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J P Labbe

Publications and source records attributed to J P Labbe.

14 recordsLinked to original sources
PubMed2003

Formation of multiple complexes between beta-dystroglycan and dystrophin family products.

Beta-dystroglycan is expressed in a wide variety of tissues and has generally been reported with an Mr of 43 kDa, sometimes accompanied with a 31 kDa protein assumed to be a truncated product. This molecule was recently identified as the anomalous beta-dystroglycan expressed in various carcinoma cell lines. We produced and characterized a G5 polyclonal antibody specific to beta-dystroglycan that is directed against the C-terminal portion of the molecule. We provide evidence that beta-dystroglycan may vary in size and properties by studying different Xenopus tissues. Besides normal beta-dystroglycan with an Mr of 43 kDa in smooth and cardiac muscle and sciatic nerve extracts, we found it in skeletal muscle and brain proteins with an Mr of 38 and 65 kDa, respectively. Glycosylation properties and proteolytic susceptibilities of these different beta-dystroglycans are analysed and compared in this work. Crosslinking experiments with various beta-dystroglycan preparations obtained from skeletal and cardiac muscles and brain gave rise to specific new covalent products with Mr of 125 kDa (doublet band), or 120 and 130 kDa, or 140 and 240 kDa, respectively. We provide evidence, using various similar beta-dystroglycan preparations, that the immunoprecipitation procedure with G5 specific polyclonal antibody allows consistent pelleting of various dystrophin-family isoforms. Skeletal muscles from Xenopus reveals the presence of two distinct beta-dystroglycan complexes, one with dystrophin and another one which involves alpha-dystrobrevin. Cardiac muscle and brain from Xenopus are shown to contain three beta-dystroglycan complexes related to various dystrophin-family isoforms. Dystrophin or alpha-dystrobrevin or Dp71 were found in cardiac muscle and dystrophin or Dp180 or Up71 in brain. This variability in the relationship between beta-dystroglycan and dystrophin-family isoforms suggests that each protein--currently known as dystrophin associated protein--could not be present in each of these complexes.

Animals↗
PubMed1992

Efficiency of cleaning agents for an inorganic membrane after milk ultrafiltration.

Cleaning of inorganic membranes after ultrafiltration (UF) of skim milk has been assessed using hydraulic, physicochemical and spectroscopic (i.r. and X-ray photoelectron spectroscopy) measurements. A cleaning sequence using hypochlorite alone or hypochlorite followed by HNO3 restored the membrane hydraulic resistance, in contrast to cleaning with HNO3 alone. When using NaOH, addition of Ca complexants (EDTA, gluconate, tripolyphosphate) and surfactants was required to obtain similar results. Three types of criteria (hydraulic, kinetic, chemical) are available to assess the effect of the sequestrant and surfactant types. In all the cases studied, traces of protein and Ca were detected on and within the membrane after cleaning. Nevertheless, it was concluded that it is possible to develop a single-step alkaline product to clean inorganic milk UF membranes if suitable surfactants and Ca sequestrants are included in its formula.

Animals↗
PubMed1991

Sarcomeric disorganization in post-mortem fish muscles.

1. The post-mortem evolution of protein pattern in fish striated muscle was followed by SDS-PAGE, after different conditions of storage time and temperature. 2. Sarcoplasmic and sarcomeric fractions were analyzed respectively by low and high ionic strength extractions of fish muscle samples. 3. No evident modification of electrophoretic patterns was observed during the pre-rigor mortis period. 4. The high mol. wt proteins titin and nebulin were highly sensitive to proteolysis during the rigor mortis period. 5. Myosin extraction was predominantly influenced by the storage temperature. The myosin content of the extracts decreased during the rigor mortis period at storage temperatures greater than 8 degrees C. 6. alpha-Actinin was very resistant to proteolysis, but could be released from Z-disc structure during post-mortem aging.

Actinin↗
PubMed1980

Photoaffinity labelling of arginine kinase and creatine kinase with a gamma-P-substituted arylazido analogue of ATP.

1. An ATP analogue with a photoactivated azide group attached to the gamma-phosphate via an amide bond, ATP gamma-p-azidoanilide, appeared to have potential use as a photoaffinity label for the nucleotide-binding regions of ATP: guanidine phosphotransferases. Upon photolysis in the presence of lobster muscle arginine kinase and rabbit muscle creatine kinase, the analogue is converted to a potent inhibito of these two kinases. This photo-dependent inhibition is specific as it cannot be induced by azidoaniline, a mixture of azidoaniline and ATP or by ATP gamma-p-aminoanilide. Preirradiated under suitable conditions, the photoanalogue still shows a transitory inhibitory effect which, however, slowly vanishes with time (t0.5 = 3 h). 2. The photoinhibition is significantly decreased by the presence of ATP or ADP but is completely prevented by the addition of a mixture of nucleotide and guanidine substrates. Differential spectroscopy and affinity chromatography on Sepharose-ATP demonstrated the inability of photoinactivated arginine kinase and creatine kinase to recognize their nucleotide substrates. 3. Experiments with [14C]ATP gamma-p-azidoanilide indicated that photolysis is associated with an irreversible and stoichiometric binding of the ATP analogue to the enzymes. Autoradiographs made with the peptide maps corresponding to the tryptic digests of each 14C-labelled photomodified enzyme showed an unexpected highly specific labelling of the proteins. 4. Thiiol titrations of the kinases which have been subjected to various photolysis conditions led to the conclusion that the arylnitrene moiety of the photoanalogue is covalently attached to the single reactive cysteinyl side chain present in the active-site region of the two homologous kinases. This amino acid residue appears, therefore, to be located near the phosphate chain binding subsite occupied by the ATP analogue and probably also by the natural nucleotide substrates.

Adenosine Triphosphate↗
PubMed1977

[Transitory dyslexia related to hematoma of the left temporal lobe in a 14-year-old adolescent].

A hematoma limited to the median region of the second left temporal convolution was the factor of an involvement of written language which rapidly set in in a 14 years old adolescent. The type of disorders observed are quite superimposable on dyslexia in children. After evacuation of the hematoma, the reading disorders disappeared, as was proved by normalization of the leximetric test.

Adolescent↗