Ljudski serumski albumin

blood albumin
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1AO6, 1BJ5, 1BKE, 1BM0, 1E78, 1E7A, 1E7B, 1E7C, 1E7E, 1E7F, 1E7G, 1E7H, 1E7I, 1GNI, 1GNJ, 1H9Z, 1HA2, 1HK1, 1HK2, 1HK3, 1HK4, 1HK5, 1N5U, 1O9X, 1TF0, 1UOR, 1YSX, 2BX8, 2BXA, 2BXB, 2BXC, 2BXD, 2BXF, 2BXG, 2BXH, 2BXI, 2BXK, 2BXL, 2BXM, 2BXN, 2BXO, 2BXP, 2BXQ, 2I2Z, 2I30, 2VDB, 2VUE, 2VUF, 2XSI, 2XVQ, 2XVU, 2XVV, 2XVW, 2XW0, 2XW1, 2YDF, 3A73, 3B9L, 3B9M, 3CX9, 3JQZ, 3JRY, 3LU6, 3LU7, 3LU8, 3SQJ, 3TDL, 3UIV, 4E99, 4EMX, 4G03, 4G04, 4HGK, 4HGM, 4IW1, 4IW2, 4K2C, 4L8U, 4L9K, 4L9Q, 4LA0, 4LB9, 4LB2, 2N0X, 2ESG, 4S1Y, 4N0F, 4Z69, 4N0U, 4K71, 2BXE, 4BKE, 5IJF, 5ID7, 5IFO, 5FUO
Identifikatori
Aliasi	ALB
Vanjski ID-jevi	OMIM: 103600 MGI: 87991 HomoloGene: 405 GeneCards: ALB
Lokacija gena (čovjek)
Hrom.	Hromosom 4 (čovjek)
Kraj	73,421,482 bp
Lokacija gena (miš)
Hrom.	Hromosom 5 (miš)
Kraj	90,624,461 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• vezivanje sa DNK; • oxygen binding; • chaperone binding; • vezivanje iona metala; • antioxidant activity; • GO:0001948, GO:0016582 vezivanje za proteine; • vezivanje identičnih proteina; • pyridoxal phosphate binding; • copper ion binding; • lipid binding; • toxic substance binding; • fatty acid binding; • exogenous protein binding;
Ćelijska komponenta	• citoplazma; • Golđijev aparat; • blood microparticle; • myelin sheath; • extracellular region; • Endoplazmatski retikulum; • Egzosom; • platelet alpha granule lumen; • jedro; • Vanćelijsko; • endoplasmic reticulum lumen; • GO:0009327 makromolekulani kompleks;
Biološki proces	• sodium-independent organic anion transport; • hemolysis by symbiont of host erythrocytes; • cellular response to starvation; • platelet degranulation; • negative regulation of apoptotic process; • receptor-mediated endocytosis; • maintenance of mitochondrion location; • retina homeostasis; • bile acid and bile salt transport; • negative regulation of programmed cell death; • cellular oxidant detoxification; • high-density lipoprotein particle remodeling; • Posttranslacione modifikacije; • GO:0015915 transport; • negative regulation of protein oligomerization;
	Izvori:Amigo / QuickGO
Ortolozi
	213
	11657
	ENSG00000163631
	ENSMUSG00000029368
	P02768
	P07724
	NM_000477
	NM_009654
	NP_000468
	NP_033784
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Ljudski serumski albumin je serumski albumin pronađen u ljudskoj krvi. To je najzastupljeniji protein u ljudskoj krvnoj plazmi; čini otprilike polovinu serumskih proteina. Proizvodi se u jetri. Rastvorljiv je u vodi, u monomernom obliku.

Albumin prenosi hormone, masne kiseline i druge spojeve, puferuje pH i održava onkotski pritisak, između ostalih funkcija.

Albumin se sintetizira u jetri kao preproalbumin, koji ima N-terminalni peptid koji se uklanja prije nego što se nastali protein oslobodi iz grubog endoplazmatskog retikuluma. Proizvod, proalbumin, se zauzvrat cijepa u Golgijevom aparatu kako bi se proizveo izlučeni albumin.

Referentni raspon za koncentracije albumina u serumu je približno 35–50 g/L (3,5–5,0 g/dL).^[5] It has a serum half-life of approximately 21 days.^[6] It has a molecular mass of 66.5 kDa.

