Intracellular Distribution of a Primate-Specific Esterase in Cultured Cells and Tissues

Whole saliva of 59 healthy persons was used for determination of esterase activity. The pattern of esterase was studied by means of isoelectrofocusing on thin-layer acrylamide gels. The esterases found in whole saliva are suggested to be derived from the cells of the tissue in the oral cavity. This origin is indicated (e.g.) by comparison between isoelectrophoretic esterase patterns of whole saliva, submandibular saliva, gingival biopsy and fibroblast culture. Antisera against partially purified saliva esterases were produced in rabbits. These sera, used in immunoelectro- osmophoresis, gave esterase-active immunoprecipitate against whole saliva, the watersoluble material of disrupted gingival biopsy and fibroblast culture, but not against the material of the bacteria, Streptococcus sanguis. Streptococcus mutans, Streptococcus mitis, Actinomyces viscosus and Lactobacillus fermentum.

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“…Vladuti and Rose (26) suggested that the ester ases may influence the permeability of the microsome membrane and take part in cell division.…”

Section: Immunoelectro-osmophoresis Of Esterases From Different Sourcesmentioning

confidence: 99%

Origin of Esterases in Human Whole Saliva

Lindqvist¹,

Nord²,

Söder³

1977

Enzyme

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“…Nonspecific esterase is thought to be synthesized and transported via the same route as acid phosphatase (Kukletova et at., 1974] and it is frequently found at the same intracellular site as the latter, namely, in the lysosomes [Holt 1963;Deimling & Madreiter, 1972;Vladutin & Rose, 1974]. It has been suggested repeatedly that the enzyme plays a role in digestion [Clements, 1967;Ryberg, 1973] specifically in fat mobilization [Bongers & Nogge, 1970;Sudderruddin & Tan, 1973;Geering & Freyvogel, 1974].…”

Section: Discussionmentioning

confidence: 99%

Rotifer Symposium IV

1987

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“…In the earliest stage of our research we were unable to find any gross antigenic differences between young and aging WI-38 cells. However, we noted a subtle change in the kinetic behavior of the enzymes toward various in hibitors in the late passage cells [Wang et al, 1970], More recently, we discovered that one of the lysosomal esterase isozymes is no longer produced in SV40-transformed WI-38 cells [Bartholomew et al, 1969;Vladutiu and Rose, 1974]. Therefore, we have looked at lysosomal enzyme activity during the growth and aging of WI-38 cells by means of elaborate specific immunochemical quantitation methods for lysosomal enzymes [Therrien et al, 1971;M ilisauskas and Rose, 1973;Milisauskas et al, 1974].…”

Section: Functional Changes In Aging Cellsmentioning

confidence: 99%

<i>In vitro </i>Senescence of Mammalian Cells

Choe¹,

Rose²

1976

Gerontology

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This review discusses the molecular and cytokinetic aspects of cellular aging of human diploid fibroblasts. Despite a large amount of data, the basis of their limited life span has not been defined. A replicative defect in aging cells lies in the mechanism(s) that initiates DNA synthesis, and the control of this mechanism(s) is mediated through an alteration in the synthesis of specific RNA and protein molecules. Two major groups of hypotheses have been offered to explain these findings. The differentiation hypotheses are based on the concept of a ‘biological clock’, while error hypotheses presuppose defects in genetic transcription or translation.

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Intracellular Distribution of a Primate-Specific Esterase in Cultured Cells and Tissues

Cited by 10 publications

References 15 publications

Origin of Esterases in Human Whole Saliva

Origin of Esterases in Human Whole Saliva

Rotifer Symposium IV

<i>In vitro </i>Senescence of Mammalian Cells

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