Mechanism of acute depletion of plasma fibronectin following thermal injury in rats. Appearance of a gelatinlike ligand in plasma.

Deno, D. Curtis; McCafferty, Michael H.; Saba, Thomas M.; Blumenstock, Frank A.

doi:10.1172/jci111191

Cited by 44 publications

(22 citation statements)

References 29 publications

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“…This is supported by data on the last five patients shown in Table 1 who all were found to have FN:C and in whom the mean plasma opsonic activity determined using a liver slice technique was only 7% of that of normal control plasma. Other workers have reported both a decrease in immunoreactivity and a depression of reticuloendothelial activity as a result of fibronectin's interactions with gelatin-like substances (30) and actin (31) released as a result of tissue injury. The latter may be of particular relevance as the appearance of complexes containing actin has recently been described in patients with FHF (32).…”

Section: Discussionmentioning

confidence: 95%

Characterization of the molecular forms of fibronectin in fulminant hepatic failure

Almasio¹,

Hughes²,

Williams³

1986

Hepatology

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The plasma levels of the opsonic glycoprotein fibronectin are decreased in patients with fulminant hepatic failure, which may be an important factor in their impaired host-defense. Twenty-nine patients in fulminant hepatic failure were studied on admission, and the mean fibronectin level in Grade 0-2 encephalopathy was 82 micrograms per ml (range = 0 to 150) and in Grade 3-4 encephalopathy 61 micrograms per ml (range = 5 to 158) as compared to normal controls (268 micrograms per ml, range = 178 to 380, n = 62). No fibronectin degradation products could be detected in fulminant hepatic failure plasma by sodium dodecyl sulfate-gel electrophoresis on a polyacrylamide gradient (5 to 15%) followed by immunoblotting onto nitrocellulose with detection using a rabbit antihuman fibronectin antiserum visualized with a peroxidase conjugate. The plasma levels of the marker proteolytic enzyme cathepsin D were significantly elevated in fulminant hepatic failure (120 +/- 31 mU per ml per hr) as compared to the normal controls (18 +/- 2.1 mU per ml per hr, n = 10, p less than 0.01). Cross-immunoelectrophoresis of fulminant hepatic failure plasma for fibronectin on agarose plates gave an additional slower migrating peak in 15 of the 29 patients, as well as that of fibronectin, which corresponded to the fibronectin complex reported by other workers in leukemia. An intermediate gel containing antihuman fibrinogen demonstrated fibrinogen to be one component of this complex. Binding of other substances to fibronectin will reduce its apparent biological activity and may be the result of their lack of clearance by the damaged liver.

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Section: Discussionmentioning

confidence: 95%

Characterization of the molecular forms of fibronectin in fulminant hepatic failure

Almasio¹,

Hughes²,

Williams³

1986

Hepatology

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“…Fibronectin opsonlzation is necessary for macrophage recognition and phagocytosis of particulate debris released from tissues after bum and trauma (23,41,53,58), resolution of bacteremia during sepsis (48,53), and clearance of fibrin during disseminated intravascular coagulation (9,11,60). In addition, macrophage adhesion to fibronectin-coated surfaces affects a variety of macrophage functions including chemotaxis (25,50), differentiation (8), secretion (7,45), and phagocytosis via immunologic receptors (12,52,66).…”

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confidence: 99%

Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1.

