Search PubMedSearch

PubMed · 2771433

[Cestode lysosomes].

Abstract

By differential centrifugation method a lysosomal fraction was obtained from five species of cestodes, which possesses the highest specific activity of acidic phosphatases as compared to other subcellular fractions. By isopyknic centrifugation in the density gradient of saccharose the lysosomal fraction is divided into primary and secondary lysosomes. Lysosomes of cestodes are similar to those of vertebrate animals in the character of fractional distribution of acidic phosphatase, sedimentation abilities and sensitivity of membranes to triton X-100.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

L P Smirnov, V V Bogdan. [Cestode lysosomes].. https://pubmed.ncbi.nlm.nih.gov/2771433/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

A novel 35 kDa frog liver acid metallophosphatase.

The lower molecular weight (35 kDa) acid phosphatase from the frog (Rana esculenta) liver is a glycometalloenzyme susceptible to activation by reducing agents and displaying tartrate and fluoride resistance. Metal chelators (EDTA, 1,10-phenanthroline) inactivate the enzyme reversibly in a time- and temperature-dependent manner. The apoenzyme is reactivated by divalent transition metal cations, i. e. cobalt, zinc, ferrous, manganese, cadmium and nickel to 130%, 75%, 63%, 62%, 55% and 34% of the original activity, respectively. Magnesium, calcium, cupric and ferric ions were shown to be ineffective in this process. Metal analysis by the emission spectrometry method (inductively coupled plasma-atomic emission spectrometry) revealed the presence of zinc, iron and magnesium. The time course of the apoenzyme reactivation, the stabilization effect and the relatively high resistance to oxidizing conditions indicate that the zinc ion is crucial for the enzyme activity. The presence of iron was additionally confirmed by the visible absorption spectrum of the enzyme with a shoulder at 417 nm and by the electron paramagnetic resonance line of high spin iron(III) with geff of 2.4. The active center containing only zinc or both zinc and iron ions is proposed. The frog liver lower molecular weight acid phosphatase is a novel metallophosphatase of lower vertebrate origin, distinct from the mammalian tartrate-resistant, purple acid phosphatases.

Acid Phosphatase

Modulation of monocytic cell activity and virus susceptibility during differentiation into macrophages.

A major component of innate immune responses relies on monocytes and macrophages, virus infection of which will pose a particular problem for immunological defense. Consequently, the monocytic cell differentiation pathway was analyzed in terms of cellular modulations therein and their relation to monocytotropic virus infection. Differentiation was characterized by down-regulation of CD14, MHC Ags, the monocytic SWC1 marker, and p53; concomitant up-regulation of the SWC9 macrophage marker, a putative porcine CD80 (detected with anti-human CD80 Ab), and acid phosphatase secretion were also characteristic. Elevated phagocytic and endocytic activities as well as endosomal/lysosomal acidification were identified as being important to the macrophage. In contrast, monocytes possessed high accessory activity. This was multifactorial, concomitantly requiring 1) high MHC Ag expression; 2) enzyme activity of esterase, peroxidase, myeloperoxidase, and 5' nucleotidase in preference to glucosidase, galactosidase, and glucuronidase; and 3) elevated capacity for spontaneous IL-1 production. Only with all parameters was efficient stimulation of Ag-specific lymphocytes possible. These results point to a continuous process during differentiation, involving inter-related characteristics linking the more accessory monocyte to the scavenger macrophage, both in vitro and in vivo. Of particular interest was how these characteristics related to monocytotropic virus infection, and how a particular virus could show a clear preference for the differentiating macrophages. Such results not only further our understanding of porcine immunology, but also provide evidence and a potential model for the determination and characterization of monocytotropic virus-host cell interactions.

Acid Phosphatase

Macrophage secretory products influence the survival of statoacoustic neurons.

Prior studies have shown that macrophages are recruited to sites of injury or infection in the sensory organs of the inner ear, but the effects of macrophages and their cytokine secretory products on the sensory structures of the ear are not known. In the present study, cultures of dissociated statoacoustic neurons were incubated with selected macrophage secretary products and the numbers of surviving neurons after 48 h in vitro were quantified. Results indicate that two macrophage secretary products, interleukin 1 and fibroblast growth factor 2, can enhance the survival of statoacoustic neurons, while another cytokine, tumour necrosis factor-alpha can diminish the survival of those neurons. Also, numerous macrophages were present in both cytokine-treated and control cultures. The findings suggest that macrophages may influence the survival of the sensory neurons of the inner ear.

Acid Phosphatase