16 research outputs found
Formation of calcium pyrophosphate crystals in vitro: implications for calcium pyrophosphate crystal deposition disease (pseudogout)
Proteoglycans from the vertebral cartilage of the clearnose skate, Raja eglanteria: Inhibition of hydroxyapatite formation
Inhibition of calcium phosphate mineral growth by proteoglycan aggregate fractions in a synthetic lymph
Patterns of morphological variability in reintroduced populations with two beaver subspecies Castor fiber orientoeuropaeus and Castor fiber belorussicus (Castoridae, Rodentia) as an example
Electrolytes of isolated epiphyseal chondrocytes, matrix vesicles, and extracellular fluid
GS32, a Novel Golgi SNARE of 32 kDa, Interacts Preferentially with Syntaxin 6
Syntaxin 1, synaptobrevins or vesicle-associated membrane proteins, and the synaptosome-associated protein of 25 kDa (SNAP-25) are key molecules involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. We report here the molecular, cell biological, and biochemical characterization of a 32-kDa protein homologous to both SNAP-25 (20% amino acid sequence identity) and the recently identified SNAP-23 (19% amino acid sequence identity). Northern blot analysis shows that the mRNA for this protein is widely expressed. Polyclonal antibodies against this protein detect a 32-kDa protein present in both cytosol and membrane fractions. The membrane-bound form of this protein is revealed to be primarily localized to the Golgi apparatus by indirect immunofluorescence microscopy, a finding that is further established by electron microscopy immunogold labeling showing that this protein is present in tubular-vesicular structures of the Golgi apparatus. Biochemical characterizations establish that this protein behaves like a SNAP receptor and is thus named Golgi SNARE of 32 kDa (GS32). GS32 in the Golgi extract is preferentially retained by the immobilized GSTâsyntaxin 6 fusion protein. The coimmunoprecipitation of syntaxin 6 but not syntaxin 5 or GS28 from the Golgi extract by antibodies against GS32 further sustains the preferential interaction of GS32 with Golgi syntaxin 6