Blystone

Graham

Lindberg

et al. 1994

The Journal of Cell Biology

234

199

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Abstract. The plasma protein fibronectin is an important opsonin in wound repair and host defense. To better understand the process of fibronectin-mediated phagocytosis, we have transfectod K562 cells, which endogenously express 0~5fll, with a,f13. In these transfectants, antibodies to t~fl3 block phagocytosis of fibronectin-opsonized beads completely, even though half the ingestion occurs through endogenous 0t5/3~ receptors, c~5/31-mediated adhesion to fibronectincoated surfaces is unaffected by c~j33 ligation. Neither av/$5 nor O/M/~2 ligation affects O~5/~1 phagocytic function in transfectants expressing these receptors. Pharmacologic data suggest that o~v/~3 ligation suppresses the phagocytic competence of high affinity ot5/$1 receptors through a signal transduction pathway, perhaps involving protein kinase C. In addition to its significance for phagocytosis, otv/33 regulation of o~5/31 function may be significant for its roles in cell migration, metastasis, and angiogenesis. MACROPHAGE interaction with fibronectin (Fn) 1 is recognized as an important aspect of host defense and wound repair. Fibronectin opsonlzation is necessary for macrophage recognition and phagocytosis of particulate debris released from tissues after bum and trauma (23,41,53,58), resolution of bacteremia during sepsis (48, 53), and clearance of fibrin during disseminated intravascular coagulation (9,11,60). In addition, macrophage adhesion to fibronectin-coated surfaces affects a variety of macrophage functions including chemotaxis (25, 50), differentiation (8), secretion (7,45), and phagocytosis via immunologic receptors (12,52,66). Nonetheless, the moleculax nature of the interactions leading to these critical macrophage functions is unknown.Studies which have examined fibronectin receptors on macrophages in detail have demonstrated an unexpectedly large number of integrin and non-integrin fibronectin-binding proteins (10,13,16,17,29,42,59,63). Four integrin receptors with fibronectin binding capability have been identified on mononuclear phagocytes. Fibronectin binding to VLA-5 (ot5/~1), the vitronectin receptor (otJ~3) and the Leukocyte Response Integrin (LRI) appears dependent on the RGD adhesion sequence (13, 16, 29); (VLA-4 (~,) binds fibronectin independent of this sequence (28). Additional macrophage integrins ~J~5, VLA-3 (ot3/~,), and OtM/~2, may also Please address all correspondence to Dr. Eric J. Brown, Infectious Diseases, Campus Box 8051, Washington University School of Medicine, St. Louis, MO 63110. bind fibronectin (1%42,59,63). To add to the complexity of fibronectin binding by macrophages, several of these receptors can recognize alternative, potentially competing ligands. Moreover, a~/31 and perhaps other of these integrins can assume two affinity states for fibronectin (26). The existence of these distinct but related receptors for the same ligand suggest that they may have different roles in macrophage function. The purpose of the present work was to begin to determine how these various receptors contributed to adhe...

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“…EN also appears to serve as a recognition molecule for compounds that by themselves are not recognized by MPS cells. For example, in vitro, FN permits the uptake of gelatin (GL)-coated particles by macrophages (16), and in vivo FN is an opsonin for fibrinogen-degradation products (17) and for collagen-degradation products released into the circulation during major body burns (18).…”

Section: Introductionmentioning

confidence: 99%

Role of fibronectin on the clearance and tissue uptake of antigen and immune complexes in rats.

Cosio¹,

Bakaletz²

1987

J. Clin. Invest.

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IntroductionIn the present study, we have evaluated how plasma fibronectin (FN) and tissue FN can affect the clearance from the circulation and organ uptake of antigen or immune complexes (IC) that have the capacity to bind to FN. Phenylated gelatin (DNP-GL) (a FN binding antigen) and IC composed of DNP-GL and monoclonal IgGl anti-dinitrophenol (DNP) antibodies were tested. These probes were compared with DNP-bovine serum albumin (BSA) (a non-FN-binding antigen) and DNP-BSA IC formed with the same anti-DNP antibody used for the preparation of DNP-GL IC. We found evidence that DNP-GL, but not DNP-BSA, formed complexes with soluble FN in vitro and the data strongly suggest that DNP-GL-FN complexes form in vivo. The formation of complexes with plasma FN aided in the clearance of DNP-GL from the circulation, as shown by the facts that DNP-GL was removed from the circulation much faster than DNP-BSA and that complexes of DNP-GL with plasma FN were removed from the circulation faster than uncomplexed DNP-GL. The sites of deposition of DNP-GL were also different from those of DNP-BSA. Thus, DNP-GL demonstrated higher hepatic, splenic, and renal uptake than did DNP-BSA. Renal uptake of DNP-GL was quite high despite the fact that DNP-GL is anionic. Indeed, expressed per gram of tissue, liver and kidney deposition of DNP-GL was not significantly different. By immunofluorescence microscopy, DNP-GL could be demonstrated in hepatic sinusoids and glomerular mesangium. In vitro, DNP-GL bound to FN in the mesangium of frozen sections of kidney tissue. IC formed with DNP-GL or DNP-BSA demonstrated virtually the same size, yet the fate of DNP-GL IC was strikingly different from that of DNP-BSA IC. The removal of DNP-GL IC from the circulation was mediated by the antigen and not by Fc receptors since gelatin (an inhibitor of DNP-GL clearance) but not aggregated IgG (an inhibitor of Fc receptors) inhibited the removal of DNP-GL IC from the circulation. In summary, these studies suggest that the ability of an antigen or IC to bind to FN markedly influences the fate of that antigen or IC. Specifically, binding to FN accelerates clearance from the circulation and favors hepatic and renal (primarily mesangial) uptake of the FN binding antigen of IC.

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Mechanism of acute depletion of plasma fibronectin following thermal injury in rats. Appearance of a gelatinlike ligand in plasma.

Cited by 44 publications

References 29 publications

Characterization of the molecular forms of fibronectin in fulminant hepatic failure

Characterization of the molecular forms of fibronectin in fulminant hepatic failure

Integrin alpha v beta 3 differentially regulates adhesive and phagocytic functions of the fibronectin receptor alpha 5 beta 1.

Role of fibronectin on the clearance and tissue uptake of antigen and immune complexes in rats.

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