Purification and Characterization of Macrophage Migration Inhibitory Factor as a Secretory Protein from Rat Epididymis: Evidences for Alternative Release and Transfer to Spermatozoa

Eickhoff, Regina; Wilhelm, Beate; Renneberg, Heiner; Wennemuth, Gunther; Bacher, Michael; Linder, Dietmar; Bucala, Richard; Seitz, Jürgen; Meinhardt, Andreas

doi:10.1007/bf03401836

Cited by 66 publications

(52 citation statements)

References 32 publications

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“…MIF, however, exists preformed in substantial amounts in the cytosol and nucleus of multiple cells, and its elaboration relies not only on de novo protein synthesis but on secretion from preformed stores (7,20,22,38,41). This is consistent with the present study, which identified constitutive MIF in whole cell cardiac Cardiac function values are expressed as means Ϯ SE.…”

Section: Discussionsupporting

confidence: 92%

Macrophage migration inhibitory factor mediates late cardiac dysfunction after burn injury

Willis¹,

Carlson²,

DiMaio

et al. 2005

American Journal of Physiology-Heart and Circulatory Physiology

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Section: Discussionsupporting

confidence: 92%

Macrophage migration inhibitory factor mediates late cardiac dysfunction after burn injury

Willis¹,

Carlson²,

DiMaio

et al. 2005

American Journal of Physiology-Heart and Circulatory Physiology

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“…This secretory process is defined by protrusions or bleb emissions from the apical cytoplasm of the epithelium that form vesicular structures called exosomes, aposomes, or epididymosomes circulating in the lumen of the genital tract (Aumuller and Seitz, 1990). Some epididymosomeassociated proteins, such as CD52, glutathione peroxidase type 5, ubiquity, and macrophage migration inhibitory factor (MIF), are selectively transferred to spermatozoa during epididymal transit (Eickhoff et al, 2001;Sullivan et al, 2005). Hence, epididymosomes, which are characterized by their surrounding plasma membrane, are thought to be involved in the modification of spermatozoa during epididymal transit.…”

Section: Discussionmentioning

confidence: 99%

Bactericidal/Permeability‐Increasing Protein Is Associated With the Acrosome Region of Rodent Epididymal Spermatozoa

Yano

Matsuyama

Kaneko

et al. 2010

Journal of Andrology

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To elucidate the molecular mechanisms involved in sperm maturation during epididymal transit, we intended to isolate secretory molecules that are region-specifically expressed along the epididymis and secreted into the lumen of epididymal ducts. By using differential display screening and DNA sequence analyses, we isolated a rat bactericidal/permeability-increasing protein (BPI) possessing a signal sequence at its N-terminal, which was expressed in the caput region of epididymis, but not in the caudal region. Reverse transcription polymerase chain reaction analysis and in situ hybridization showed that rat BPI messenger RNA (mRNA) was highly expressed in caput epididymal epithelium and that its expression level was developmentally up-regulated. Confocal laser scanning microscopy with the anti-BPI antibody revealed that in both rats and mice, BPI protein was detected on granulelike structures in the lumen of both caput and cauda epididymal ducts, as well as at the sperm surface covering the acrosome region in spermatozoa freshly isolated from epididymis. Acrosome reaction induced by calcium ionophore A23187 in vitro brought about the disappearance of BPI on mouse spermatozoa. These data suggested that BPI, which is synthesized in caput epididymis and secreted into the lumen, is associated with not only the granulelike structures, but also the sperm surface covering the acrosome region, and that BPI bound to the acrosome region is extinguished by acrosome reaction. Possibly BPI bound to the sperm surface covering the acrosome region in rodent spermatozoa is involved in sperm maturation or fertilization.

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“…Studying the epithelium of rat epididymis, the principal cells have been delineated as the source of the cytokine, whereas the basal cells as well as the stromal cells were MIF negative [Eickhoff et al, 2001]. In addition, a differential distribution pattern with highest amounts of MIF in the caput region decreasing in more distal parts of the epididymis was described in that report, and MIF was also localized in vesicles detectable in the epididymal fl uid [Eickhoff et al, 2001].…”

mentioning

confidence: 91%

Immunohistochemical Detection of Macrophage Migration Inhibitory Factor in Fetal and Adult Bovine Epididymis: Release by the Apocrine Secretion Mode?

Eickhoff

Jennemann

Hoffbauer

et al. 2006

Cells Tissues Organs

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Originally defined as a lymphokine inhibiting the random migration of macrophages, the macrophage migration inhibitory factor (MIF) is an important mediator of the host response to infection. Beyond its function as a classical cytokine, MIF is currently portrayed as a multifunctional protein with growth-regulating properties present in organ systems beyond immune cells. In previous studies, we detected substantial amounts of MIF in the rat epididymis and epididymal spermatozoa, where it appears to play a role during post-testicular sperm maturation and the acquisition of fertilization ability. To explore its presence in other species not yet examined in this respect, we extended the range of studies to the bull. Using a polyclonal antibody raised against MIF purified from bovine eye lenses, we detected MIF in the epithelium of the adult bovine epididymis with the basal cells representing a prominently stained cell type. A distinct accumulation of MIF at the apical cell pole of the epithelial cells and in membranous vesicles localized in the lumen of the epididymal duct was obvious. In the fetal bovine epididymis, we also detected MIF in the epithelium, whereas MIF accumulation was evident at the apical cell surface and in apical protrusions. By immunoelectron microscopy of the adult bovine epididymis, we localized MIF in apical protrusions of the epithelial cells and in luminal membrane-bound vesicles that were found in close proximity to sperm cells. Although the precise origin of the MIF-containing vesicles remains to be delineated, our morphological observations support the hypothesis that they become detached from the apical surface of the epididymal epithelial cells. Additionally, an association of MIF with the outer dense fibers of luminal spermatozoa was demonstrated. Data obtained in this study suggest MIF release by an apocrine secretion mode in the bovine epididymis. Furthermore, MIF localized in the basal cells of the epithelium and in the connective tissue could be responsible for regulating the migration of macrophages in order to avoid contact of immune cells with spermatozoa that carry a wide range of potent antigens.

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Purification and Characterization of Macrophage Migration Inhibitory Factor as a Secretory Protein from Rat Epididymis: Evidences for Alternative Release and Transfer to Spermatozoa

Cited by 66 publications

References 32 publications

Macrophage migration inhibitory factor mediates late cardiac dysfunction after burn injury

Macrophage migration inhibitory factor mediates late cardiac dysfunction after burn injury

Bactericidal/Permeability‐Increasing Protein Is Associated With the Acrosome Region of Rodent Epididymal Spermatozoa

Immunohistochemical Detection of Macrophage Migration Inhibitory Factor in Fetal and Adult Bovine Epididymis: Release by the Apocrine Secretion Mode?

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