Comparative studies of the age-related changes in protein synthesis in the rat pancreas and parotid gland

Kim, S. K.; Weinhold, Paul A.; Calkins, Debby W.; Hartog, V. W.

doi:10.1016/0531-5565(81)90012-7

Cited by 33 publications

(13 citation statements)

References 28 publications

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“…The incorporation of [~4C]leucine into CC13 COOH insoluble material was ~20°/0 lower (Table I). These data are similar to results reported previously by Kim and colleagues [27,28]. The incorporation of [3H]mannose into parotid gland protein, which over a 1-h time period represents assembly of N-linked oligosaccharides [16,17], was also reduced in cells from aged animals but to a greater extent than seen with leucine incorporation (~35%).…”

Section: Resultssupporting

confidence: 91%

N-linked protein glycosylation in the rat parotid gland during aging

Kousvelari

Banerjee

Murty

et al. 1988

Mechanisms of Ageing and Development

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N-Linked protein glycosylation was examined in vitro in dispersed rat parotid acinar cells from young adult (3-6 months) and aged (22-24 months) rats. A small decrease in general protein production was observed with cells from aged animals (approximately 20% lower incorporation of [14C]leucine into 10% CCl3 COOH insoluble protein during continuous pulse labeling). Incorporation of [3H]mannose into N-linked glycoproteins by aged cells was further reduced (approximately 35%). Similarly microsomal membranes from parotid glands of aged animals showed approximately 50% reduction in the synthesis of mannosylphosphoryl dolichol, a key intermediate in the dolichol pathway of protein N-glycosylation. Man-P-Dol synthase, the microsomal enzyme responsible for production of this saccharide-lipid, displayed no change in apparent Km for GDP-mannose when preparations from aged animals were utilized, but did show approximately 50% reduction in Vmax. Following beta-adrenoreceptor activation, cells from both young adult and aged glands showed increased N-linked protein glycosylation almost to the same extent (approximately 2-fold). The data suggested that in aged rat parotid cells there is a basal reduction of activity in the pathway responsible for asparagine-linked protein glycosylation, but that following exocytotic stimuli this pathway responds in a manner comparable to cells from young adult glands.

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Section: Resultssupporting

confidence: 91%

N-linked protein glycosylation in the rat parotid gland during aging

Kousvelari

Banerjee

Murty

et al. 1988

Mechanisms of Ageing and Development

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“…One group of investigators has reported decreased collagen production (Johnson et al, 1986) and variable changes in the production of glycosaminoglycans as a function of the age of the donor (Bartold et al, 1986) in gingival fibroblast cultures of comparable in vitro age. These observations are consistent with the reported overall decrease of protein synthesis in vivo (Kim et al, 1981). Although a causal relationship between the observed changes in the production of these matrix molecules and the susceptibility to this chronic inflammatory condition remains to be established, it is very likely that these alterations of cellular activity are causally related to decrements of the functional competence of tissues in vivo.…”

Section: Relevance To Aging In Vivosupporting

confidence: 90%

The Cultured Diploid Fibroblast as a Model for the Study of Cellular Aging

Norwood

Pendergrass

1992

Critical Reviews in Oral Biology & Medicine

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The limited proliferative potential of the cultured human diploid fibroblast is now well established. A number of biological correlates suggest that this culture system is a model for the study of aging at the cellular level. The mechanism(s) that causes the loss of proliferative activity is unknown; the results of some recent studies indicate that specific genes may play a pivotal role in cellular aging in vitro. The extent to which changes in proliferative functions are causally related to aging in vivo is currently under investigation.

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“…The reduction of this cytoplasmic compartment in senescent cells implies an impaired ability to produce polypeptide secretory products, and is correlated with the reduced number and size of apical secretion granules, and with the lower concentrations of EGF and protease detected chemically. A decreased capacity for protein synthesis with age has been documented for other exocrine glands, such as the rat parotid gland and pancreas [16][17][18] and dog pancreas [23]. Kim and coworkers [16][17][18] also report that in spite of considerable declines in the content of alpha amylase in the parotid gland and pancreas of 30 month-old rats, cytologic changes were not very dramatic, and acinar cells all contained secretion granules similar in size to those seen at younger ages.…”

Section: Discussionmentioning

confidence: 87%

Age‐Related Changes in EGF and Protease in Submandibular Glands of C57BL/6J Mice^1,⁴

1982

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The submandibular glands of male C57BL/6J mice were studied cytologically and chemically at the following ages (months): 1–1.5, 6–8, 12–13, 28–32. The relative proportion of granular convoluted tubules (GCT) as well as the size and content of secretion granules of GCT cells, progressively increased throughout the first year of life. Correspondingly, the concentration within the glands of two GCT cell products, epidermal growth factor (EGF) and protease, also steadily increased. In senescent glands, GCTs formed relatively less of the gland parenchyma and were composed of shorter cells with reduced amounts of secretory granules. The concentration of EGF was reduced to 17% of its peak value at one year, while protease activity declined to 50% of its peak value. These morphologic and chemical findings imply a functional impairment in submandibular glands of the mouse with senescence.

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Comparative studies of the age-related changes in protein synthesis in the rat pancreas and parotid gland

Cited by 33 publications

References 28 publications

N-linked protein glycosylation in the rat parotid gland during aging

N-linked protein glycosylation in the rat parotid gland during aging

The Cultured Diploid Fibroblast as a Model for the Study of Cellular Aging

Age‐Related Changes in EGF and Protease in Submandibular Glands of C57BL/6J Mice^1,⁴

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Comparative studies of the age-related changes in protein synthesis in the rat pancreas and parotid gland

Cited by 33 publications

References 28 publications

N-linked protein glycosylation in the rat parotid gland during aging

N-linked protein glycosylation in the rat parotid gland during aging

The Cultured Diploid Fibroblast as a Model for the Study of Cellular Aging

Age‐Related Changes in EGF and Protease in Submandibular Glands of C57BL/6J Mice1,4

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Age‐Related Changes in EGF and Protease in Submandibular Glands of C57BL/6J Mice^1,⁴