The sequence 130–137 of human interferon-α2 is involved in the competition of interferon, prothymosin α and cholera toxin B subunit for common receptors on human fibroblasts

Zav’yalov, V.P.; Navolotskaya, E. V.; Vasilenko, Raisa N.; Abramov, Vyacheslav M.; Volodina, Eva Yu.; Roslovtseva, O.A.; Prusakov, A.N.; Kaurov, O. A.

doi:10.1016/0161-5890(94)00161-s

Cited by 25 publications

(19 citation statements)

References 26 publications

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“…Earlier Scatchard analysis of the binding revealed only one type of receptors for the octapeptide on the thymocyte cells and murine thymocyte plasma membranes (213, 214) (Scatchard plot represents a direct line). The albeferon competitive inhibition coefficient ( IC50) and the calculated inhi-bition constant (Ki) are very close to that of HuIFN-a2 (57,213,214). This means that albeferon has a high affinity to the murine thymocyte receptor and binds it practically with the same efficiency as IFN itself.…”

Section: Grufting O J Ifn-a's Th4al-like Immu-mentioning

confidence: 57%

“…One of the synthesized peptides (a-peptoferon) overlapping the TMal -like sequence of HuIFN-a2 effectively competed with HuIFN-a2, TMa,. proTMa for common receptors on mouse thymocytes (i.e., the K, of reHuIFN-a2 binding by a-peptoferon is equal to about lo-" M) (213,214) and with sB-CT on human fibroblasts (214) and activated thymocyte blast transformation at a concentration comparable to that of HuIFN-a2 (lo-" M).…”

Section: Localization Of Ifns-a@ Active Sites By Analysis Of Homologymentioning

confidence: 99%

“…g7deca entaplegic gene product of Drosophilu "the mammalian Vg-I homologue, "growth differentiation factor I , .Human G-CSF were responsible for competition of IFNs and sB-CT for common ganglioside receptors (78). Moreover, attention was drawn to the fact that the homology site of HuIFN-a2 to sB-CT is at the same time homologous to TMal (214). In this connection, competition between HuIFN-a2, TMal, proTMa, peptide, corresponding to the TMa,-like sequence of HuIFN-a2 (a-peptoferon), and sB-CT was studied (214).…”

Section: Structure Of Receptors Jbr If"@mentioning

confidence: 99%

“…Moreover, attention was drawn to the fact that the homology site of HuIFN-a2 to sB-CT is at the same time homologous to TMal (214). In this connection, competition between HuIFN-a2, TMal, proTMa, peptide, corresponding to the TMa,-like sequence of HuIFN-a2 (a-peptoferon), and sB-CT was studied (214). Such a competition was revealed on human fibroblasts.…”

Section: Structure Of Receptors Jbr If"@mentioning

confidence: 99%

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Interferons α/β and their receptors: place in the hierarchy of cytokines

Zav’yalov¹,

Zav’yalova²

1997

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Interferons α/β (IFNs‐α/β) are the first cytokines to be produced by recombinant DNA technology. They regulate growth and differentiation, affecting cellular communication, signal transduction pathways and immunological control. This review focuses on the relationships between the structure and biological activities of IFNs‐α/β induced as a result of specific interactions with different types of polypeptide receptors as well as on the role of glycolipids in the modulation of these activities. The discovery of the primary structure homology of HuIFNs‐α and thymus hormone‐thymosin α‐1 (TMα1), the experimental finding of the competition between IFN‐α and TMα1 for common receptors and the reproduction by reHuIFN‐α2 of TMα1 immunomodulating activities create the basis of reHu‐IFN‐α therapeutics instead of TMα1 and potentiation of vaccines by reHuIFN‐α. The first successful attempt at grafting of the HuIFN‐α2′s TMα1‐like immunomodulating site to the designed de novo protein albeferon is described. This article also aims at reviewing recent data concerning the structure of other cytokines and their receptors. Their reciprocal structure‐function taxonomy is proposed. The place of IFNs‐α/β and their receptors in the hierarchy of cytokines is determined.

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Section: Grufting O J Ifn-a's Th4al-like Immu-mentioning

confidence: 57%

Section: Localization Of Ifns-a@ Active Sites By Analysis Of Homologymentioning

confidence: 99%

Section: Structure Of Receptors Jbr If"@mentioning

confidence: 99%

Section: Structure Of Receptors Jbr If"@mentioning

confidence: 99%

See 2 more Smart Citations

Interferons α/β and their receptors: place in the hierarchy of cytokines

Zav’yalov¹,

Zav’yalova²

1997

APMIS

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show abstract

“…More than two decades ago octapeptide LKEKKYSP corresponding to the sequence 131-138 of human interferon-α 1 (IFN-α 2 ) capable of high affinity binding to murine thymocytes and human fibroblasts [32] was obtained. [31] Binding of labeled octapeptide was competitively inhibited by unlabeled IFN-α 2 , thymosin-α 1 (TM-α 1 ) and cholera toxin B-subunit (CT-B).…”

Section: Introductionmentioning

confidence: 99%