Immunoregulatory properties of the cytokine IL-34

Interleukin-34 is a cytokine with only partially understood functions, described for the first time in 2008. Although IL-34 shares very little homology with CSF-1 (CSF1, M-CSF), they share a common receptor CSF-1R (CSF-1R) and IL-34 has also two distinct receptors (PTP-ζ) and CD138 (syndecan-1). To make the situation more complex, IL-34 has also been shown as pairing with CSF-1 to form a heterodimer. Until now, studies have demonstrated that this cytokine is released by some tissues that differ to those where CSF-1 is expressed and is involved in the differentiation and survival of macrophages, monocytes, and dendritic cells in response to inflammation. The involvement of IL-34 has been shown in areas as diverse as neuronal protection, autoimmune diseases, infection, cancer, and transplantation. Our recent work has demonstrated a new and possible therapeutic role for IL-34 as a Foxp3⁺ Treg-secreted cytokine mediator of transplant tolerance. In this review, we recapitulate most recent findings on IL-34 and its controversial effects on immune responses and address its immunoregulatory properties and the potential of targeting this cytokine in human.     

Synaptic glomeruli in the thalamus of the rat: Three-dimensional relationships between glomerular components

Résumé L'organisation tridimensionelle des glomérules synaptiques enveloppés dans les processus astrocytiques du thalamus somatosensoriel du rat a été étudié par microscopie électronique. Un glomérule entier a été reconstruit et divers paramètres des rapports synaptiques et non-synaptiques entre les éléments constitutifs ont été mesurés.     

Enhancement of anaphylaxis of isolated smooth muscle by adenosine phosphates and inhibition of anaphylactic mechanisms by adenosine-3′,5′-cyclic monophosphate

Zusammenfassung Zyklisches 3,5-Adenosinmonophosphat hindert in vitro die Anaphylaxis des glatten Muskels vom Meerschweinchenuterus, während Adenosin und Adenosin-5-Monophosphat die anaphylaktische Reaktion erhöhen.     

Inhibition of angiotensin-converting enzyme by analogs of peptides fromBothrops jararaca venom

Zusammenfassung Nachweis mit Analogen der im Gifte vonBothrops jararaca gefundenen Peptide, dass die Inhihibition des Angiotensins «converting enzyme» von zwei eindeutigen Teilsequenzen dieser Peptide abhängig ist. Die hohe spezifische kompetitive Inhibition, hervorgerufen durch die Peptide vonBothrops jararaca, wird der Bindung ihrer Tripeptidreste vom Carboxyterminus mit dem aktiven Zentrum des Enzyms zugeschrieben, die in gleicher Weise wie die Peptidsubstrate mit dem Enzym gebunden werden. Die Wirksamkeit der Giftpeptide hängt von der Bindung eines zweiten Teiles der Peptide mit dem Enzym ab.