Abstract: The present disclosure relates to the use of the non-toxic proteolytic C fragment of tetanus toxin and plasmids encoding such protein fragment to increase muscle mass and/or muscle strength in a subject in need thereof. As such, methods of ameliorating the severity of a pathological condition characterized, at least in part, by a decreased amount, development, or metabolic activity of muscle are provided. The disclosed compositions and method are also useful for the treatment of condition in which increase in muscle mass and muscle strength are desirable, including cosmetic uses.

Abstract: The present invention relates to the therapeutic use of the encoding sequence of the carboxy-terminal domain of the heavy chain of the tetanus toxin and of the polypeptide encoded by said sequence, preferably for the treatment of amyotrophic lateral sclerosis (ALS).

Abstract: The present invention relates to the therapeutic use of the carboxy-terminal domain of the heavy chain of the tetanus toxin for the treatment of amyotrophic lateral sclerosis (ALS).

Abstract: The invention relates to methods based on the quantification of a set of biomarkers, preferably in biological samples isolated from skeletal muscle, for performing the diagnosis, prognosis and/or monitoring of muscular degeneration, preferably muscular degeneration caused by motor neuron diseases, more preferably amyotrophic lateral sclerosis (ALS); and to a kit for the diagnosis, prognosis and monitoring of said type of diseases. The method in the invention for the prognosis and/or monitoring of muscular degeneration makes it possible to determine the rate of progression of said degeneration (fast or slow rate of progression in relation to the normal rate of progression).

Abstract: The non-toxic proteolytic C fragment of tetanus toxin (TTC peptide) has the same ability to bind nerve cells and be retrogradely transported through a synapse as the native toxin. A hybrid protein encoded by the LacZ-TTC gene fusion retains the biological functions of both proteins in vivo, i.e. retrograde transynaptic transport of the TTC fragment and ?gal enzymatic activity. After intramuscular injection, enzymatic activity can be detected in motoneurons and connected neurons of brainstem areas. This strategy is useful for the delivery of a biological activity to neurons from the periphery to the central nervous system. Such a hybrid protein can also be used to map synaptic connections between neural cells.

Abstract: The present invention relates to the therapeutic use of the encoding sequence of the carboxy-terminal domain of the heavy chain of the tetanus toxin and of the polypeptide encoded by said sequence, preferably for the treatment of amyotrophic lateral sclerosis (ALS).

Abstract: The non-toxic proteolytic C fragment of tetanus toxin (TTC peptide) has the same ability to bind nerve cells and be retrogradely transported through a synapse as the native toxin. A hybrid protein encoded by the IacZ-TTC gene fusion retains the biological functions of both proteins in vivo, i.e. retrograde transynaptic transport of the TTC fragment and ?-gal enzymatic activity. After intramuscular injection, enzymatic activity could be detected in motoneurons and connected neurons of the brainstem areas. This strategy is useful for the delivery of a biological activity to neurons from the periphery to the central nervous system. Such a hybrid protein can also be used to map synaptic connections between neural cells.

Abstract: The non-toxic proteolytic C fragment of tetanus toxin (TTC peptide) has the same ability to bind nerve cells and be retrogradely transported through a synapse as the native toxin. A hybrid protein encoded by the lacZ-TTC gene fusion retains the biological functions of both proteins in vivo, i.e. retrograde transynaptic transport of the TTC fragment and -gal enzymatic activity. After intramuscular injection, enzymatic activity could be detected in motoneurons and connected neurons of the brainstem areas. This strategy is useful for the delivery of a biological activity to neurons from the periphery to the central nervous system. Such a hybrid protein can also be used to map synaptic connections between neural cells.

Abstract: The non-toxic proteolytic C fragment of tetanus toxin (TTC peptide) has the same ability to bind nerve cells and be retrogradely transported through a synapse as the native toxin. A hybrid protein encoded by the IacZ-TTC gene fusion retains the biological functions of both proteins in vivo, i.e. retrograde transynaptic transport of the TTC fragment and ?-gal enzymatic activity. After intramuscular injection, enzymatic activity could be detected in motoneurons and connected neurons of the brainstem areas. This strategy is useful for the delivery of a biological activity to neurons from the periphery to the central nervous system. Such a hybrid protein can also be used to map synaptic connections between neural cells.

Abstract: The non-toxic proteolytic C fragment of tetanus toxin (TTC peptide) has the same ability to bind nerve cells and be retrogradely transported through a synapse as the native toxin. A hybrid protein encoded by the IacZ-TTC gene fusion retains the biological functions of both proteins in vivo, i.e. retrograde transynaptic transport of the TTC fragment and &bgr;-gal enzymatic activity. After intramuscular injection, enzymatic activity could be detected in motoneurons and connected neurons of the brainstem areas. This strategy is useful for the delivery of a biological activity to neurons from the periphery to the central nervous system. Such a hybrid protein can also be used to map synaptic connections between neural cells.