関: cell membrane protein、cell surface protein、membrane protein、membrane-associated protein、surface protein

WordNet

of or denoted by an integer
the result of a mathematical integration; F(x) is the integral of f(x) if dF/dx = f(x)
constituting the undiminished entirety; lacking nothing essential especially not damaged; "a local motion keepeth bodies integral"- Bacon; "was able to keep the collection entire during his lifetime"; "fought to keep the union intact" (同)entire, intact
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
a thin pliable sheet of material
a pliable sheet of tissue that covers or lines or connects the organs or cells of animals or plants (同)tissue layer

PrepTutorEJDIC

全体の一部分として欠くことのできない,完全なものになるに必要な / 完全無欠な / (数学で)整数の
蛋白(たんばく)質
(生物の)膜,皮膜

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/02/10 13:55:05」(JST)

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E=extracellular space; P=plasma membrane; I=intracellular space

An integral membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins are IMPs, but not all IMPs are transmembrane proteins.^[1] IMPs comprise a significant fraction of the proteins encoded in an organism's genome.^[2] Proteins that cross the membrane are surrounded by "annular" lipids (see annular lipid shell), which are defined as lipids that are in direct contact with a membrane protein. Such proteins can be separated from the biological membranes only using detergents, nonpolar solvents, or sometimes denaturing agents.

Structure

Three-dimensional structures of ~160 different integral membrane proteins have been determined at atomic resolution by X-ray crystallography or nuclear magnetic resonance spectroscopy. They are challenging subjects for study owing to the difficulties associated with extraction and crystallization. In addition, structures of many water-soluble protein domains of IMPs are available in the Protein Data Bank. Their membrane-anchoring α-helices have been removed to facilitate the extraction and crystallization. Search integral membrane proteins in the PDB (based on gene ontology classification)

IMPs can be divided into two groups:

Integral polytopic proteins (Transmembrane proteins)
Integral monotopic proteins

Integral polytopic protein

The most common type of IMP is the transmembrane protein (TM), which spans the entire biological membrane. Single-pass membrane proteins cross the membrane only once, while multi-pass membrane proteins weave in and out, crossing several times. Single pass TM proteins can be categorized as Type I, which are positioned such that their carboxyl-terminus is towards the cytosol, or Type II, which have their amino-terminus towards the cytosol. Type III proteins have multiple transmembrane domains in a single polypeptide, while type IV consists of several different polypeptides assembled together in a channel through the membrane. Type V proteins are anchored to the lipid bilayer through covalently linked lipids. Finally Type VI proteins have both a transmembrane domains and lipid anchors. ^[3]

Integral monotopic proteins

Integral monotopic proteins are associated to the membrane from one side but do not span the lipid bilayer completely.

Determination of protein structure

The Protein Structure Initiative (PSI), funded by the U.S. National Institute of General Medical Sciences (NIGMS), part of the National Institutes of Health (NIH), has among its aim to determine three-dimensional protein structures and to develop techniques for use in structural biology, including for membrane proteins. Homology modeling can be used to construct an atomic-resolution model of the "target" integral protein from its amino acid sequence and an experimental three-dimensional structure of a related homologous protein. This procedure has been extensively used for ligand-G protein-coupled receptors (GPCR) and their complexes.^[4]

Function

IMPs include transporters, linkers, channels, receptors, enzymes, structural membrane-anchoring domains, proteins involved in accumulation and transduction of energy, and proteins responsible for cell adhesion. Classification of transporters can be found in Transporter Classification Database.^[5]

For example the relationship of the bacterial phototraping pigment, bacteriorhodopsin, and the phospholipid bilayer is illustrated below. In this case the integral membrane protein spans the phospholipid bilayer seven times. The part of the protein that is embedded in the hydrophobic regions of the bilayer are alpha helical and composed of predominantly hydrophobic amino acids. The amino terminal end of the protein is in the cytosol while the C terminal region is in the outside of the cell. When a membrane contain this protein the membrane can function in photosynthesis. ^[6]

Examples

Examples of integral membrane proteins:

Insulin receptor
Some types of cell adhesion proteins or cell adhesion molecules (CAMs) such as integrins, cadherins, NCAMs, or selectins
Some types of receptor proteins
Glycophorin
Rhodopsin
Band 3
CD36
GPR30
Glucose Permease
Ion channels and Gates
Gap junction Proteins

