remains into the granulous cell cytoplasm
and at the same time the granulous cell develop to the horny cell it is
placed on the thick cell membrane inner surface contributing to its
thickness; 2. Another part after reaching the extracellular compartment it
is spread over the thick membrane out surface. Inside the thick cell
membrane, into the horny layer, free cholesterol is continuously esterified
since the keratinizing cell migrate to the periphery; however even at the
most peripheral layers the free cholesterol predominates. Either free
cholesterol or its esters, contained into the keratinizing cell thick
membrane, were excreted throughout the horny layer exfoliation. The
keratinizing cell cytoplasm does not contain neither free cholesterol nor
its esters.
- Language of Publication
- English
- Unique Identifier
- 84276708
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- MeSH Heading (Major)
- Cholesterol|*ME; Histological Techniques|*; Skin|AH/*ME
- MeSH Heading
- Animal; Cats; Cholesterol Esters|ME; Cytoplasm|ME; Cytoplasmic Granules|ME;
Dogs; Epidermis|ME; Guinea Pigs; Human; Mice; Opossums; Protein Binding;
Rabbits; Rats
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0065-1281
- Country of Publication
- GERMANY, EAST
Record 4 from database: MEDLINE
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- Title
- A histochemical study on the vitamin D synthesis into the epidermis.
- Author
- Silveira SR; Hadler WA
- Address
-
- Source
- Acta Histochem, 1985, 76:2, 225-34
- Abstract
- Using a suitable histochemical method vitamins D and 7-dehydrocholesterol
could be shown into the epidermis of several mammal species. As the
histochemical method used is able to discriminate vitamins D and
7-dehydrocholesterol from cholesterol and its esters, the sites where these
vitamins were synthesized within the epidermis layers could be established.
Vitamins D and 7-dehydrocholesterol were found into the epidermis in the
same sites where cholesterol and its esters take place, such as: the
keratinizing cell thick membrane and the stratum spinosum and stratum
granulosum keratinocytes cytoplasm. Inside the keratinocyte cytoplasm
vitamin D shows a granular pattern and appears weakly bound to proteins. The
reactivity of such granules seems to be partially blocked as could be shown
by an hydrolysis accomplished previously. After the hydrolysis reactive
vitamin D was also found inside the epidermis intercellular space. The
results suggest that vitamin D is synthesized into the cytoplasm of stratum
spinosum and stratum granulosum keratinocytes, where it appears weakly bound
to proteins. Afterwards it reaches the intercellular space, where its
synthesis is accomplished and it becomes firmly protein-bound losing its
histochemical reactivity. However, after a suitable hydrolysis the
histochemical reactivity could be recovered. From the intercellular spaces
vitamin D could take 2 fates: It was partially incorporated on the
keratinizing cell thick membrane out surface and eliminated by means of the
epidermis exfoliation. It was partially absorbed after passing across the
basement membrane. On the other hand, the vitamin D placed inside the
stratum spinosum and stratum granulosum keratinocytes cytoplasm become
incorporated on the inner surface of the keratinizing cell thick membrane.
The relationship between vitamin D biosynthesis and the epidermis lamellar
bodies was discussed.
- Language of Publication
- English
- Unique Identifier
- 85303059
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- MeSH Heading (Major)
- Skin|CY/*ME; Vitamin D|*ME
- MeSH Heading
- Animal; Cats; Comparative Study; Cytoplasm|ME; Dogs; Guinea Pigs;
Histocytochemistry; Human; Mice; Opossums; Protein Binding; Rabbits; Rats;
Species Specificity
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0065-1281
- Country of Publication
- GERMANY, EAST
Record 5 from database: MEDLINE
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- Title
- Expression of human apolipoprotein E but not that of apolipoprotein A-I by
mouse C127 cells is associated with increased secretion of lipids in the
form of vesicles and discs.
- Author
- Herscovitz H; Gantz D; Tercyak AM; Zannis VI; Small DM
- Address
- Department of Biophysics, Boston University School of Medicine, Housman
Medical Center, MA 02118-2394.
- Source
- J Lipid Res, 1992 Jun, 33:6, 791-803
- Abstract
- Transfected mouse mammary-derived cells (C127) expressing human
apolipoprotein (apo) E (C127E) were used a) to determine whether the
lipid-binding character of apoE is sufficient to promote its assembly with
lipid to form lipoprotein-like particles when expressed by cells not
normally expressing apolipoproteins; b) to characterize the secreted
complexes in terms of morphology, size, and composition; and finally c) to
determine whether apoE or apoA-I gene expression by these transfected cells
has any effect on the levels and the profiles of the synthesized and
secreted lipids. The findings of the present study demonstrate that: a) as
determined by density gradient ultracentrifugation and gel filtration
chromatography, about 20% of the secreted [35S]methionine-labeled apoE
expressed by C127E cells is lipid-associated. b) Negative-stain electron
microscopic analysis of the lipid-protein complexes recovered in the
lipoprotein fractions (d less than 1.21 g/ml) revealed that approximately
13% of the total population of particles were discs (16 +/- 5 nm mean
diameter and 4-6 nm thick), resembling nascent high density lipoproteins (HDL).
The majority of the particles however (greater than 82%) appeared vesicular
with varying diameters (48 +/- 40 nm mean diameter). The discoidal and the
vesicular appearance of the particles secreted by C127E cells is consistent
with the composition of lipids. These consisted mostly of surface lipids,
phospholipids (45 +/- 18%), diacylglycerols (36 +/- 17%), and free
cholesterol (17 +/- 7%) (by weight). c) Expression of apoE by C127E cells
was associated with an increased release of [35S]methionine-labeled protein
and [3H]glycerol-labeled lipid (3- to 5- and 4- to 8-fold, respectively)
compared to nontransfected C127 cells. Expression of mutant apoE or normal
apoA-I, however, was not associated with increased release of the major
lipid classes compared to the parent C127 cells, strongly suggesting that
this character of C127E cells is specific to apoE expression. The release of
lipids by C127E cells could be reduced considerably by the addition of the
metabolic inhibitors, colchicine or cycloheximide (10 and 1 microM,
respectively), suggesting that lipid release by C127E cells is an active
process requiring both protein synthesis and functional secretory
mechanisms. Taken together the findings suggest that apoE expression by C127
cells promotes the formation of nascent discoidal lipoprotein-like particles
and enhances the release of vesicular lipids, possibly by promoting shedding
of cell plasma membrane fragments.
- Language of Publication
- English
- Unique Identifier
- 92381399
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- MeSH Heading (Major)
- Apolipoprotein A-I|BI/*ME/SE; Apolipoproteins E|BI/*ME/SE; Lipids|*SE
- MeSH Heading
- Animal; Cell Fractionation; Cell Line; Centrifugation, Density Gradient;
Chromatography, Gel; Clone Cells; Culture Media|CH; Human; Lipid Bilayers;
Macromolecular Systems; Mammary Neoplasms, Experimental; Mice; Support, U.S.
Gov't, P.H.S.; Transfection; Tumor Cells, Cultured
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0022-2275
- Country of Publication
- UNITED STATES
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