F13B

F13B

Coagulation factor XIII, B polypeptide, also known as F13B, is a human gene.

PBB_Summary
section_title =
summary_text = This gene encodes coagulation factor XIII B subunit. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as a plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon activation by the cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion.cite web | title = Entrez Gene: F13B coagulation factor XIII, B polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2165| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Muszbek L, Adány R, Mikkola H |title=Novel aspects of blood coagulation factor XIII. I. Structure, distribution, activation, and function. |journal=Critical reviews in clinical laboratory sciences |volume=33 |issue= 5 |pages= 357–421 |year= 1997 |pmid= 8922891 |doi=
*cite journal | author=Murdock PJ, Owens DL, Chitolie A, "et al." |title=Development and evaluation of ELISAs for factor XIIIA and XIIIB subunits in plasma. |journal=Thromb. Res. |volume=67 |issue= 1 |pages= 73–9 |year= 1992 |pmid= 1359667 |doi=
*cite journal | author=Nishimura DY, Leysens NJ, Murray JC |title=A dinucleotide repeat for the D1S53 locus. |journal=Nucleic Acids Res. |volume=20 |issue= 5 |pages= 1167 |year= 1992 |pmid= 1549502 |doi=
*cite journal | author=Bottenus RE, Ichinose A, Davie EW |title=Nucleotide sequence of the gene for the b subunit of human factor XIII. |journal=Biochemistry |volume=29 |issue= 51 |pages= 11195–209 |year= 1991 |pmid= 2271707 |doi=
*cite journal | author=Saito M, Asakura H, Yoshida T, "et al." |title=A familial factor XIII subunit B deficiency. |journal=Br. J. Haematol. |volume=74 |issue= 3 |pages= 290–4 |year= 1990 |pmid= 2334637 |doi=
*cite journal | author=Grundmann U, Nerlich C, Rein T, Zettlmeissl G |title=Complete cDNA sequence encoding the B subunit of human factor XIII. |journal=Nucleic Acids Res. |volume=18 |issue= 9 |pages= 2817–8 |year= 1990 |pmid= 2339067 |doi=
*cite journal | author=Greenberg CS, Dobson JV, Miraglia CC |title=Regulation of plasma factor XIII binding to fibrin in vitro. |journal=Blood |volume=66 |issue= 5 |pages= 1028–34 |year= 1985 |pmid= 2413926 |doi=
*cite journal | author=Carrell NA, Erickson HP, McDonagh J |title=Electron microscopy and hydrodynamic properties of factor XIII subunits. |journal=J. Biol. Chem. |volume=264 |issue= 1 |pages= 551–6 |year= 1989 |pmid= 2491853 |doi=
*cite journal | author=Webb GC, Coggan M, Ichinose A, Board PG |title=Localization of the coagulation factor XIII B subunit gene (F13B) to chromosome bands 1q31-32.1 and restriction fragment length polymorphism at the locus. |journal=Hum. Genet. |volume=81 |issue= 2 |pages= 157–60 |year= 1989 |pmid= 2563250 |doi=
*cite journal | author=Grundmann U, Amann E, Zettlmeissl G, Küpper HA |title=Characterization of cDNA coding for human factor XIIIa. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 21 |pages= 8024–8 |year= 1986 |pmid= 2877457 |doi=
*cite journal | author=Ichinose A, McMullen BA, Fujikawa K, Davie EW |title=Amino acid sequence of the b subunit of human factor XIII, a protein composed of ten repetitive segments. |journal=Biochemistry |volume=25 |issue= 16 |pages= 4633–8 |year= 1986 |pmid= 3021194 |doi=
*cite journal | author=Bender K, Bissbort S, Klein A, "et al." |title=Coagulation factor XIII: genetic linkage studies with F13B. |journal=Genet. Epidemiol. |volume=4 |issue= 1 |pages= 43–9 |year= 1987 |pmid= 3471677 |doi= 10.1002/gepi.1370040106
*cite journal | author=Kaczmarek E, Liu Y, Berse B, "et al." |title=Biosynthesis of plasma factor XIII: evidence for transcription and translation in hepatoma cells. |journal=Biochim. Biophys. Acta |volume=1247 |issue= 1 |pages= 127–34 |year= 1995 |pmid= 7873582 |doi=
*cite journal | author=Hashiguchi T, Saito M, Morishita E, "et al." |title=Two genetic defects in a patient with complete deficiency of the b-subunit for coagulation factor XIII. |journal=Blood |volume=82 |issue= 1 |pages= 145–50 |year= 1993 |pmid= 8324218 |doi=
*cite journal | author=Radek JT, Jeong JM, Wilson J, Lorand L |title=Association of the A subunits of recombinant placental factor XIII with the native carrier B subunits from human plasma. |journal=Biochemistry |volume=32 |issue= 14 |pages= 3527–34 |year= 1993 |pmid= 8466897 |doi=
*cite journal | author=Siebenlist KR, Meh DA, Mosesson MW |title=Plasma factor XIII binds specifically to fibrinogen molecules containing gamma chains. |journal=Biochemistry |volume=35 |issue= 32 |pages= 10448–53 |year= 1996 |pmid= 8756701 |doi= 10.1021/bi9606206
*cite journal | author=Kaetsu H, Hashiguchi T, Foster D, Ichinose A |title=Expression and release of the a and b subunits for human coagulation factor XIII in baby hamster kidney (BHK) cells. |journal=J. Biochem. |volume=119 |issue= 5 |pages= 961–9 |year= 1997 |pmid= 8797098 |doi=
*cite journal | author=Sugimura D, Fukue H, Arai M, "et al." |title= [Changes of factor XIII a and b subunit in patients with disseminated intravascular coagulation syndrome] |journal=Rinsho Byori |volume=44 |issue= 4 |pages= 355–61 |year= 1996 |pmid= 8847818 |doi=
*cite journal | author=Achyuthan KE, Rowland TC, Birckbichler PJ, "et al." |title=Hierarchies in the binding of human factor XIII, factor XIIIa, and endothelial cell transglutaminase to human plasma fibrinogen, fibrin, and fibronectin. |journal=Mol. Cell. Biochem. |volume=162 |issue= 1 |pages= 43–9 |year= 1997 |pmid= 8905624 |doi=

