Literature DB >> 6893215

Functional tuftsin binding sites on macrophage-like tumor line P388D1 and on bone marrow cells differentiated in vitro into mononuclear phagocytes.

Z Bar-Shavit, I Bursuker, R Goldman.   

Abstract

Mouse bone marrow cells, differentiated in vitro into mononuclear phagocytes (BMDMP), posess functional tuftsin binding sites, i.e. both tuftsin binding capacity and augmented phagocytic response related to tuftsin binding. The binding capacity of BMDMP was shown to be higher by a factor of about three than that exhibited by mouse monocytes and by normal, thioglycollate and Corynebacterium parvum induced peritoneal macrophages. The relatively high binding capacity did not depend on experimental variations in the in vitro culture of these populations (i.e. length of in vitro cultivation, source of serum or presence of conditioned medium leading to cell proliferation). The macrophage-like line, P388D1, was also shown to possess functional tuftsin binding sites and its binding capacity was comparable to that of the peritoneal macrophage populations.

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Year:  1980        PMID: 6893215     DOI: 10.1007/bf00230168

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN: 0300-8177            Impact factor:   3.396


  10 in total

1.  Studies on the effect of soluble lymphocyte products (lymphokines) on macrophage physiology. I. Early changes in enzyme activity and permeability.

Authors:  L W Poulter; J L Turk
Journal:  Cell Immunol       Date:  1975-11       Impact factor: 4.868

2.  Identification of macrophage-like characteristics in a cultured murine tumor line.

Authors:  H S Koren; B S Handwerger; J R Wunderlich
Journal:  J Immunol       Date:  1975-02       Impact factor: 5.422

3.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

4.  Quantitative and functional differences induced in bone marrow-derived mononuclear phagocytes by inflammatory stimuli.

Authors:  I Bursuker; R Goldman
Journal:  J Reticuloendothel Soc       Date:  1979-05

5.  The chemical synthesis of the phagocytosis-stimulating tetrapeptide tuftsin (Thr-Lys-Pro-Arg) and its biological properties.

Authors:  K Nishioka; P S Sato; A Constantopoulos; V A Najjar
Journal:  Biochim Biophys Acta       Date:  1973-05-17

6.  Specific binding sites for the phagocytosis stimulating peptide tuftsin on human polymorphonuclear leukocytes and monocytes.

Authors:  Y Stabinsky; P Gottlieb; V Zakuth; Z Spirer; M Fridkin
Journal:  Biochem Biophys Res Commun       Date:  1978-07-28       Impact factor: 3.575

7.  "Tuftsin": a natural phagocytosis stimulating peptide.

Authors:  V A Najjar; K Nishioka
Journal:  Nature       Date:  1970-11-14       Impact factor: 49.962

8.  Tuftsin-macrophage interaction: specific binding and augmentation of phagocytosis.

Authors:  Z Bar-Shavit; Y Stabinsky; M Fridkin; R Goldman
Journal:  J Cell Physiol       Date:  1979-07       Impact factor: 6.384

9.  Synthesis of the second component of complement by long-term primary cultures of human monocytes.

Authors:  L P Einstein; E E Schneeberger; H R Colten
Journal:  J Exp Med       Date:  1976-01-01       Impact factor: 14.307

10.  The pinocytic rate of activated macrophages.

Authors:  P J Edelson; R Zwiebel; Z A Cohn
Journal:  J Exp Med       Date:  1975-11-01       Impact factor: 14.307

  10 in total
  2 in total

1.  Tuftsin (Thr-Lys-Pro-Arg), a natural modulator of macrophage activity: further studies.

Authors:  N J Bump; V A Najjar
Journal:  Mol Cell Biochem       Date:  1984-09       Impact factor: 3.396

Review 2.  Tuftsin, Thr-Lys-Pro-Arg. Anatomy of an immunologically active peptide.

Authors:  M Fridkin; P Gottlieb
Journal:  Mol Cell Biochem       Date:  1981-12-04       Impact factor: 3.396

  2 in total

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