The influence of factor XIII on the fibrosing of a nerve anastomosis in the rat

Herter, Th.; Anaguostopoulos-Schleep, J.; Windmann, D

doi:10.1007/bf01856025

Cited by 3 publications

(3 citation statements)

References 43 publications

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“…In conclusion, prepara-tion A also has supramaximum levels with regard to an optimum clot cross-linking. Beyond that, Factor XIII possesses an fibrosis-promoting effect itself [11]. Hence, with the same fibrinolytic potency, the amount of fibronectin alone is probably determining.…”

Section: Discussionmentioning

confidence: 98%

“…Beyond that, Factor XIII possesses an fibrosis-promoting effect itself [11], but it may be necessary for cross-linking of fibronectin [21].…”

Section: Discussionmentioning

confidence: 99%

“…High concentrations of fibrinogen are necessary in fibrin adhesives and cannot be called in question. After studying the influence of the fibrin clot [10], aprotinin [28], thrombin [9], and Factor XIII [11], the objective of this study was to examine the effect of fibronectin on fibrosis.…”

Section: Introductionmentioning

confidence: 99%

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The influence of fibronectin on the fibrosing of a nerve anastomosis in the rat

Herter¹,

Bennefeld

1989

Res. Exp. Med.

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Although the fibrin adhesion enjoys increasing success in many areas of surgery, it has not, however, become fully established in nerve anastomosis. It was in this area particularly that significant advantages were expected, especially by the avoidance of suture granulomas. As the fibrin clot dissolved prematurely, however, and dehiscences ensued, antifibrinolytic substances had to be added to the adhesive. Fibroses occurred frequently as a result, which to date encumber nerve adhesive. We examined fibronectin for its fibrosis-inducing effect, comparing both presently available fibrin adhesive systems, because one contained up to 5 times more fibronectin per milliliter than the other. On the basis of a test grouping using 100 and 1000 KIU aprotinin/ml, we were able to establish that fibronectin in fibrin adhesives possesses a fibrosis-promoting effect.

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Section: Discussionmentioning

confidence: 98%

“…Beyond that, Factor XIII possesses an fibrosis-promoting effect itself [11], but it may be necessary for cross-linking of fibronectin [21].…”

Section: Discussionmentioning

confidence: 99%

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The influence of fibronectin on the fibrosing of a nerve anastomosis in the rat

Herter¹,

Bennefeld

1989

Res. Exp. Med.

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Factors To Be Considered in Nerve Anastomosis with Fibrin Adhesive

Herter¹,

Kreutzer

1993

Advances in Neurosurgery

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Novel Aspects of Blood Coagulation Factor XIII. I. Structure, Distribution, Activation, and Function

Muszbek

Adány

Mikkola

1996

Critical Reviews in Clinical Laboratory Sciences

189

146

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Blood coagulation factor XIII (FXIII) is a protransglutaminase that becomes activated by the concerted action of thrombin and Ca2+ in the final stage of the clotting cascade. In addition to plasma, FXIII also occurs in platelets, monocytes, and monocyte-derived macrophages. While the plasma factor is a heterotetramer consisting of paired A and B subunits (A2B2), its cellular counterpart lacks the B subunits and is a homodimer of potentially active A subunits (A2). The gene coding for the A and B subunits has been localized to chromosomes 6p24-25 and 1q31-32.1, respectively. The genomic as well as the primary protein structure of both subunits has been established, and most recently the three-dimensional structure of recombinant cellular FXIII has also been revealed. Monocytes/macrophages synthesize their own FXIII, and very likely FXIII in platelets is synthesized by the megakaryocytes. Cells of bone marrow origin seem to be the primary site for the synthesis of subunit A in plasma FXIII, but hepatocytes might also contribute. The B subunit of plasma FXIII is synthesized in the liver. Plasma FXIII circulates in association with its substrate precursor, fibrinogen. Fibrin(ogen) has an important regulatory role in the activation of plasma FXIII. The most important steps of the activation of plasma FXIII are the proteolytic removal of activation peptide by thrombin, the dissociation of subunits A and B, and the exposure of the originally buried active site on the free A subunits. The end result of this process is the formation of an active transglutaminase, which cross-links peptide chains through epsilon(gamma-glutamyl)lysyl isopeptide bonds. Cellular FXIII in platelets becomes activated through a nonproteolytic process. When intracytoplasmic Ca2+ is raised during platelet activation, the zymogen--in the absence of subunit B--assumes an active configuration. The protein substrates of activated FXIII include components of the clotting-fibrinolytic system, adhesive and contractile proteins. The main physiological function of plasma FXIII is to cross-link fibrin and protect it from the fibrinolytic plasmin. The latter effect is achieved mainly by covalently linking alpha 2 antiplasmin, the most potent physiological inhibitor of plasmin, to fibrin. Plasma FXIII seems to be involved in wound healing and tissue repair, and it is essential to maintaining pregnancy. Cellular FXIII, if exposed to the surface of the cells, might support or perhaps take over the hemostatic functions of plasma FXIII; however, its intracellular role has remained mostly unexplored.

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The influence of factor XIII on the fibrosing of a nerve anastomosis in the rat

Cited by 3 publications

References 43 publications

The influence of fibronectin on the fibrosing of a nerve anastomosis in the rat

The influence of fibronectin on the fibrosing of a nerve anastomosis in the rat

Factors To Be Considered in Nerve Anastomosis with Fibrin Adhesive

Novel Aspects of Blood Coagulation Factor XIII. I. Structure, Distribution, Activation, and Function

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