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужен реферат?

Look at other dictionaries:

  • Transglutaminase — Transglutaminases are a family of enzymes (EC 2.3.2.13) that catalyze the formation of a covalent bond between a free amine group (e.g., protein or peptide bound lysine) and the gamma carboxamid group of protein or peptide bound glutamine. Bonds… …   Wikipedia

  • Factor XIII — protein Name = coagulation factor XIII, A1 polypeptide caption = width = HGNCid = 3531 Symbol = F13A1 AltSymbols = F13A EntrezGene = 2162 OMIM = 134570 RefSeq = NM 000129 UniProt = P00488 PDB = ECnumber = Chromosome = 6 Arm = p Band = 24… …   Wikipedia

  • Factor XIII — Fibrinstabilisierender Faktor Schema der Vernetzung durch Faktor XIII …   Deutsch Wikipedia

  • Faktor XIII — Fibrinstabilisierender Faktor Schema der Vernetzung durch Faktor XIII …   Deutsch Wikipedia

  • Fibrin-Stabilisierender Faktor — Fibrinstabilisierender Faktor Schema der Vernetzung durch Faktor XIII …   Deutsch Wikipedia

  • Fibrinstabilisierender Faktor — Bänder /Oberflächenmodell des Dimer der A Kette von …   Deutsch Wikipedia

  • Gerinnungsfaktor XIII — Fibrinstabilisierender Faktor Schema der Vernetzung durch Faktor XIII …   Deutsch Wikipedia

  • Laki-Lorand-Faktor — Fibrinstabilisierender Faktor Schema der Vernetzung durch Faktor XIII …   Deutsch Wikipedia

  • Coagulation factor XIII, A1 polypeptide — PDB rendering based on 1evu …   Wikipedia

  • Transglutaminase — La transglutaminase est une enzyme (EC 2.3.2.13) qui catalyse la formation de liaisons covalentes entre des groupements amines libres (ex. : lysines) et le groupement gamma carboxamide des glutamines. Les liaisons formées par la… …   Wikipédia en Français

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”