Electron microscopy and hydrodynamic properties of factor XIII subunits - PubMed (original) (raw)
. 1989 Jan 5;264(1):551-6.
Affiliations
- PMID: 2491853
Free article
Electron microscopy and hydrodynamic properties of factor XIII subunits
N A Carrell et al. J Biol Chem. 1989.
Free article
Abstract
Factor XIII is a transglutaminase important in blood coagulation and fibrinolysis. Its function is to catalyze peptide bond formation between the gamma-carboxamide group of glutamines in one protein and the epsilon-amino group of lysine in another. There are two zymogenic forms of factor XIII: one is a noncovalent, intracellular dimer (A2); the other is a noncovalent, extracellular tetramer (A2B2). The catalytic function resides in the activated A chain (A2.). Purified forms of factor XIII (A2B2, A2, A2.B2, B) were prepared and analyzed by electron microscopy, gel filtration, and gradient centrifugation. Hydrodynamic constants were derived. Electron microscopy of rotary-shadowed molecules showed A2 to consist of two globular particles each about 6 x 9 nm in size. The A2 dimer is significantly elongated, 18 nm long and 6 nm in diameter. Sedimentation and gel filtration of the A2 dimer are consistent with this asymmetric structure. B protein is a filamentous, flexible strand with kinks, with a contour length of 30 nm and a diameter of approximately 2-3 nm. The sedimentation and gel filtration behavior of the B subunit are characteristic of a highly asymmetric molecule. The observed structure of the B subunit, combined with data for its amino acid sequence, suggests a modular structure. The B subunit is a member of a family of proteins composed of tandem, repeating structures (referred to as GP-I domains); the structure seen by electron microscopy for B subunit is probably applicable to all proteins in this family. Plasma and platelet factor XIII zymogens are tetrameric and dimeric, but B protein, in the absence of A protein, appears to be monomeric. Our model for the A2B2 zymogen has the elongated A2 dimer forming the core and the two B strands wrapping around the outside.
Similar articles
- Factor XIII topology: organization of B subunits and changes with activation studied with single-molecule atomic force microscopy.
Protopopova AD, Ramirez A, Klinov DV, Litvinov RI, Weisel JW. Protopopova AD, et al. J Thromb Haemost. 2019 May;17(5):737-748. doi: 10.1111/jth.14412. Epub 2019 Mar 14. J Thromb Haemost. 2019. PMID: 30773828 Free PMC article. - Resistance of factor XIII to degradation or activation by plasmin.
Rider DM, McDonagh J. Rider DM, et al. Biochim Biophys Acta. 1981 Jul;675(2):171-7. doi: 10.1016/0304-4165(81)90223-3. Biochim Biophys Acta. 1981. PMID: 6456019 - Novel aspects of blood coagulation factor XIII. I. Structure, distribution, activation, and function.
Muszbek L, Adány R, Mikkola H. Muszbek L, et al. Crit Rev Clin Lab Sci. 1996;33(5):357-421. doi: 10.3109/10408369609084691. Crit Rev Clin Lab Sci. 1996. PMID: 8922891 Review. - Physiopathology and regulation of factor XIII.
Ichinose A. Ichinose A. Thromb Haemost. 2001 Jul;86(1):57-65. Thromb Haemost. 2001. PMID: 11487042 Review.
Cited by
- Phenotype and genotype of FXIII deficiency in two unrelated probands: identification of a novel F13A1 large deletion mediated by complex rearrangement.
Ma S, Chen C, Liang Q, Wu X, Wang X, Wu W, Liu Y, Ding Q. Ma S, et al. Orphanet J Rare Dis. 2019 Jul 24;14(1):182. doi: 10.1186/s13023-019-1144-z. Orphanet J Rare Dis. 2019. PMID: 31340840 Free PMC article. - Factor XIII topology: organization of B subunits and changes with activation studied with single-molecule atomic force microscopy.
Protopopova AD, Ramirez A, Klinov DV, Litvinov RI, Weisel JW. Protopopova AD, et al. J Thromb Haemost. 2019 May;17(5):737-748. doi: 10.1111/jth.14412. Epub 2019 Mar 14. J Thromb Haemost. 2019. PMID: 30773828 Free PMC article. - Fibroblast migration in fibrin gel matrices.
Brown LF, Lanir N, McDonagh J, Tognazzi K, Dvorak AM, Dvorak HF. Brown LF, et al. Am J Pathol. 1993 Jan;142(1):273-83. Am J Pathol. 1993. PMID: 8424460 Free PMC article. - Plasma factor XIII activity in patients with disseminated intravascular coagulation.
Song JW, Choi JR, Song KS, Rhee JH. Song JW, et al. Yonsei Med J. 2006 Apr 30;47(2):196-200. doi: 10.3349/ymj.2006.47.2.196. Yonsei Med J. 2006. PMID: 16642548 Free PMC article. - Molecular and cellular basis of deficiency of the b subunit for factor XIII secondary to a Cys430-Phe mutation in the seventh Sushi domain.
Hashiguchi T, Ichinose A. Hashiguchi T, et al. J Clin Invest. 1995 Mar;95(3):1002-8. doi: 10.1172/JCI117744. J Clin Invest. 1995. PMID: 7883947 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources