Cryoprecipitate Reversal of Opsonic α
            <sub>2</sub>
            -Surface Binding Glycoprotein Deficiency in Septic Surgical and Trauma Patients

Saba, Thomas M.; Blumenstock, Frank A.; Scovill, William A.; Bernard, H. Russell

doi:10.1126/science.675246

Cited by 204 publications

(59 citation statements)

References 16 publications

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“…Fibronectin has also been shown to increase adherence of bacteria to neutrophils (36, 37), although whether bacterial uptake by neutrophils is facilitated by fibronectin remains unclear (36)(37)(38)(39). However, regardless of opsonic activity, binding of plasma fibronectin to the bacterial surface might block adhesion receptors on S. aureus, thus representing an important defense mechanism against tissue invasion (35,(40)(41)(42) (44,46,47). The FnBP signal peptide is apparently recognized by the E. coli membranes (17).…”

Section: Discussionmentioning

confidence: 99%

Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides.

Signäs

Raucci

Jönsson

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

354

295

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Binding of cells of Staphylococcus aureus to fibronectin, which may represent a mechanism of host tissue adherence, involves a fibronectin-receptor protein present on the bacterial surface. Cloning of a gene coding for a staphylococcal fibronectin-binding protein and construction of a fusion protein with fibronectin-binding properties was previously reported from our laboratory. We have now sequenced the gene and deduced a primary sequence of the fibronectin-binding protein. The protein resembles other cell-wall-associated proteins on Gram-positive bacteria in that it (i) appears to be anchored in the cell membrane via its C-terminal end, (ii) contains a proline-rich repeating unit outside the membrane anchor, and (iii) contains a long (36-amino acid) signal sequence at the N terminus. The fibronectin-binding activity has been localized to a domain composed of a 38-amino acid unit repeated completely three times and partially a fourth time; the identity between the three 38-amino acid sequences varies from 42 to 87%. Three synthetic peptides mimicking the structure of each 38-amino acid unit were constructed. All three peptides interacted with fibronectin, as indicated by their ability to inhibit binding of fibronectin to staphylococcal cells, whereas an unrelated 37-amino acid peptide showed no inhibitory activity.

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Section: Discussionmentioning

confidence: 99%

Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides.

Signäs

Raucci

Jönsson

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

354

295

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“…Fibronectin deficiency is seen acutely after trauma or burn and in association with sepsis in injured patients (5,13,15,16). Deficiency also exists in critically-ill adult patients with disseminated intravascular coagulation and organ failure (10).…”

Section: Res Reticuloendothelial Systemmentioning

confidence: 99%

“…Much interest exists as to fibronectin levels in septic injured adult patients (10,13,14,17), and the ability to reverse fibronectin deficiency by infusion of fresh plasma cryoprecipitate (15,16). Although the range of normal has been defined by several studies in the adult population, changes in circulating fibronectin in the pediatric population with age has not been reported.…”

Section: Res Reticuloendothelial Systemmentioning

confidence: 99%

Normal Fibronectin Levels as a Function of Age in the Pediatric Population

et al. 1983

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SummaryFibronectin is an important non-immune opsonic protein influencing phagocytic clearance of blood-borne nonbacterial particulates which may arise in association with septic shock, tissue injury, and intravascular coagulation. In the present study, serum fibronectin was measured by both electroimmunoassay as well as rapid immunoturbidimetric assay in healthy children (n = 114) ranging in age from 1 month to 15 years in order to delineate the temporal alterations in fibronectin with age. Normal adult serum fibronectin concentrations are typically 220 pg/ml + 20 pg/ml. Serum concentration is 3540% lower than normal plasma concentration due to the binding of fibronectin to fibrin during clot formation. Children between 1-12 months of age had significantly (P < 0.05) lower serum fibronectin levels than children between the ages of 1-15 years. Progressive elevation in fibronectin levels was observed within the last 8 months of the first year of age. Fibronectin levels in children older than 1 year of age remained constant up to 15 years and were within the lower limit of the normal adult concentration. No significant (P > 0.05) difference in serum fibronectin was observed between male and female children at all age groups. Fibronectin levels thus, increase during the first year of age and normal levels of this blood protein in the infant are less than the normal range for adults.

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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).…”

mentioning

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

233

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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Cryoprecipitate Reversal of Opsonic α ₂ -Surface Binding Glycoprotein Deficiency in Septic Surgical and Trauma Patients

Cited by 204 publications

References 16 publications

Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides.

Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides.

Normal Fibronectin Levels as a Function of Age in the Pediatric Population

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

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Cryoprecipitate Reversal of Opsonic α 2 -Surface Binding Glycoprotein Deficiency in Septic Surgical and Trauma Patients

Cited by 204 publications

References 16 publications

Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides.

Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides.

Normal Fibronectin Levels as a Function of Age in the Pediatric Population

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

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Cryoprecipitate Reversal of Opsonic α ₂ -Surface Binding Glycoprotein Deficiency in Septic Surgical and Trauma Patients