Interstrain variation of esterase-22, a new isozyme of the house mouse

Eisenhardt, E.; Deimling, Otto von

doi:10.1016/0305-0491(82)90102-x

Cited by 16 publications

(3 citation statements)

References 13 publications

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“…This region is syntenic to a region of mouse chromosome 8 at 8C5 [90]. The murine carboxylesterases Es22 [92,93] and Es1 [94,95] genome sequencing project unambiguously demonstrated that the murine TGH gene was located on the minus strand of chromosome 8 at 8C5 in a cluster of six carboxylesterase genes that spans 260.6 kb in total ( fig. 4).…”

Section: Tgh Gene and The Carboxylesterase Gene Familymentioning

confidence: 99%

Triacylglycerol hydrolase: role in intracellular lipid metabolism

Dolinsky

Gilham

Alam

et al. 2004

CMLS, Cell. Mol. Life Sci.

108

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Recent scientific advances have revealed the identity of several enzymes involved in the synthesis, storage and catabolism of intracellular neutral lipid storage droplets. An enzyme that hydrolyzes stored triacylglycerol (TG), triacylglycerol hydrolase (TGH), was purified from porcine, human and murine liver microsomes. In rodents, TGH is highly expressed in liver as well as heart, kidney, small intestine and adipose tissues, while in humans TGH is mainly expressed in the liver, adipose and small intestine. TGH localizes to the endoplasmic reticulum and lipid droplets. The TGH genes are located within a cluster of carboxylesterase genes on human and mouse chromosomes 16 and 8, respectively. TGH hydrolyzes stored TG, and in the liver, the lipolytic products are made available for VLDL-TG synthesis. Inhibition of TGH activity also inhibits TG and apolipoprotein B secretion by primary hepatocytes. A role for TGH in basal TG lipolysis in adipocytes has been proposed. TGH expression and activity is both developmentally and hormonally regulated. A model for the function of TGH is presented and discussed with respect to tissue specific functions.

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Section: Tgh Gene and The Carboxylesterase Gene Familymentioning

confidence: 99%

Triacylglycerol hydrolase: role in intracellular lipid metabolism

Dolinsky

Gilham

Alam

et al. 2004

CMLS, Cell. Mol. Life Sci.

108

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“…The high concentration of ES-22 in the cauda as compared to other organs is remarkable. Only liver shows a stronger expression of ES-22 (Eisenhardt & von Deimling, 1982). Also, ES-17 appears to be much more active in the cauda than in other organs.…”

Section: Discussionmentioning

confidence: 85%

Genetic identification of non-specific esterases of the mouse cauda epididymidis and description of esterase-28, a new carboxylesterase isoenzyme (EC 3.1.1.1)

Deimling

Wassmer²

1990

Reproduction

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Twenty-five (25) electrophoretic bands with esterase activity were distinguished in supernatants of cauda epididymidis of DBA/2J mice. Twenty (20) of these were assigned to 10 genetically defined esterases (ES-1, ES-2, ES-3, ES-6, ES-7, ES-11, ES-14, ES-17, ES-19, ES-22) which were already known from investigations of other mouse tissues. Furthermore, ES-10 was identified in cauda supernatants after isoelectric focussing. A hitherto genetically undefined esterase was assigned to locus Es-28 which was expressed solely in the epididymis. Three phenotypes were distinguished: ES-28A was present in the majority of the inbred strains examined. ES-28B was observed in AKR/Han mice and ES-28C was found in SEG/1 mice.

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“…7 A). Purified egasyn migrates as three principal esterase components probably representing charge isomers (10,27). All esterases, including egasyn, appear to be lumenal components as gel scanning determined they were 50% released at 0.03-0.04 % detergent similarly to lumenal proteins (Fig.…”

Section: Free Egasyn Is a Lumenal Component Of Microsomesmentioning

confidence: 89%

Lumenal location of the microsomal beta-glucuronidase-egasyn complex.

Brown¹,

Novak²,

Takeuchi³

et al. 1987

The Journal of Cell Biology

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Abstract. Mouse liver l~-glucuronidase is stabilized within microsomal vesicles by complexation with the accessory protein egasyn. The location of the 13-glucuronidase-egasyn complex and free egasyn within microsomal vesicles was investigated. Surprisingly, it was found that neither the complex nor free egasyn are intrinsic membrane components. Rather, both are either free within the vesicle lumen or only weakly bound to the inside of the vesicle membrane. This conclusion was derived from release studies using low concentrations of Triton X-100 or controlled sonication. Both the intact complex and free egasyn were released in parallel with lumenal proteins, not with intrinsic membrane components. Also, 13-glucuronidase was protected from digestion by proteinase K by the membrane of microsomal vesicles. The hydrophilic nature of both the complex and free egasyn was confirmed by phase separation experiments with the detergent Triton X-114. Egasyn is one of an unusual group of esterases that, despite being located within the lumen or only weakly bound to the lumenal surface of the endoplasmic reticulum, do not enter the secretory pathway. ~-Glucuronidase is an unusual acid hydrolase in that large amounts (20-40%) of stable enzyme exist in the microsomal comparmaent of liver in addition to the usual lysosomal location. A wide variety of biochemical and genetic information indicates that the same polypeptide is found at both subcellular sites and that complex formation with the accessory protein, egasyn, is required for stabilization of ~glucuronidase in microsomes (reviewed in 24). The system thus serves as a model for the specific subceUular localization of enzymes. Mutant mice that lack egasyn have no stable microsomal I~-glucuronidase (14). More recent studies have shown that egasyn is associated exclusively with the precursor form of 13-glucuronidase in microsomes (9) and that egasyn is identical with mouse esterase-22 (26,27).It has been postulated that egasyn stabilizes the l~-glucuronidase complex in microsomes by serving as an integral membrane anchor peptide (24). Others (12) have suggested that microsomal I~-glucuronidase serves in a membrane structural role. In this paper we present evidence that the microsomal 13-glucuronidase-egasyn complex, rather than being an integral membrane component, surprisingly is either free within the lumen of microsomal vesicles or very weakly attached to the inside of these vesicles. These results suggest, in turn, that the binding protein, egasyn, stabilizes 13-glucuronidase within the microsomal lumen. Materials and Methods AnimalsC57BL/6J, Mus musculus molossinus and Mus spretus mice were raised in the animal facilities of Roswell Park Memorial Institute. Mice 2-4 mo old and of both sexes were used. Unless otherwise indicated, C57BL/6J mice were used. Radiolabeling ExperimentsRadiolabeling of membrane and secretory components of microsomes was done according to the method of Kreibich and Sabatini (20). Membrane phospholipids were labeled by injecting mice intraperitoneal...

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Interstrain variation of esterase-22, a new isozyme of the house mouse

Cited by 16 publications

References 13 publications

Triacylglycerol hydrolase: role in intracellular lipid metabolism

Triacylglycerol hydrolase: role in intracellular lipid metabolism

Genetic identification of non-specific esterases of the mouse cauda epididymidis and description of esterase-28, a new carboxylesterase isoenzyme (EC 3.1.1.1)

Lumenal location of the microsomal beta-glucuronidase-egasyn complex.

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