Standardized and extended catalog of major proteins of the human kidney

A new version of a two-dimensional electrophoretic catalog of proteins of the human kidney and of various morphological and functional structures of the human kidney is presented; it contains information about 179 polypeptides. The following proteins were identified: crystallin, albumin, mitochondrial Superoxide dismutase, actin, fatty acid-binding protein, alpha-ATP-synthase, and transferrin. Some protein groups are specific for certain morphological structures

Proteomic analysis of human skeletal muscle (m. vastus lateralis) proteins: Identification of 89 gene expression products

Proteins from bioptates and autoptates of human skeletal muscle m. vastus lateralis were separated by O'Farrell two-dimensional gel electrophoresis (2DE). MALDI-TOF MS and MS/MS enabled identification of 89 protein spots as expression products of 55 genes. A modification of the O'Farrell's method including non-equilibrium electrophoresis in a pH gradient allowed detection - among major sarcomeric, mitochondrial, and cytosolic proteins - of several proteins, such as PDZ- and LIM domain-containing ones (pI > 8.70), fragments of known proteins, and a stable complex of heavy and light ferritin chains. The data underlie further studies of human skeletal muscle proteins in terms of molecular mechanisms of some physiological and pathological processes. © 2009 Pleiades Publishing, Ltd

Standardized and extended catalog of major proteins of the human kidney

A new version of a two-dimensional electrophoretic catalog of proteins of the human kidney and of various morphological and functional structures of the human kidney is presented; it contains information about 179 polypeptides. The following proteins were identified: crystallin, albumin, mitochondrial Superoxide dismutase, actin, fatty acid-binding protein, alpha-ATP-synthase, and transferrin. Some protein groups are specific for certain morphological structures

Proteomic analysis of human skeletal muscle (m. vastus lateralis) proteins: Identification of 89 gene expression products

Proteins from bioptates and autoptates of human skeletal muscle m. vastus lateralis were separated by O'Farrell two-dimensional gel electrophoresis (2DE). MALDI-TOF MS and MS/MS enabled identification of 89 protein spots as expression products of 55 genes. A modification of the O'Farrell's method including non-equilibrium electrophoresis in a pH gradient allowed detection - among major sarcomeric, mitochondrial, and cytosolic proteins - of several proteins, such as PDZ- and LIM domain-containing ones (pI > 8.70), fragments of known proteins, and a stable complex of heavy and light ferritin chains. The data underlie further studies of human skeletal muscle proteins in terms of molecular mechanisms of some physiological and pathological processes. © 2009 Pleiades Publishing, Ltd

Studies of the pathogenesis of slow neuroinfections using proteomic techniques

The etiology and pathogenesis of amyotrophic lateral sclerosis (ALS) are still unknown. Autoimmune mechanisms are considering to be possible causes of ALS, among several other possible mechanisms. In this paper, we describe the determination of autoantibodies against proteins of the brain motor zone and skeletal muscular system in the sera of patients suffering from ALS. Autoantibodies against carbonyl reductase 1, α-enolase, 2′,3′-phosphodiesterase of cyclic nucleotides, and pyruvate kinase 3 (isoform 2) were primarily found in the motor zone, whereas those against muscular creatine phosphokinase, myoglobine, carboanhydrase III, and troponin 1 of the fast type were identified in the skeletal muscle in the majority of patients with ALS. In addition, dynamic changes in the structure of the troponin complex were demonstrated in the tissue of skeletal muscle. The significance of the presence of autoantibodies against proteins of the brain motor zone in the sera of ALS patients is unknown. These autoantibodies most likely appeared as a secondary immunological effect of neuron damage. We can also conjecture that they accelerate the affection of muscle tissue and motoneurons. © Pleiades Publishing, Ltd. 2007

Studies of the pathogenesis of slow neuroinfections using proteomic techniques

The etiology and pathogenesis of amyotrophic lateral sclerosis (ALS) are still unknown. Autoimmune mechanisms are considering to be possible causes of ALS, among several other possible mechanisms. In this paper, we describe the determination of autoantibodies against proteins of the brain motor zone and skeletal muscular system in the sera of patients suffering from ALS. Autoantibodies against carbonyl reductase 1, α-enolase, 2′,3′-phosphodiesterase of cyclic nucleotides, and pyruvate kinase 3 (isoform 2) were primarily found in the motor zone, whereas those against muscular creatine phosphokinase, myoglobine, carboanhydrase III, and troponin 1 of the fast type were identified in the skeletal muscle in the majority of patients with ALS. In addition, dynamic changes in the structure of the troponin complex were demonstrated in the tissue of skeletal muscle. The significance of the presence of autoantibodies against proteins of the brain motor zone in the sera of ALS patients is unknown. These autoantibodies most likely appeared as a secondary immunological effect of neuron damage. We can also conjecture that they accelerate the affection of muscle tissue and motoneurons. © Pleiades Publishing, Ltd. 2007