Lysosomal enzymes in normal and leukemic B lymphocytes

Kraaijenhagen, Rob J.; Schipper-Kester, Gerda P.M.; Rijksen, Gert; Gast, Gijsbert C. de; Staal, Gerard E.J.

doi:10.1016/0009-8981(82)90012-2

Cited by 15 publications

(2 citation statements)

References 11 publications

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“…Other reports have identified pathophysiological effects of decline or increase in ARSB activity in association with: uterine leiomyomas [increased ARSB in small (<10 g), decreased in large (>100 g) [ 103 ]; increased serum ARSB activity in bullous pemphigoid [ 170 ]; increased ARSB activity in Wharton’s jelly from pre-eclampsia samples [ 171 ]; increased serum ARSB in nasal allergy, but reduced in severe obstruction [ 172 ]; reduced ARSB in lymphocytes from chronic lymphocytic leukemia [ 173 ]; and increased ARSB and a phosphorylated form of ARSB in peripheral leukocytes in chronic myelogenous leukemia [ 174 ].…”

Section: Diseases With Deficiency Of Arylsulfatase Bmentioning

confidence: 99%

Profound Impact of Decline in N-Acetylgalactosamine-4-Sulfatase (Arylsulfatase B) on Molecular Pathophysiology and Human Diseases

Tobacman

Bhattacharyya

2022

IJMS

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The enzyme N-acetylgalactosamine-4-sulfatase (Arylsulfatase B; ARSB) was originally identified as a lysosomal enzyme which was deficient in Mucopolysaccharidosis VI (MPS VI; Maroteaux-Lamy Syndrome). The newly directed attention to the impact of ARSB in human pathobiology indicates a broader, more pervasive effect, encompassing roles as a tumor suppressor, transcriptional mediator, redox switch, and regulator of intracellular and extracellular-cell signaling. By controlling the degradation of chondroitin 4-sulfate and dermatan sulfate by removal or failure to remove the 4-sulfate residue at the non-reducing end of the sulfated glycosaminoglycan chain, ARSB modifies the binding or release of critical molecules into the cell milieu. These molecules, such as galectin-3 and SHP-2, in turn, influence crucial cellular processes and events which determine cell fate. Identification of ARSB at the cell membrane and in the nucleus expands perception of the potential impact of decline in ARSB activity. The regulation of availability of sulfate from chondroitin 4-sulfate and dermatan sulfate may also affect sulfate assimilation and production of vital molecules, including glutathione and cysteine. Increased attention to ARSB in mammalian cells may help to integrate and deepen our understanding of diverse biological phenomenon and to approach human diseases with new insights.

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Section: Diseases With Deficiency Of Arylsulfatase Bmentioning

confidence: 99%

Profound Impact of Decline in N-Acetylgalactosamine-4-Sulfatase (Arylsulfatase B) on Molecular Pathophysiology and Human Diseases

Tobacman

Bhattacharyya

2022

IJMS

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“…We do not yet know enough about the impairment of LDL metabolism in cancer cells to ascertain whether the origin of this defect lies in the internalization or the intracellular degradation of LDL. Kraaijenhagen et al [6] showed that the activities of all enzymes, except acid phosphatase, were significantly lower in leukemic B lymphocytes than in normal lymphocytes, while Anderson et al [7] demonstrated that cancerous A-431 cells have an abnormally small capacity for internalizing LDL. We previously found that the uptake of '"I-LDL by L2C cells reaches a plateau in 4-5 h but we were unable to conclude which of the two processes (internalization or degradation) was defective [2].…”

mentioning

confidence: 99%

Internalization of low‐density‐lipoprotein‐specific receptors in leukemic guinea pig lymphocytes

Sainte‐Marie

Vidal

Philippot

et al. 1986

European Journal of Biochemistry

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Leukemic guinea pig lymphocytes (L2C) have ten times as many low-density lipoprotein (LDL) receptors as healthy lymphocytes, but LDL accounts for only 38% of the cholesterol in L2C cells, compared to more than 95% in normal cells, Our data show that LDL fails to regulate cholesterol biosynthesis and that there is a defect in LDL internalization and receptor turnover in L2C cells. We also demonstrate that the degradation of LDL is not a limiting process. By discriminating between binding and internalization, we show that internalization in L2C is much slower than in normal cells and that the decrease in metabolism is related to the slow turnover of the LDL receptors.In human lymphocytes, as in many eukaryotic cells, cholesterol homeostasis depends on endogenous cholesterol synthesis via the 3-hydroxy-3-methylglutaryl-CoA reductase pathway and on the supply of cholesterol from the endocytosis of LDL after binding to LDL-specific receptors [l]. We have shown that in healthy guinea pig lymphocytes, cholesterol biosynthesis and LDL endocytosis account for 2.3% and 97.7%, respectively, of total cellular cholesterol needs. These cells, when freshly isolated, have about 2000 LDL-specific receptors per cell [2] and their cholesterol synthesis is directly regulated by cellular LDL metabolism [3]. On the other hand, guinea pig leukemic lymphocytes (L2C) are characterized by abnormally high cholesterol biosynthesis in vivo [4] and in vitro [5] but the regulation of cholesterol synthesis by LDL is defective [3]. Our previous results demonstrated that although L2C cells have 20000 LDL-specific receptors per cell, they have a very poor LDL metabolism compared to normal lymphocytes. The decreased rate of internalization and degradation relative to binding in the L2C cells is reflected in the internalization index, which is nearly four times as low in L2C cells as in normal cells [2]. Thus, in these cells, the de novo production of cholesterol corresponds to 62% of the whole cellular cholesterol supply, whereas only 38% comes from the LDL pathway [2]. We do not yet know enough about the impairment of LDL metabolism in cancer cells to ascertain whether the origin of this defect lies in the internalization or the intracellular degradation of LDL. Kraaijenhagen et al. [6] showed that the activities of all enzymes, except acid phosphatase, were significantly lower in leukemic B lymphocytes than in normal lymphocytes, while Anderson et al. [7] demonstrated that cancerous A-431 cells have an abnormally small capacity for internalizing LDL. We previously found that the uptake of '"I-LDL by L2C cells reaches a plateau in 4-5 h but we were unable to conclude which of the two processes (internalization or degradation) was defective [2]. In the present study, we have separately analyzed the rate of LDL internalization and the yield of its degradation by lysosomal enzymes, and the turnover of LDL receptors. Our data show that LDL internalization and/or the turnover of the receptors are the limiting steps. At equilibrium, degradation always ...

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Acid glycosidases of bovine lymphocytes from normal cows and cows with chronic lymphatic leukemia

Preobrazhenskaya¹,

Gevorkyan²

1985

Bull Exp Biol Med

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Lysosomal enzymes in normal and leukemic B lymphocytes

Cited by 15 publications

References 11 publications

Profound Impact of Decline in N-Acetylgalactosamine-4-Sulfatase (Arylsulfatase B) on Molecular Pathophysiology and Human Diseases

Profound Impact of Decline in N-Acetylgalactosamine-4-Sulfatase (Arylsulfatase B) on Molecular Pathophysiology and Human Diseases

Internalization of low‐density‐lipoprotein‐specific receptors in leukemic guinea pig lymphocytes

Acid glycosidases of bovine lymphocytes from normal cows and cows with chronic lymphatic leukemia

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