pmc logo image
Logo of jclinpathJournal of Clinical PathologyCurrent TOCInstructions for authors
Journal List > J Clin Pathol > v.33(5); May 1980

Formats:
J Clin Pathol. 1980 May; 33(5): 434–437.
PMCID: PMC1146106
Copyright notice
Fibrin cross-linking in congenital factor XIII deficiency.
F Rodeghiero and T Barbui
Abstract
Homozygous patients with factor XIII deficiency are devoid of immunologically identifiable A protein, the active enzymatic component. Quantitative studies of transamidase activity of the factor are available in only a few cases, and the fibrin cross-linking pattern is not well known. The present paper deals with the quantitative estimation of factor XIII transamidase activity (dansylcadaverine system), factor XIII molecular subunits, and the corresponding fibrin cross-linking pattern in seven homozygous patients with factor XIII deficiency. The results indicate that transamidase activity was present in all patients, and the range was 0.5-1.7%. The pattern of fibrin stabiisation showed an absence of cross-linking in two patients, the presence of gamma-gamma-dimers (traces) in four, and gamma-gamma-dimers plus incomplete alpha-polymers (traces) in one patient. In conclusion, the homozygous patients reported here were not completely devoid of functioning factor XIII.
Full text
Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (801K), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.
 
icon of scanned page 434
434
icon of scanned page 435
435
icon of scanned page 436
436
icon of scanned page 437
437
 
Images in this article
p436-a
p436-a

p436-a
on p.436
Click on the image to see a larger version.
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
  • LORAND L, KONISHI K. ACTIVATION OF THE FIBRIN STABILIZING FACTOR OF PLASMA BY THROMBIN. Arch Biochem Biophys. 1964 Apr;105:58–67. [PubMed]
  • Pisano JJ, Finlayson JS, Peyton MP. [Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine.]. Science. 1968 May 24;160(830):892–893. [PubMed]
  • Bohn H, Haupt H, Kranz T. Die molekulare Struktur der fibrinstabilisierteenden Faktoren des Menschen. Blut. 1972 Oct;25(4):235–248. [PubMed]
  • Lorand L, Gray AJ, Brown K, Credo RB, Curtis CG, Domanik RA, Stenberg P. Dissociation of the subunit structure of fibrin stabilizing factor during activation of the zymogen. Biochem Biophys Res Commun. 1974 Feb 27;56(4):914–922. [PubMed]
  • Bohn H, Becker W, Trobisch H. Die molekulare Struktur der fibrinstablisierenden Faktoren des Menschen. II. Vergleichennde immunologische Untersuchungen von Faktor-XIII-Mangelplasmen und Normalplasma. Blut. 1973 May;26(5):303–311. [PubMed]
  • Israels ED, Paraskevas F, Israels LG. Immunological studies of coagulation factor XIII. J Clin Invest. 1973 Oct;52(10):2398–2403. [PubMed]
  • Barbui T, Cartei G, Chisesi T, Dini E. Electroimmunoassay of plasma subunits-a and -s in a case of congenital fibrin stabilizing factor deficiency. Thromb Diath Haemorrh. 1974 Sep 30;32(1):124–131. [PubMed]
  • Barbui T, Rodeghiero F, Dini E, Mariani G, Paa ML, De Biasi R, Murillo RC, Umana CM. Subunits A and S inheritance in four families with congenital factor XIII deficiency. Br J Haematol. 1978 Feb;38(2):267–271. [PubMed]
  • Duckert F. Documentation of the plasma factor XIII deficiency in man. Ann N Y Acad Sci. 1972 Dec 8;202:190–199. [PubMed]
  • Ikkala E. Transfusion therapy in congenital deficiencies of plasma factor XIII. Ann N Y Acad Sci. 1972 Dec 8;202:200–203. [PubMed]
  • Pisano JJ, Finlayson JS, Peyton MP, Nagai Y. Epsilon-(gamma glutamyl) lysine in fibrin: lack of crosslink formation in Factor 13 deficiency. Proc Natl Acad Sci U S A. 1971 Apr;68(4):770–772. [PubMed]
  • Duckert F. Importance physiologique du facteur stabilisant la fibrine (facteur XIII). Schweiz Med Wochenschr. 1974 Sep 28;104(39):1342–1347. [PubMed]
  • McDonagh J, McDonagh RP, Myllylä G, Ikkala E. Factor XIII deficiency: a genetic study of two affected kindreds in Finland. Blood. 1974 Mar;43(3):327–332. [PubMed]
  • Lorand L, Urayama T, De Kiewiet JW, Nossel HL. Diagnostic and genetic studies on fibrin-stabilizing factor with a new assay based on amine incorporation. J Clin Invest. 1969 Jun;48(6):1054–1064. [PubMed]
  • Laurell CB. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem. 1966 Apr;15(1):45–52. [PubMed]
  • Laurell CB. Electroimmuno assay. Scand J Clin Lab Invest Suppl. 1972;124:21–37. [PubMed]
  • Weber K, Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed]
  • Finlayson JS, Morton RO. Gel electrophoresis for assessing fibrin crosslinking: a precaution. Clin Chim Acta. 1972 Jan;36(1):254–256. [PubMed]
  • Chung SI. Comparative studies on tissue transglutaminase and factor XIII. Ann N Y Acad Sci. 1972 Dec 8;202:240–255. [PubMed]
  • Miloszewski K, Losowsky MS. The half-life of factor XIII in vivo. Br J Haematol. 1970 Dec;19(6):685–690. [PubMed]
Articles from Journal of Clinical Pathology are provided here courtesy of
BMJ Group

PubMed articles by these authors