Cytochemical localization of Ca++-ATPase activity in the lateral cochlear wall of the guinea pig

1987 ◽  
Vol 243 (6) ◽  
pp. 395-400 ◽  
Author(s):  
T. Yoshihara ◽  
M. Igarashi
Keyword(s):  
Guinea Pig ◽  
Atpase Activity ◽  
Cytochemical Localization

scholarly journals Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical myosin ATPase and anti-myosin monoclonal antibodies.

1990 ◽  
Vol 38 (2) ◽  
pp. 257-265 ◽  
Author(s):  
L Gorza
Keyword(s):  
Monoclonal Antibodies ◽  
Guinea Pig ◽  
Atpase Activity ◽  
High Activity ◽  
Skeletal Muscles ◽  
Enzyme Histochemistry ◽  
Myosin Atpase ◽  
Myosin Atpase Activity ◽  
Combined Use

A novel type of myosin heavy chain (MHC), called 2X, has been recently identified in type 2 fibers of rat skeletal muscles using an immunochemical approach. In the present study, the same panel of anti-MHC monoclonal antibodies was used in immunohistochemistry combined with enzyme histochemistry to identify and compare type 2X fibers in hindlimb skeletal muscles of rat, mouse, and guinea pig. Immunohistochemistry shows that 2X MHC is localized in a large subset of type 2 fibers and is co-expressed with 2A or 2B MHC in a small number of fibers. Enzyme histochemistry shows that type 2X fibers display low myosin ATPase activity after pre-incubation at pH 4.3 and high activity after paraformaldehyde pre-incubation at pH 10.4. After pre-incubation at pH 4.6, myosin ATPase shows intermediate and high activity in rat and mouse 2X fibers, respectively, whereas it is low in guinea pig 2X fibers. Succinate dehydrogenase displays moderate to high activity in 2X fibers of all species. Taken together, these staining patterns allow this novel fiber population to be distinguished from the other type 2 fibers using only enzyme histochemistry. Nevertheless, the combined use of immuno- and enzyme histochemistry prevents incorrect fiber typing due to the interspecies variability of myosin ATPase activity among the correspondent fiber types, and completely modifies the presently used classification of mouse type 2 fibers.

scholarly journals Effects of divalent cations and La3+ on contractility and ecto-ATPase activity in the guinea-pig urinary bladder

1995 ◽  
Vol 114 (3) ◽  
pp. 632-639 ◽  
Author(s):  
Airat U. Ziganshin ◽  
Lilia E. Ziganshina ◽  
Charles H.V. Hoyle ◽  
Geoffrey Burnstock
Keyword(s):  
Urinary Bladder ◽  
Guinea Pig ◽  
Atpase Activity ◽  
Divalent Cations

scholarly journals Cytochemical localization of ecto-ATPases in rat neurohypophysis.

1996 ◽  
Vol 44 (2) ◽  
pp. 103-111 ◽  
Author(s):  
S Thirion ◽  
J D Troadec ◽  
G Nicaise
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Atpase Activity ◽  
Outer Surface ◽  
Nerve Endings ◽  
Glutaraldehyde Fixation ◽  
Cytochemical Localization ◽  
Cytochemical Method ◽  
Ca Pump ◽  
Dependent Atpase

We studied the distribution of Ca(2+)- or Mg(2+)-dependent ATPase activity in rat neurohypophysis using the lead cytochemical method of Ando et al. In electron microscopy, precipitates were found lining the outer surface of the plasma membrane surrounding nerve endings and pituicytes. These precipitates were believed to represent the activity of ecto-ATPases (as opposed to Ca pump ATPases) for the following reasons: there was equal activation by Ca2+ in the absence of Mg2+ or Mg2+ in the absence of Ca2+; the effects of the two ions were not additive; there was activation by ATP or GTP; and there was resistance to glutaraldehyde fixation, to high (10 mM) Ca2+ concentrations, and to various inhibitors such as NEM, vanadate, oligomycin, quercetin, p-chloromercuribenzoate, ouabain, and levamisole. Cytosolic activity observed in certain nerve endings in the same conditions of incubation but more sensitive to NEM is also described and discussed.

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