The structure and physicochemical properties of rat liver macrophage migration inhibitory factor

Nishihira, Jun; Kuriyama, Taisuke; Sakai, Masaharu; Nishi, Shinzo; Ohki, Shinya; Hikichi, Kunio

doi:10.1016/0167-4838(94)00215-3

Cited by 65 publications

(42 citation statements)

References 12 publications

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“…In previous studies, MIF has been described as a monomer or dimer [14,15]. However, the fact that the same trimer structure was found in different crystals of proteins from different species strongly suggests that the trimer is the physiologically important structure.…”

Section: Resultsmentioning

confidence: 98%

Crystal structure of macrophage migration inhibitory factor from human Å lymphocyte at 2.1 Å resolution

et al. 1996

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The three-dimensional structure of the macrophage migration inhibitory factor (MIF) from human lymphocytes has been determined by X-ray crystallography at 2.1 A resolution. The structure was solved by a molecular replacement technique using the coordinates of rat MIF. The molecule forms a trimer structure similar to the rat MIF. However, unlike the rat MIF whose C-terminal tail (residues 104-114) is disordered in the crystal, human MIF has a deftite main-chain conformation up to the C-terminal end. These eleven residues create two more b strands and join to the inter-subunit bsheet, which contribute to forming a trhner structure. Thus, the trimer structure consists of three seven-stranded @-sheets surrounded by six a-helices. Each f&sheet is comprised of bstrands from each of the three monomers. This architecture is almost identical to S-carboxymethyl-2-hydroxymuconate isomerase (CHMI) and is related to the E. coli signal transducing protein Pn. k :y words: Cytokine; Isomerase; Macrophage; X-ray crystal sl ,mucture

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Section: Resultsmentioning

confidence: 98%

Crystal structure of macrophage migration inhibitory factor from human Å lymphocyte at 2.1 Å resolution

et al. 1996

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“…MIF has long been considered to be expressed exclusively in activated T-lymphocytes; however, a recent report indicated that macrophages are another major source of MIF [4]. We cloned rat MIF cDNA, and reported its physicochemical properties [5,6]. Moreover, we succeeded in the crystallization of both human and rat MIF [7,8], During the course of our MIF study, we unexpectedly found the presence of MIF in human corneal epithelium (manuscript submitted for publication).…”

Section: Materials"mentioning

confidence: 89%

Identification of macrophage migration inhibitory factor (MIF) in human skin and its immunohistochemical localization

et al. 1996

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The presence and tissue localization of macrophage migration inhibitory factor (MIF) in human skin were examined. Reverse transcription-polymerasc chain reaction analysis revealed that MIF mRNA was expressed in both surgically obtained normal human epidermis and primary cultured human keratinocytes. The expression of MIF was further conf'wmed by Western blot analysis, which demonstrated a single band at about 12.5 kDa using a polyelonal antibody against human recombinant MIF. Immunohistochemical studies showed that MIF existed in human epidermis, especially in the basal layer. The pathophysiological role of MIF in human skin remains undefined; however, the present results indicate that MIF may play an important role in immunity, inflammation and cellular differentiation of epidermal cells.

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“…X-ray crystallography studies indicate that MIF exists predominantly in a trimeric form [36,37], whereas NMR [21], sedimentation velocity [24], size exclusion chromatography [22], and solution crosslinking studies [23] indicate that MIF also may exist in dimeric and monomeric forms. However, recent studies reexamining the molecular size and hydrodynamic properties of MIF in solution suggest that it exists in solution predominantly (>95%) as a trimer, which sediments with a sedimentation coefficient of 3.1S [38].…”

Section: Analytical Ultracentrifugation Analysis Of the Ph-dependent mentioning

confidence: 99%

“…1B). Although MIF crystallizes as a trimer [19], experimental studies employing NMR spectroscopy [21], size-exclusion chromatography [22], chemical cross-linking [23,24], and analytical ultracentrifugation support the existence of dimeric and monomeric forms in solution [24].…”

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confidence: 99%

Amyloid fibril formation by macrophage migration inhibitory factor

Lashuel

Aljabari

Sigurdsson

et al. 2005

Biochemical and Biophysical Research Communications

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We demonstrate herein that human macrophage migration inhibitory factor (MIF), a pro-inflammatory cytokine expressed in the brain and not previously considered to be amyloidogenic, forms amyloid fibrils similar to those derived from the disease associated amyloidogenic proteins b-amyloid and a-synuclein. Acid denaturing conditions were found to readily induce MIF to undergo amyloid fibril formation. MIF aggregates to form amyloid-like structures with a morphology that is highly dependent on pH. The mechanism of MIF amyloid formation was probed by electron microscopy, turbidity, Thioflavin T binding, circular dichroism spectroscopy, and analytical ultracentrifugation. The fibrillar structures formed by MIF bind Congo red and exhibit the characteristic green birefringence under polarized light. These results are consistent with the notion that amyloid fibril formation is not an exclusive property of a select group of amyloidogenic proteins, and contribute to a better understanding of the factors which govern protein conformational changes and amyloid fibril formation in vivo. Ó 2005 Elsevier Inc. All rights reserved.Keywords: Amyloid; Amyloid fibrils; AlzheimerÕs disease; Acid denaturation; Macrophage; Migration Inhibitory Factor; Cytokine; P53; Apoptosis; Sedimentation velocity; Electron microscopy Amyloidogenic proteins undergo a conformational change either prior to or coincident with their self-assembly into highly ordered fibrils that have a characteristic cross b-structure [1]. The presence of amyloid fibrils surrounding dead neurons in the brain is a hallmark of certain neurodegenerative conditions, including AlzheimerÕs disease, ParkinsonÕs disease, and Prion diseases. Amyloid formation in tissues can also be a pathological sequelae of many chronic inflammatory diseases [2,3]. Electron microscopic examination of the amyloid fibrils that form in vivo reveals long and unbranching filaments that are typically 10 nm in diameter. These fibrils often are detected in vivo by their ability to bind to the dye Congo red, which produces a characteristic green birefringence when illuminated by a polarized light source. Approximately 20 human proteins have been demonstrated to form amyloid in vivo, and several of these have been linked by genetic evidence with neurodegeneration and/or organ dysfunction [4]. A comparison of the primary sequence or tertiary structure of the 20 amyloidogenic proteins that occur in vivo has revealed no clear homology. Nevertheless, these amyloidogenic proteins are each capable of forming highly ordered fibrils of similar structure as discerned by X-ray fibril diffraction, electron, and atomic force microscopy [5]. The ability of these structurally and functionally diverse proteins to form amyloid fibrils with a common structure [6] is puzzling, and has been explained by the apparent tendency of these proteins to adopt a common, alternative b-sheet rich conformation (amyloidogenic intermediate(s)) that facilitates conversion into a cross-b amyloid structure 0006-291X/$ -see front ma...

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The structure and physicochemical properties of rat liver macrophage migration inhibitory factor

Cited by 65 publications

References 12 publications

Crystal structure of macrophage migration inhibitory factor from human Å lymphocyte at 2.1 Å resolution

Crystal structure of macrophage migration inhibitory factor from human Å lymphocyte at 2.1 Å resolution

Identification of macrophage migration inhibitory factor (MIF) in human skin and its immunohistochemical localization

Amyloid fibril formation by macrophage migration inhibitory factor

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