Ibelgaufts H (1995). Dictionary of Cytokines. MIF-1. Macrophage migration inhibitory factor 1

March 28, 2019

Citate :
Horst Ibelgaufts. Dictionary of Cytokines. 1995 VCH. Winham, New York, Basel, Cambridge, Tokyo. Page 522-3.

MIF, Migration Inhibition factor, Macrophage migration inhibitory factor (MMIF).
An operational definition for factors that inhibit in vitro the migration of macrophages out of capillary tubes or small pieces of tissue.
Many proteins have been described to possess MIF activity, including TNF, IFN-gamma, IL1, IL2, GM-CSF , LIF leucocyte migration inhibitory factor.
The proteins known as MRP8 and MRP14 ( MIF-related protein) are MIF- related proteins that are recognized by some monoclonal antibodies directed against MIF- activities.
Another protein MIF-1, with MIF activity is secreted by T sell hybridoma,
Another poorly characterized migration inhibitory factor is FSMIF-2.
Another factor influencing the chemotactic behavior of neutrophilic macrophages is ”HDLF” ( Hodgin-derived leucocyte factor).
In addition there are many other poorly characterized factors with MIF activity that cannot be blocked by antibodies against known cytokines and that are therefore probably distinct factors.

MMIF, a major secreted protein released by anterior pituitary cells in response to bacterial LPS.
It is identical with Sarcolectin binding protein. Pituitary-derived MIF contributes to circulating MIF present in the post-acute phase of endotoxinemia ( see also. Septic chock).
Recombinant murin MIF greatly enhances lethality when co-injected with LPSs,
and anti-MIF antibodies confer protection against lethal endotoxinemia.

One particular factor with MIF activity is also found in chicken murine and human embryonic eye lenses ( see 10K protein). A 12kDa factor of 115 amino acids that also inhibits the migration of macrophages is produced by antigen-stimulated T cells.

These proteins show extensive seq homology with each other and with a rat liver protein , designed ”TRANSMIF”, a murine protein designated GIF (glycosylation inhibiting factor),
and a mouse delayed early responsive gene, designated ”DER6”.
These highly homol. prot. sharing seq. homol. up to 98%, are structurally related to the theta-class of GST, Glutathione S – transferase, a subclass of GSTs thought to be the most ancient evolutionary GST class. All proteins have retained a Glutathione (GSH) binding domaine and demonstrate transferase activity.
GSTs protect against xenobiotic chemicals by catalyzing the conjugation of glutathione (GSH), which renders them non-toxic.

MIF is known as a mediator of cellular immunity with specific effects on the differentiation of mononuclear phagocytes. The expression of MIF activity correlates well with delayed hypersensitivity and cellular immunity in humans and MIF is now recognized as a principal cytokine modulating T cell/macrophage interactions in the expression of delayed hypersensitivity and acquired cellular immunity.

Recombinant human MIF is responsible for the specific activation of macrophages to kill intracellular parasites such as Mycobacterium avium and Leishmania donovani.
Recombinant human MIF has been shown to activate macrophage expression of NO, a potent antimicrobial agent that is produced by the NO synthase (NOS) – mediated oxidation ot terminal L-arginine guanidine nitrogen atoms.
Recombinant human MIF upregulates expression of genes encoding HLA-DR and IL1 beta and elaboration of IL1beta by human monocyte-derived macrophages.
Human recombinant MIF can also activate cultural human peripheral blood monocytes and monocyte-derived macrophages to become cytotoxic for tumor cells in vitro.
MIF also induces macrophages to produce TNF-alfa and IL1beta.

Administration of soluble bovine serum albumin of human immunodeficiency virus 120 kDa glycoprotein to mice in the presence of recombinant MIF together with incomplete Freund´s adjuvant induces a strong T cell proliferative response comparable to that of complete Freund´s adjuvant.
Recombinant MIF also increases antibody production, especially IgG1 and IgM, in mice. MIF may be useful, therefore , as an adjuvant in the development of vaccines.
MIF activity can be detected in the synovia of patients with rhematoid arthritis.
The expression of MIF at sites of inflammation also suggest a role for the mediator in regulation the function of macrophages in host defence.

Muistiin 28.3. 2019

Comments are closed.

Leabright's Blog

Just another WordPress.com weblog


WordPress.com is the best place for your personal blog or business site.

%d bloggers like this: