Evaluation of a relationship between polymer bulk hydroxyl and surface oxygen content and in vitro serum-material interaction.

To evaluate serum-material interaction for six types of minimodule and to assess the relationship between the interaction and chemical composition, notably bulk polymer hydroxyl (-OH) percent of polymer, or surface oxygen (SO) percent, polymeric membranes with varying -OH and SO percents were evaluated with normal human serum. The membrane materials (-OH percent and SO percent) evaluated included polypropylene (PP; 0% and 1.9%), polyvinyl alcohol (PVA; 23.7% and 27.3%), ethylene vinyl alcohol (EVAL 4A and D; 30.4% and 25.3%), Cuprophan (CP; 31.5% and 37.4%), and Hemophan (HP; 30.9% and 23.6%), respectively. Data from serum perfusions expressed as percent changes to sham perfusion showed that solute percent decreases were less than 10% in all materials except PVA (10-22%). PVA and CP had higher C3a, C4a, and C5a, and C3a concentration increases, and had larger suppressive effects for all three mitogen-induced mononuclear cell transformation functions (MNCTF) and concanavalin A-induced MNCTF, respectively. PVA had higher SO percent than EVAL and CP was higher than HP, despite PVA and CP having lower or comparable bulk -OH percent to EVAL or HP. The results obtained in the serum material interaction studies related more with the SO percent of the polymer rather than bulk -OH percent. The differences for C4a and PHA-induced MNCTF observed between the two EVAL membranes may be associated with significantly different pore size and therefore different surface structural properties. These results suggest that surface chemical (SO percent on the materials) and structural property analyses are important factors in biocompatibility parameter studies.

[1]  P. Malchesky,et al.  Immunomodulating effects of serum-material interactions. , 1991, Journal of biomedical materials research.

[2]  F. Wiese,et al.  Chemical modification of cellulosic membranes and their blood compatibility. , 2008, Artificial organs.

[3]  H. Yasuda,et al.  A study of surface dynamics of polymers. II. Investigation by plasma surface implantation of fluorine–containing moieties , 1988 .

[4]  P. Malchesky,et al.  Anticoagulant and membrane effects on humoral and cellular changes during plasmapheresis. , 1988, ASAIO transactions.

[5]  J. Vienken,et al.  Modified cellulosic dialyzer membranes: an investigative tool in thrombogenicity studies. , 1988, ASAIO transactions.

[6]  P. Malchesky,et al.  Humoral, cellular, and hemodynamic changes induced by blood-material interaction in membrane plasmapheresis. , 1987, ASAIO transactions.

[7]  T. Horbett,et al.  Complement activation by hydroxyethylmethacrylate-ethylmethacrylate copolymers. , 1987, Journal of biomedical materials research.

[8]  U. Baurmeister,et al.  Dialyzer membranes: effect of surface area and chemical modification of cellulose on complement and platelet activation. , 1987, Artificial organs.

[9]  P. Malchesky,et al.  Changes in interleukin-1 during membrane plasmapheresis. , 1986, ASAIO transactions.

[10]  F. Lasky,et al.  Bromocresol purple dye-binding method for the estimation of serum albumin adapted to the SMA 12/60. , 1985, Clinical biochemistry.

[11]  D. Chenoweth Complement activation during hemodialysis: clinical observations, proposed mechanisms, and theoretical implications. , 1984, Artificial organs.

[12]  T. Hugli,et al.  Mechanisms of leukocyte regulation by complement-derived factors. , 1984, Contemporary topics in immunobiology.

[13]  A. Cheung,et al.  Anaphylatoxin formation during hemodialysis: effects of different dialyzer membranes. , 1983, Kidney international.

[14]  M. Kazatchkine,et al.  Heparin prevents formation of the human C3 amplification convertase by inhibiting the binding site for B on C3b. , 1983, Molecular immunology.

[15]  R. Sassetti,et al.  Complement metabolism during membrane plasma separation. , 1983, Artificial organs.

[16]  R. DiSipio,et al.  Suppression of T lymphocyte functions by human C3 fragments. I. Inhibition of human T cell proliferative responses by a kallikrein cleavage fragment of human iC3b. , 1983, Journal of immunology.

[17]  M. Thoman,et al.  Anaphylatoxin-mediated regulation of the immune response. II. C5a-mediated enhancement of human humoral and T cell-mediated immune responses. , 1983, Journal of immunology.

[18]  M. Macart,et al.  An improvement of the Coomassie Blue dye binding method allowing an equal sensitivity to various proteins: application to cerebrospinal fluid. , 1982, Clinica chimica acta; international journal of clinical chemistry.

[19]  T. Hugli,et al.  Anaphylatoxin-mediated regulation of the immune response. I. C3a- mediated suppression of human and murine humoral immune responses , 1982, The Journal of experimental medicine.

[20]  J. Weiler,et al.  Inhibition of secondary in vitro antibody responses by the third component of complement. , 1982, Journal of immunology.

[21]  R. Nakamura,et al.  Collaborative calibration of the U. S. National and the College of American Pathologists reference preparations for specific serum proteins. , 1982, American journal of clinical pathology.

[22]  J. Weiler,et al.  The third component of complement inhibits human lymphocyte blastogenesis. , 1981, Journal of immunology.

[23]  M. Kazatchkine,et al.  Structural determinants of the capacity of heparin to inhibit the formation of the human amplification C3 convertase. , 1981, The Journal of clinical investigation.

[24]  D. Clark,et al.  Plasma polymerization. II. An ESCA investigation of polymers synthesized by excitation of inductively coupled RF plasma in perfluorobenzene and perfluorocyclohexane , 1980 .

[25]  R. Genco,et al.  Inhibition of lymphocyte blastogenesis by C3c and C3d. , 1979, Journal of immunology.

[26]  A. G. Osler,et al.  Studies of immunosuppression by cobra venom factor. I. On early IgG and IgM responses to sheep erythrocytes and DNP-protein conjugates. , 1978, Journal of immunology.

[27]  J. Sternberg A rate nephelometer for measuring specific proteins by immunoprecipitin reactions. , 1977, Clinical chemistry.

[28]  C. N. Reilley,et al.  ESCA study of polymer surfaces treated by plasma , 1977 .

[29]  A. Allison,et al.  Effects of activated complement components on enzyme secretion by macrophages. , 1976, Immunology.

[30]  S. Wahl,et al.  Interaction of soluble C3 fragments with guinea pig lymphocytes. Comparison of effects of C3a, C3b, C3c, and C3d on lymphokine production and lymphocyte proliferation. , 1976, Journal of immunology.

[31]  T. Hugli Human anaphylatoxin (C3a) from the third component of complement. Primary structure. , 1975, Journal of Biological Chemistry.

[32]  S. Wahl,et al.  Lymphokine production by C3b-stimulated B cells. , 1975, Journal of immunology.

[33]  M. Pepys,et al.  Inhibition by C3 fragments of C3-dependent rosette formation and antigen-induced lymphocyte transformation. , 1974, Clinical and experimental immunology.

[34]  D. Rosenstreich,et al.  Induction of lymphokine production by EAC and of blastogenesis by soluble mitogens during human B-cell activation , 1974, Nature.

[35]  W. Richmond Preparation and properties of a cholesterol oxidase from Nocardia sp. and its application to the enzymatic assay of total cholesterol in serum. , 1973, Clinical chemistry.