References

^ Steven R. Goodman (2008). Medical cell biology. Academic Press. pp. 37–. ISBN 978-0-12-370458-0. Retrieved 24 November 2010.
^ Wallin E, von Heijne G (1998). "Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms". Protein Science 7 (4): 1029–38. doi:10.1002/pro.5560070420. PMC 2143985. PMID 9568909.
^ Nelson, D. L., & Cox, M. M. (2008). Principles of Biochemistry (5th ed., p. 377). New York, NY: W.H. Freeman and Company.
^ Fruchart-Marquer C, Fruchart-Gaillard C, Letellier G, Marcon E, Mourier G, Zinn-Justin S, Ménez A, Servent D, Gilquin B. (September 2011). "Structural model of ligand-G protein-coupled receptor (GPCR) complex based on experimental double mutant cycle data: MT7 snake toxin bound to dimeric hM1 muscarinic receptor.". J Biol Chem. 286 (36): 31661–75. doi:10.1074/jbc.M111.261404. PMC 3173127. PMID 21685390.
^ Saier MH, Yen MR, Noto K, Tamang DG, Elkan C (January 2009). "The Transporter Classification Database: recent advances". Nucleic Acids Res. 37 (Database issue): D274–8. doi:10.1093/nar/gkn862. PMC 2686586. PMID 19022853.
^ http://academic.brooklyn.cuny.edu/ http://academic.brooklyn.cuny.edu/biology/bio4fv/page/integra.htm |url= missing title (help). Retrieved 29 January 2015.

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English Journal

Terpinen-4-ol Induces Apoptosis in Human Nonsmall Cell Lung Cancer In Vitro and In Vivo.

Wu CS, Chen YJ, Chen JJ, Shieh JJ, Huang CH, Lin PS, Chang GC, Chang JT, Lin CC.SourceDepartment of Dermatology, School of Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung 80708, Taiwan.
Evidence-based complementary and alternative medicine : eCAM.Evid Based Complement Alternat Med.2012;2012:818261. Epub 2011 Jun 20.
Terpinen-4-ol, a monoterpene component of the essential oils of several aromatic plants, exhibits antitumor effects. In this study, the antitumor effects of terpinen-4-ol and the cellular and molecular mechanisms responsible for it were evaluated and studied, respectively on human nonsmall cell lung
PMID 21760828

Expression of nestin, mesothelin and epithelial membrane antigen (EMA) in developing and adult human meninges and meningiomas.

Petricevic J, Forempoher G, Ostojic L, Mardesic-Brakus S, Andjelinovic S, Vukojevic K, Saraga-Babic M.SourceDepartment of Pathology, Cytology and Forensic Medicine, University Clinical Hospital Mostar, Kralja Tvrtka bb, 88000 Mostar, Bosnia and Herzegovina; Department of Histology and Embryology, School of Medicine, University of Mostar, Bijeli brijeg bb, 88000 Mostar, Bosnia and Herzegovina.
Acta histochemica.Acta Histochem.2011 Nov;113(7):703-11. Epub 2010 Oct 12.
The spatial and temporal pattern of appearance of nestin, epithelial membrane antigen (EMA) and mesothelin proteins was immunohistochemically determined in the cells of normal developing and adult human meninges and meningiomas. Human meninges developed as two mesenchymal condensations in the head r
PMID 20943257

Japanese Journal

One-step direct reconstitution of biomembranes onto cationic organic polymer bead supports.

Osei-Asante Samuel,Haratake Mamoru,Fuchigami Takeshi,Nakayama Morio
Journal of colloid and interface science 351(1), 96-101, 2010-11-01
… The RBC membrane-bead complex was obtained by the incubation of white, unsealed rat RBC ghost membranes with a nonporous quaternary ammonium-type anion-exchange polymer bead with a 350-550 microm diameter. … Confocal microscopic observations using a fluorescence membrane probe revealed that the RBC membranes were reconstituted on the outer surface of the bead without any remarkable structural gaps in the membrane. …
NAID 120002400753

Generation of single-chain Fvs against detergent-solubilized recombinant antigens with a simple coating procedure(METHODS)

Tanaka Torahiko,Hasegawa Yuichiro,Saito Makoto,Ikeda Masanori,Kato Nobuyuki
Journal of bioscience and bioengineering 110(3), 374-376, 2010-09
… We present here a simple procedure to coat detergent-solubilized antigen for subsequent panning selection of single-chain Fv (scFv), the target antigen of which was the hepatitis C virus (HCV) non-structural protein (NS)4B, an integral membrane protein. …
NAID 110007730034

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★リンクテーブル★

リンク元	「membrane-associated protein」「surface protein」「内在性膜タンパク質」「cell surface protein」「cell membrane protein」
関連記事	「integral」「membrane」