Gen za albumin nalazi se na hromosomu 4 u lokusu 4q13.3 i mutacije ovog gena mogu dovesti do anomalnih proteina. Gen za ljudski albumin je dugačak 16.961 nukleotida od pretpostavljenog 'kap' mjesta do prvog poli(A) adicijskog mjesta. Podijeljen je na 15 egzona koji su simetrično raspoređeni unutar 3 domena za koje se smatra da su nastali triplikacijom jednog primordijalnog domena.

Ljudski serumski albumin (HSA) je visoko topiv u vodi kao plazmatski globulasti monomerni protein s relativnom molekulskom težinom od 67 KDa, koji se sastoji od 585 aminokiselinskih ostataka, jedne sulfhidrilne grupe i 17disulfidnih mostova. Među nosačima nanočestica, HSA nanočestice su dugo bile u centru pažnje u farmaceutskoj industriji zbog svoje sposobnosti da se vežu za različite molekule lijekova, velike stabilnosti tokom skladištenja i upotrebe in vivo, bez toksičnosti i antigenosti, a biorazgradljivost, reproducibilnosti, povećanje proizvodnog procesa i bolja kontrola nad svojstvima oslobađanja. Osim toga, značajne količine lijeka mogu se ugraditi u matriks čestica zbog velikog broja vezivnih mjesta na molekuli albumina.^[7]

Funkcija

Održava onkotski pritisak
Prenosi hormon štitnjače
Prenosi druge hormone, posebno one koji su rastvorljivi u mastima
Prenosi masne kiseline ("slobodne" masne kiseline) do jetre i do miocita radi iskorištavanja energije
Prenosi nekonjugirani bilirubin
Prenosii mnoge lijekove; nivoi albumina u serumu mogu uticati na poluvrijeme eliminacije lijekova. Konkurencija između lijekova za mjesta vezanja albumina može uzrokovati interakciju lijekova povećanjem slobodne frakcije jednog od lijekova, čime se utiče na potenciju.
Kompetitivno vezuje kalcijeve ione (Ca²⁺)
Serumski albumin, kao negativan protein akutne faze, je smanjen u upalnim stanjima. Kao takav, nije validan marker nutritivnog statusa; već je to marker upalnog stanja
Sprečava fotodegradaciju folne kiseline
Sprečava patogene efekte infekcija toksinima Clostridioides difficile ^[8]

Interakcije

Pokazalo se da humani serumski albumin Reaguje sa FCGRT.^[9]

Također može stupiti u interakciju sa još neidentificiranim albondin (gp60), određenim parom gp18/gp30 i nekim drugim proteinima, kao što su osteonektin, hnRNPs, kalretikulin , cubilin i megalin.^[10]

Također pogledajte

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000163631 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000029368 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Harmonisation of Reference Intervals" (PDF). pathologyharmony.co.uk. Pathology Harmony. Arhivirano s originala (PDF), 2. 8. 2013. Pristupljeno 23. 6. 2013.
^ "Hypoalbuminemia: Background, Pathophysiology, Etiology". Medscape Reference. 10. 11. 2019. Pristupljeno 22. 12. 2019.
^ Kouchakzadeh H, Shojaosadati SA, Shokri F (septembar 2014). "Efficient loading and entrapment of tamoxifen in human serum albumin based nanoparticulate delivery system by a modified desolvation technique". Chemical Engineering Research and Design. 92 (9): 1681–1692. doi:10.1016/j.cherd.2013.11.024.
^ di Masi A, Leboffe L, Polticelli F, Tonon F, Zennaro C, Caterino M, et al. (septembar 2018). "Human Serum Albumin Is an Essential Component of the Host Defense Mechanism Against Clostridium difficile Intoxication". The Journal of Infectious Diseases. 218 (9): 1424–1435. doi:10.1093/infdis/jiy338. PMID 29868851.
^ Chaudhury C, Mehnaz S, Robinson JM, Hayton WL, Pearl DK, Roopenian DC, Anderson CL (februar 2003). "The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan". The Journal of Experimental Medicine. 197 (3): 315–322. doi:10.1084/jem.20021829. PMC 2193842. PMID 12566415.
^ Merlot AM, Kalinowski DS, Richardson DR (2014). "Unraveling the mysteries of serum albumin-more than just a serum protein". Frontiers in Physiology. 5: 299. doi:10.3389/fphys.2014.00299. PMC 4129365. PMID 25161624.

