Role of group-specific component (vitamin D binding protein) in clearance of actin from the circulation in the rabbit.

The possible role of group specific component (Gc) (vitamin D-binding protein) in the clearance of cellular actin entering the circulation was examined with 125I-labeled Gc and actin injected into a rabbit model. Although filamentous F-actin is depolymerized primarily by plasma gelsolin, greater than or equal to 90% 125I-actin injected in either monomeric G- or F-form became complexed eventually with Gc (1:1 molar ratio). Clearance of Gc complexes was much faster (greater than 90% within 5 h) than that of native Gc (t1/2 = 17.2 h). Nephrectomy did not significantly alter the clearance of either Gc or actin. Since Gc complexes are dramatically increased in situations of tissue necrosis such as in fulminant hepatic failure, the current results suggest a crucial role for Gc in sequestration and clearance of released cellular actin.

[1]  J. Haddad,et al.  Vitamin D binding protein sequesters monomeric actin in the circulation of the rat. , 1987, The Journal of clinical investigation.

[2]  P. Goldschmidt-Clermont,et al.  Group-specific component (vitamin D binding protein) prevents the interaction between G-actin and profilin. , 1986, Biochemistry.

[3]  D. B. Smith,et al.  Role of plasma gelsolin and the vitamin D-binding protein in clearing actin from the circulation. , 1986, The Journal of clinical investigation.

[4]  J. Haddad,et al.  Characterization of a monoclonal antibody to human serum vitamin D binding protein (Gc globulin): recognition of an epitope hidden in membranes of circulating monocytes. , 1986, Endocrinology.

[5]  P. Janmey,et al.  Sequential binding of actin monomers to plasma gelsolin and its inhibition by vitamin D-binding protein. , 1986, Biochemical and biophysical research communications.

[6]  M. Coué,et al.  Interaction of plasma gelsolin with ADP-actin. , 1986, The Journal of biological chemistry.

[7]  N. Cooke.  Rat vitamin D binding protein. Determination of the full-length primary structure from cloned cDNA. , 1986, The Journal of biological chemistry.

[8]  T D Pollard,et al.  Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. , 1986, Annual review of biochemistry.

[9]  M. Harricane,et al.  Interactions of plasma gelsolin with actin. Isolation and characterization of binary and ternary plasma-gelsolin-actin complexes. , 1986, European journal of biochemistry.

[10]  P. Janmey,et al.  Isolation and properties of two actin-binding domains in gelsolin. , 1985, The Journal of biological chemistry.

[11]  N. Cooke,et al.  Serum vitamin D-binding protein is a third member of the albumin and alpha fetoprotein gene family. , 1985, The Journal of clinical investigation.

[12]  S. Naylor,et al.  Human group-specific component (Gc) is a member of the albumin family. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[13]  P. Janmey,et al.  Effects of semi-dilute actin solutions on the mobility of fibrin protofibrils during clot formation. , 1985, Biochimica et biophysica acta.

[14]  P. Janmey,et al.  Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking. , 1985, Biochemistry.

[15]  P. Goldschmidt-Clermont,et al.  Accurate quantitation of native Gc in serum and estimation of endogenous Gc: G-actin complexes by rocket immunoelectrophoresis. , 1985, Clinica chimica acta; international journal of clinical chemistry.

[16]  F. Schoentgen,et al.  Homology between the human vitamin D‐binding protein (group specific component), α‐fetoprotein and serum albumin , 1985, FEBS letters.

[17]  P. Arnaud,et al.  Distinct sites on the G-actin molecule bind group-specific component and deoxyribonuclease I. , 1985, The Biochemical journal.

[18]  P. Goldschmidt-Clermont,et al.  Decreased serum group‐specific component protein levels and complexes with actin in fulminant hepatic necrosis , 1985, Hepatology.

[19]  P. Arnaud,et al.  Structural studies of T lymphocyte Fc receptors. Association of Gc protein with IgG binding to Fc gamma. , 1985, The Journal of biological chemistry.

[20]  P. Goldschmidt-Clermont,et al.  Effects of ligand binding upon measurement of Gc by rocket immunoelectrophoresis: Implications for protein determination and for studies of protein/ligand interactions , 1985 .

[21]  D. Emerson,et al.  Presence of Gc (vitamin D-binding protein) and interactions with actin in human placental tissue. , 1985, American journal of reproductive immunology and microbiology : AJRIM.

[22]  J. Bryan,et al.  Actin-gelsolin interactions. Evidence for two actin-binding sites. , 1984, The Journal of biological chemistry.

[23]  J. Haddad,et al.  Brevin and vitamin D binding protein: comparison of the effects of two serum proteins on actin assembly and disassembly. , 1984, Biochemistry.

[24]  S. Brenner,et al.  The critical concentration of actin in the presence of ATP increases with the number concentration of filaments and approaches the critical concentration of actin.ADP. , 1984, The Journal of biological chemistry.

[25]  J. Haddad.  Nature and Functions of the Plasma Binding Protein for Vitamin D and its Metabolites , 1984 .

