Similarity of antigelatin factor and cold insoluble globulin

Dessau, Waltraud; Jilek, F.; Adelmann, B.; Hörmann, Helmut

doi:10.1016/0005-2795(78)90566-4

Cited by 63 publications

(25 citation statements)

References 20 publications

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“…Loss of fibronectin-adhesive moleules from the cell surface of circulating reticulocytes mi occur by an endocytotic mechanism, since spectrin-free surface invaginations and intracellular vesicles have been observed in reticulocytes within normal rabbit spleen (21). Fibronectin or fibronectinadhesive molecules on the surface of reticulocytes may also serve as an attachment site for splenic macrophages that participate in remodeling of the surface membrane, because macrophages are known to adhere and ingest fibronectincoated particles (22)(23)(24). Interactions of cells with extracellular matrices are essential for many developmental processes (25,26), and it will be important to determine the specificity of interactions among erythroid precursor cells, extracellular matrix proteins, and-7macrophages.…”

Section: Discussionmentioning

confidence: 99%

Mammalian reticulocytes lose adhesion to fibronectin during maturation to erythrocytes.

Patel¹,

Ciechanover²,

Platt³

et al. 1985

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

102

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We describe three situations in which a large fraction of circulating red blood cells attach tightly and specifically to fibronectin: (0) rabbits made anemic by repeated bleeding, (ii) patients with hemolytic anemia and functional asplenia and splenectomized normal humans, and (iii) splenectomized mice. Upon induction of anemia in rabbits, the proportion of circulating red blood cells capable of specifically attaching to fibronectin-coated plastic increased in parallel with the number of reticulocytes. Fibronectin-adherent red cells were barely detectable when the rabbit had recovered from the anemia. Attachment of reticulocytes to fibronectin was specific; cells did not attach to dishes coated with albumin, laminin, or collagen. None of these proteins promoted the attachment of normal erythrocytes. About 75% of the erythrocytes from splenectomized mice (but not control mice) also attached specifically to fibronectin 40 days after surgery. The effect of splenectomy was incomplete and transient; adherent cells were not detectable 8 weeks after splenectomy. As judged by labeling studies with [35S]methionine, newly emergent reticulocytes preferentially attached to fibronectin. We suggest that about half of the reticulocytes in erythropoietically unstressed mice lose their ability to attach to fibronectin, possibly due to loss of fibronectin-adhesive components, during passage through the spleen. The others lose their ability to interact with fibronectin before release, in the bone marrow, or in some extrasplenic site.Erythrocyte production in adult mammals begins in the bone marrow; nucleated erythroid stem cells undergo proliferation and terminal differentiation into nonnucleated reticulocytes, the immediate precursor of mature erythrocytes. Before the final stages of maturation, reticulocytes are released from the bone marrow into the circulation. Reticulocyte maturation is completed within 1-3 days; during this period remnants of mitochondria, Golgi complex, and polyribosomes are eliminated. Reticulocyte maturation also involves the remodeling of the plasma membrane, resulting in loss of the ability to exhibit endocytosis (1-3).Undifferentiated murine erythroleukemia (MEL) cells growing in culture adhere tightly to fibronectin, and erythroid differentiation is accompanied by the loss of adhesion fibronectin (4). Fibronectin is a glycoprotein associated with extracellular matrices of many tissues; it is tightly bound to the surface of many cells, and is also found in the blood plasma (5, 6). Fibronectin is a major component of the interstitial matrix in the bone marrow (7). We speculated that the bone marrow precursors of erythrocytes interact with fibronectin and that loss of fibronectin adhesion is associated with release of the cell into the circulation (4). But the function of such interactions during erythroid differentiation remains to be investigated.We show here that human, rabbit, and mouse reticulocytes specifically attach to fibronectin and that the remodeling of the reticulocyte plasma membran...

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Section: Discussionmentioning

confidence: 99%

Mammalian reticulocytes lose adhesion to fibronectin during maturation to erythrocytes.

Patel¹,

Ciechanover²,

Platt³

et al. 1985

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

102

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“…Fibronectin was also purified from whole plasma by affinity chromatography on immobilized gelatin (16,17). Adsorbed fibronectin was eluted from the column with 1 M sodium bromide, pH 5.3 (18), dialyzed against Tris-buffered saline, pH 7.4, and concentrated by precipitation with 40% ammonium sulfate. Fibrinogen, Factor XIII, and fibronectin were >95% pure as assayed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.…”

Section: Introductionmentioning

confidence: 99%

Cross-linking of fibronectin to collagen by blood coagulation Factor XIIIa.

Mosher¹,

Schad²

1979

J. Clin. Invest.

318

129

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“…They interpreted this response as an interaction with anticollagen antibodies. However, these anticollagen antibodies, which are naturally occurring, may actually be plasma fibronectin (34)(35)(36)(37).…”

Section: Discussionmentioning

confidence: 99%

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

Deno¹,

McCafferty²,

Saba³

et al. 1984

J. Clin. Invest.

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Abs tract. Plasma fibronectin was depleted within 15 min following sublethal burn, followed by partial recovery at 8 h and complete restoration by 24 h in anesthetized rats. Radiolabeled 7Se-plasma fibronectin, injected intravenously before burn, was rapidly sequestered in burn skin as well as the liver. Fibronectin levels at 2 h postburn as detected by immunoassay vs. 7"Seplasma fibronectin indicated that more fibronectin was in the plasma than detected by electroimmunoassay. Crossed September 1983. plasma had an apparent molecular weight -40% greater than that observed in normal plasma. These data suggest the release into the blood of a gelatinlike ligand from burned skin, which complexes with plasma fibronectin. Thus, fibronectin deficiency acutely postburn appears mediated by (a) its accumulation at the site ofburn injury; (b) its removal from the circulation by the liver; and (c) its presence in the plasma in a form that is less detectable by immunoassay.

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Similarity of antigelatin factor and cold insoluble globulin

Cited by 63 publications

References 20 publications

Mammalian reticulocytes lose adhesion to fibronectin during maturation to erythrocytes.

Mammalian reticulocytes lose adhesion to fibronectin during maturation to erythrocytes.

Cross-linking of fibronectin to collagen by blood coagulation Factor XIIIa.

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

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