Dopunska literatura

Komatsu T, Nakagawa A, Curry S, Tsuchida E, Murata K, Nakamura N, Ohno H (septembar 2009). "The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O(2) and CO binding to iron protoporphyrin IX". Organic & Biomolecular Chemistry. 7 (18): 3836–3841. doi:10.1039/b909794e. PMID 19707690.
Milojevic J, Raditsis A, Melacini G (novembar 2009). "Human serum albumin inhibits Abeta fibrillization through a "monomer-competitor" mechanism". Biophysical Journal. 97 (9): 2585–2594. Bibcode:2009BpJ....97.2585M. doi:10.1016/j.bpj.2009.08.028. PMC 2770600. PMID 19883602.
Silva AM, Hider RC (oktobar 2009). "Influence of non-enzymatic post-translation modifications on the ability of human serum albumin to bind iron. Implications for non-transferrin-bound iron speciation". Biochimica et Biophysica Acta. 1794 (10): 1449–1458. doi:10.1016/j.bbapap.2009.06.003. PMID 19505594.
Otosu T, Nishimoto E, Yamashita S (februar 2010). "Multiple conformational state of human serum albumin around single tryptophan residue at various pH revealed by time-resolved fluorescence spectroscopy". Journal of Biochemistry. 147 (2): 191–200. doi:10.1093/jb/mvp175. PMID 19884191.
Blindauer CA, Harvey I, Bunyan KE, Stewart AJ, Sleep D, Harrison DJ, et al. (august 2009). "Structure, properties, and engineering of the major zinc binding site on human albumin". The Journal of Biological Chemistry. 284 (34): 23116–23124. doi:10.1074/jbc.M109.003459. PMC 2755717. PMID 19520864.
Juárez J, López SG, Cambón A, Taboada P, Mosquera V (juli 2009). "Influence of electrostatic interactions on the fibrillation process of human serum albumin". The Journal of Physical Chemistry B. 113 (30): 10521–10529. doi:10.1021/jp902224d. PMID 19572666.
Fu BL, Guo ZJ, Tian JW, Liu ZQ, Cao W (august 2009). "[Advanced glycation end products induce expression of PAI-1 in cultured human proximal tubular epithelial cells through NADPH oxidase dependent pathway]". Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi = Chinese Journal of Cellular and Molecular Immunology. 25 (8): 674–677. PMID 19664386.
Ascenzi P, di Masi A, Coletta M, Ciaccio C, Fanali G, Nicoletti FP, et al. (novembar 2009). "Ibuprofen impairs allosterically peroxynitrite isomerization by ferric human serum heme-albumin". The Journal of Biological Chemistry. 284 (45): 31006–31017. doi:10.1074/jbc.M109.010736. PMC 2781501. PMID 19734142.
Sowa ME, Bennett EJ, Gygi SP, Harper JW (juli 2009). "Defining the human deubiquitinating enzyme interaction landscape". Cell. 138 (2): 389–403. doi:10.1016/j.cell.2009.04.042. PMC 2716422. PMID 19615732.
Curry S (august 2002). "Beyond expansion: structural studies on the transport roles of human serum albumin". Vox Sanguinis. 83 (Suppl 1): 315–319. doi:10.1111/j.1423-0410.2002.tb05326.x. PMID 12617161. S2CID 44482133.
Guo S, Shi X, Yang F, Chen L, Meehan EJ, Bian C, Huang M (septembar 2009). "Structural basis of transport of lysophospholipids by human serum albumin". The Biochemical Journal. 423 (1): 23–30. doi:10.1042/BJ20090913. PMID 19601929.
de Jong PE, Gansevoort RT (2009). "Focus on microalbuminuria to improve cardiac and renal protection". Nephron Clinical Practice. 111 (3): c204-10, discussion c211. doi:10.1159/000201568. PMID 19212124.
Page TA, Kraut ND, Page PM, Baker GA, Bright FV (septembar 2009). "Dynamics of loop 1 of domain I in human serum albumin when dissolved in ionic liquids". The Journal of Physical Chemistry B. 113 (38): 12825–12830. doi:10.1021/jp904475v. PMID 19711930.
Roche M, Rondeau P, Singh NR, Tarnus E, Bourdon E (juni 2008). "The antioxidant properties of serum albumin". FEBS Letters. 582 (13): 1783–1787. doi:10.1016/j.febslet.2008.04.057. PMID 18474236. S2CID 5364683.
Wyatt AR, Wilson MR (februar 2010). "Identification of human plasma proteins as major clients for the extracellular chaperone clusterin". The Journal of Biological Chemistry. 285 (6): 3532–3539. doi:10.1074/jbc.M109.079566. PMC 2823492. PMID 19996109.
Cui FL, Yan YH, Zhang QZ, Qu GR, Du J, Yao XJ (februar 2010). "A study on the interaction between 5-Methyluridine and human serum albumin using fluorescence quenching method and molecular modeling". Journal of Molecular Modeling. 16 (2): 255–262. doi:10.1007/s00894-009-0548-4. PMID 19588173. S2CID 9042021.
Caridi G, Dagnino M, Simundic AM, Miler M, Stancic V, Campagnoli M, et al. (mart 2010). "Albumin Benkovac (c.1175 A > G; p.Glu392Gly): a novel genetic variant of human serum albumin". Translational Research. 155 (3): 118–119. doi:10.1016/j.trsl.2009.10.001. PMID 20171595.
Deeb O, Rosales-Hernández MC, Gómez-Castro C, Garduño-Juárez R, Correa-Basurto J (februar 2010). "Exploration of human serum albumin binding sites by docking and molecular dynamics flexible ligand-protein interactions". Biopolymers. 93 (2): 161–170. doi:10.1002/bip.21314. PMID 19785033.
Karahan SC, Koramaz I, Altun G, Uçar U, Topbaş M, Menteşe A, Kopuz M (2010). "Ischemia-modified albumin reduction after coronary bypass surgery is associated with the cardioprotective efficacy of cold-blood cardioplegia enriched with N-acetylcysteine: a preliminary study". European Surgical Research. 44 (1): 30–36. doi:10.1159/000262324. PMID 19955769. S2CID 26699371.
Jin C, Lu L, Zhang RY, Zhang Q, Ding FH, Chen QJ, Shen WF (oktobar 2009). "Association of serum glycated albumin, C-reactive protein and ICAM-1 levels with diffuse coronary artery disease in patients with type 2 diabetes mellitus". Clinica Chimica Acta; International Journal of Clinical Chemistry. 408 (1–2): 45–49. doi:10.1016/j.cca.2009.07.003. PMID 19615354.