[26]  P. Arnaud,et al.  Gc (vitamin D binding protein) binds to cytoplasm of all human lymphocytes and is expressed on B-cell membranes. , 1984, Clinical immunology and immunopathology.

[27]  P. Arnaud,et al.  Evidence of Increased Gc: Actin Complexes in Pregnant Serum: A Possible Result of Trophoblast Embolism , 1983, American journal of reproductive immunology : AJRI : official journal of the American Society for the Immunology of Reproduction and the International Coordination Committee for Immunology of Reproduction.

[28]  D. Emerson,et al.  Linkage between surface immunoglobulin and cytoskeleton of B lymphocytes may involve Gc protein , 1983, Nature.

[29]  A. Weeds,et al.  Plasma actin depolymerizing factor has both calcium-dependent and calcium-independent effects on actin. , 1983, Biochemistry.

[30]  J. Vandekerckhove,et al.  Purification and characterization of a new mammalian serum protein with the ability to inhibit actin polymerization and promote depolymerization of actin filaments. , 1982, Biochemistry.

[31]  E. Korn,et al.  Actin polymerization and its regulation by proteins from nonmuscle cells. , 1982, Physiological reviews.

[32]  J. Haddad.  Human serum binding protein for vitamin D and its metabolites (DBP): evidence that actin is the DBP binding component in human skeletal muscle. , 1982, Archives of biochemistry and biophysics.

[33]  C. Blum,et al.  Turnover of the plasma binding protein for vitamin D and its metabolites in normal human subjects. , 1981, The Journal of clinical endocrinology and metabolism.

[34]  J. Albrecht,et al.  Identification of gelsolin, a Ca2+-dependent regulatory protein of actin gel-sol transformation, and its intracellular distribution in a variety of cells and tissues , 1981, The Journal of cell biology.

[35]  J. H. Schwartz,et al.  Characterization of brevin, a serum protein that shortens actin filaments. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[36]  F. Oksman,et al.  Binding of the apo and holo forms of the serum vitamin D-binding protein to human lymphocyte cytoplasm and membrane by indirect immunofluorescence. , 1981, Immunology letters.

[37]  D. Lawson,et al.  Vitamin D plasma binding protein. Turnover and fate in the rabbit. , 1981, The Journal of clinical investigation.

[38]  A. Wyllie.  Cell death: a new classification separating apoptosis from necrosis , 1981 .

[39]  J. R. Bamburg,et al.  Actin filament disassembly in blood plasma , 1980, FEBS letters.

[40]  K. Zaner,et al.  Ca2+ control of actin gelation. Interaction of gelsolin with actin filaments and regulation of actin gelation. , 1980, The Journal of biological chemistry.

[41]  T. Stossel,et al.  Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages. , 1980, The Journal of biological chemistry.

[42]  M. Forni,et al.  Tumor localization of radiolabeled antibodies against carcinoembryonic antigen in patients with carcinoma: a critical evaluation. , 1980, The New England journal of medicine.

[43]  P. D. de Moor,et al.  Lack of effect of the vitamin D status on the concentration of the vitamin D-binding protein in rat serum. , 1980, Endocrinology.

[44]  P. D. de Moor,et al.  Vitamin D-binding protein (Gc-globulin) binds actin. , 1980, The Journal of biological chemistry.

[45]  R. Thorstensson,et al.  F-Actin-depolymerizing activity of human serum. , 1979, European journal of biochemistry.

[46]  T. Stossel,et al.  Control of cytoplasmic actin gel–sol transformation by gelsolin, a calcium-dependent regulatory protein , 1979, Nature.

[47]  J. Haddad,et al.  Human serum binding protein for vitamin D and its metabolites. I. Physicochemical and immunological identification in human tissues. , 1979, The Journal of biological chemistry.

[48]  J. Haddad,et al.  Human serum binding protein for vitamin D and its metabolites. II. Specific, high affinity association with a protein in nucleated tissue. , 1979, The Journal of biological chemistry.

[49]  R. Norberg,et al.  Anti-actin antibodies. , 1978, Current topics in microbiology and immunology.

[50]  P. D. de Moor,et al.  The measurement of the vitamin D-binding protein in human serum. , 1977, The Journal of clinical endocrinology and metabolism.

[51]  U. Rosa.  Advances in protein labelling , 1976 .

[52]  L. Cavalli-Sforza,et al.  Group-specific component (Gc) proteins bind vitamin D and 25-hydroxyvitamin D. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[53]  K. Laki,et al.  On the interaction of F-actin with fibrin. , 1974, Biochimica et biophysica acta.

[54]  H. Cleve.  The variants of the group-specific component. A review of their distribution in human populations. , 1973, Israel journal of medical sciences.

[55]  A. Wyllie,et al.  Apoptosis: A Basic Biological Phenomenon with Wide-ranging Implications in Tissue Kinetics , 1972, British Journal of Cancer.

[56]  J. Hirschfeld.  Immune-electrophoretic demonstration of qualitative differences in human sera and their relation to the haptoglobins. , 2009, Acta pathologica et microbiologica Scandinavica.

[57]  O. Smithies,et al.  Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. , 1955, The Biochemical journal.