Neurons compute internal models of the physical laws of motion

A critical step in self-motion perception and spatial awareness is the integration of motion cues from multiple sensory organs that individually do not provide an accurate representation of the physical world. One of the best-studied sensory ambiguities is found in visual processing, and arises because of the inherent uncertainty in detecting the motion direction of an untextured contour moving within a small aperture. A similar sensory ambiguity arises in identifying the actual motion associated with linear accelerations sensed by the otolith organs in the inner ear. These internal linear accelerometers respond identically during translational motion (for example, running forward) and gravitational accelerations experienced as we reorient the head relative to gravity (that is, head tilt). Using new stimulus combinations, we identify here cerebellar and brainstem motion-sensitive neurons that compute a solution to the inertial motion detection problem. We show that the firing rates of these populations of neurons reflect the computations necessary to construct an internal model representation of the physical equations of motion.     

Biological indicators of cadmium exposure and toxicity

The increasing environmental and occupational exposure of populations to cadmium creates the need for biological indicators of cadmium exposure and toxicity. The advantages and disadvantages of monitoring blood cadmium, urinary, fecal, hair, and tissue cadmium, serum creatinine, beta 2-microglobulin, alpha 1-antitrypsin and other proteins, and urinary amino acids, enzymes, total proteins, glucose, beta 2-microglobulin, retinol-binding protein, lysozyme, and metallothionein are discussed. It is concluded that urinary cadmium, metallothionein and beta 2-microglobulin may be used together to assess cadmium exposure and toxicity.     

Cadmium as a trace element and cadmium binding components in human cells

Zusammenfassung Fötale menschliche Fibroblasten wurden in einem¹⁰⁹Cd und⁶⁵Zn enthaltenden Kultur medium gezÜchtet.¹⁰⁹Cd wurde in allen Zellen kontinuierlich absorbiert. Mit Gel-Filtration wurde der Zellsaft in 2 Komponenten aufgetrennt, die beide¹⁰⁹Cd enthielten. ähnliche,¹⁰⁹Cd bindende Komponenten wurden auch in Rattenleber-Homogenaten gefunden.     

Isolation of cadmium-binding proteins

Résumé Un procédé pour l'isolation des protéines combinées au Cd radioactif (^109Cd) a été mis au point. La méthode ne détruit pas les protéines. D'autres protéines ayant des affinités pour les métaux lourds pourront ainsi être isolées.     

Chronic cadmium intake results in dose-related excretion of metallothionein in urine

Urinary excretion of metallothionein was measured by radioimmunoassay in rats given drinking water containing 5 or 50 mg cadmium/l for up to 2 years. The metallothionein levels corresponded to the concentration of cadmium in the drinking water and increased linearly over the course of the study. These results demonstrate that urinary metallothionein is a sensitive biological indicator of oral cadmium exposure.     

Biological indicators of cadmium exposure and toxicity

Summary The increasing environmental and occupational exposure of populations to cadmium creates the need for biological indicators of cadmium exposure and toxicity. The advantages and disadvantages of monitoring blood cadmium, urinary, fecal, hair, and tissue cadmium, serum creatinine, ₂-microglobulin, ₁-antitrypsin and other proteins, and urinary amino acids, enzymes, total proteins, glucose ₂-microglobulin, retinol-binding protein, lysozyme, and metallothionein are discussed. It is concluded that urinary cadmium, metallothionein and ₂-microglobulin may be used together to assess cadmium, exposure and toxicity.     

Structure of the E. coli protein-conducting channel bound to a translating ribosome

Secreted and membrane proteins are translocated across or into cell membranes through a protein-conducting channel (PCC). Here we present a cryo-electron microscopy reconstruction of the Escherichia coli PCC, SecYEG, complexed with the ribosome and a nascent chain containing a signal anchor. This reconstruction shows a messenger RNA, three transfer RNAs, the nascent chain, and detailed features of both a translocating PCC and a second, non-translocating PCC bound to mRNA hairpins. The translocating PCC forms connections with ribosomal RNA hairpins on two sides and ribosomal proteins at the back, leaving a frontal opening. Normal mode-based flexible fitting of the archaeal SecYEbeta structure into the PCC electron microscopy densities favours a front-to-front arrangement of two SecYEG complexes in the PCC, and supports channel formation by the opening of two linked SecY halves during polypeptide translocation. On the basis of our observation in the translocating PCC of two segregated pores with different degrees of access to bulk lipid, we propose a model for co-translational protein translocation.     

Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism

The bacterial flagellum is a motile organelle, and the flagellar hook is a short, highly curved tubular structure that connects the flagellar motor to the long filament acting as a helical propeller. The hook is made of about 120 copies of a single protein, FlgE, and its function as a nano-sized universal joint is essential for dynamic and efficient bacterial motility and taxis. It transmits the motor torque to the helical propeller over a wide range of its orientation for swimming and tumbling. Here we report a partial atomic model of the hook obtained by X-ray crystallography of FlgE31, a major proteolytic fragment of FlgE lacking unfolded terminal regions, and by electron cryomicroscopy and three-dimensional helical image reconstruction of the hook. The model reveals the intricate molecular interactions and a plausible switching mechanism for the hook to be flexible in bending but rigid against twisting for its universal joint function.     

Similarities between metallothionein and low molecular weight testicular cadmium-binding protein

The incorporation of 35S-cysteine and 3H-glutamic acid was studied in mouse hepatic and renal metallothionein and in testicular cadmium-binding protein of similar molecular weight. Preferential incorporation of 35S-cysteine over 3H-glutamic acid was observed not only in hepatic and renal metallothionein, but also in testicular cadmium-binding protein. When the antigenic reactivity of these proteins was compared, all three proteins reacted with the metallothionein antibody. These similarities suggest that the low molecular weight testicular cadmium-binding protein is apparently metallothionein.