Vanjski linkovi

Human Albumin structure in the Protein data bank
Human Serum Albumin Arhivirano 24. 4. 2006. na Wayback Machine on the Human Protein Reference Database Arhivirano 24. 4. 2006. na Wayback Machine
Albumin binding prediction
Albumin at Lab Tests Online
Albumin: analyte monograph from the Association for Clinical Biochemistry and Laboratory Medicine
P02768

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000163631 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000029368 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[Pathology_Harmony-5] "Harmonisation of Reference Intervals" (PDF). pathologyharmony.co.uk. Pathology Harmony. Arhivirano s originala (PDF), 2. 8. 2013. Pristupljeno 23. 6. 2013.

[Medscape_Reference_2019-6] "Hypoalbuminemia: Background, Pathophysiology, Etiology". Medscape Reference. 10. 11. 2019. Pristupljeno 22. 12. 2019.

[7] Kouchakzadeh H, Shojaosadati SA, Shokri F (septembar 2014). "Efficient loading and entrapment of tamoxifen in human serum albumin based nanoparticulate delivery system by a modified desolvation technique". Chemical Engineering Research and Design. 92 (9): 1681–1692. doi:10.1016/j.cherd.2013.11.024.

[8] Masi A, Leboffe L, Polticelli F, Tonon F, Zennaro C, Caterino M, et al. (septembar 2018). "Human Serum Albumin Is an Essential Component of the Host Defense Mechanism Against Clostridium difficile Intoxication". The Journal of Infectious Diseases. 218 (9): 1424–1435. doi:10.1093/infdis/jiy338. PMID 29868851.

[pmid12566415-9] Chaudhury C, Mehnaz S, Robinson JM, Hayton WL, Pearl DK, Roopenian DC, Anderson CL (februar 2003). "The major histocompatibility complex-related Fc receptor for IgG (FcRn) binds albumin and prolongs its lifespan". The Journal of Experimental Medicine. 197 (3): 315–322. doi:10.1084/jem.20021829. PMC 2193842. PMID 12566415.

[10] Merlot AM, Kalinowski DS, Richardson DR (2014). "Unraveling the mysteries of serum albumin-more than just a serum protein". Frontiers in Physiology. 5: 299. doi:10.3389/fphys.2014.00299. PMC 4129365. PMID 25161624.

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