Characterization of lipoprotein lipase activity, secretion, and degradation at different sites of post-translational processing in primary cultures of rat adipocytes.

Simsolo, RB; Ong, John M.; Kern, PA

doi:10.1016/s0022-2275(20)41335-5

Cited by 38 publications

(2 citation statements)

References 26 publications

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“…Inhibition of glucosidase activity also blocks secretion or cell surface expression of other glycoproteins [for example, see Gross et al (1983); Moore and Spiro (1993), Schlesinger et al (1984), and Simsolo et al (1992)]. In several cases glucosylated proteins were rapidly degraded [for example, see Moore and Spiro (1993)] or retained intracellularly (Simsolo et al, 1992), suggesting that the glucosylated V-glycan functions as a specific signal for glycoprotein retention and/or degradation in the endoplasmic reticulum. However, since glucosidase inhibitors do not inhibit secretion or cell surface expression of other glycoproteins [for example.…”

Section: Cell Associated Secretedmentioning

confidence: 99%

Stable secretion of a soluble, oligomeric form of rabies virus glycoprotein: influence of N-glycan processing on secretion

Wójczyk¹,

Shakin-Eshleman²,

Doms³

et al. 1995

Biochemistry

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Rabies virus glycoprotein (RGP) is a 505 amino acid type I transmembrane glycoprotein that is important in the pathogenesis of rabies virus infection. RGP also stimulates the development of neutralizing antibodies by the host. N-linked glycosylation is required for both cell surface expression and immunogenicity of RGP. In the current study, a soluble form of RGP, constructed by insertion of a stop codon external to the transmembrane domain, was expressed in transfected Chinese hamster ovary cells. The soluble form of RGP was found to be appropriately antigenic and immunogenic. Similar to full-length RGP, the soluble form was assembled into homodimers and homotrimers. Core glycosylation was required for secretion of soluble RGP and cell surface expression of full-length RGP. In addition, initial glucose trimming of the N-glycans was necessary and sufficient for secretion of soluble RGP and cell surface expression of full-length RGP. Further N-glycan processing was not required for secretion or cell surface expression of soluble or full-length RGP, respectively.

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Section: Cell Associated Secretedmentioning

confidence: 99%

Stable secretion of a soluble, oligomeric form of rabies virus glycoprotein: influence of N-glycan processing on secretion

Wójczyk¹,

Shakin-Eshleman²,

Doms³

et al. 1995

Biochemistry

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“…while rat HL (33) and mouse HL (34) have two. Trimming in ER of glucose residues from the oligoglycans is required for activation and secretion of LPL in rat (35) and mouse adipocytes (36) and HL in rat liver (37). Although active LPL (38,39) and active HL (37) secreted by incubated rodent cells have endo H-resistant oligosaccharide chains, processing of their oligosaccharides to endo H-resistance is not required for synthesis or secretion of active forms of these lipases (37,39).…”

mentioning

confidence: 99%

Adrenal and liver in normal and cld/cld mice synthesize and secrete hepatic lipase, but the lipase is inactive in cld/cld mice

Schultz

Blanchette‐Mackie

Scow

2000

Journal of Lipid Research

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Combined lipase deficiency ( cld ) is a recessive mutation in mice that causes a severe lack of lipoprotein lipase (LPL) and hepatic lipase (HL) activities, hyperlipemia, and death within 3 days after birth. Earlier studies showed that inactive LPL and HL were synthesized by cld / cld tissues and that LPL synthesized by cld / cld brown adipocytes was retained in their ER. We report here a study of HL in liver, adrenal, and plasma of normal newborn and cld / cld mice. Immunofluorescence studies showed HL was present in extracellular space, but not in cells, in liver and adrenal of both normal and cld / cld mice. When protein secretion was blocked with monensin, HL was retained intracellularly in liver cell cultures and in incubated adrenal tissues of both groups of mice. These findings demonstrated that HL was synthesized and secreted by liver and adrenal cells in normal newborn and cld / cld mice. HL activities in liver, adrenal, and plasma in cld / cld mice were very low, Ͻ 8% of that in normal newborn mice, indicating that HL synthesized and secreted by cld / cld cells was inactive. Livers of both normal newborn and cld / cld mice synthesized LPL, but the level of LPL activity in cld / cld liver was very low, Ͻ 9% of that in normal liver. Immunofluorescence studies showed that LPL was present intracellularly in liver of cld/cld mice, indicating that LPL was synthesized but not secreted by cld/ cld liver cells. Immunofluorescent LPL was not found in normal newborn liver cells unless the cells were treated with monensin, thus demonstrating that normal liver cells synthesized and secreted LPL. Livers of both groups of mice contained an unidentified alkaline lipase activity which accounted for 34-54% of alkaline lipase activity in normal and 65% of that in cld / cld livers. Our findings indicate that liver and adrenal cells synthesized and secreted HL in both normal newborn and cld / cld mice, but the lipase was inactive in cld/cld mice. That cld / cld liver cells secreted inactive HL while retaining inactive LPL indicates that these closely related lipases were processed differently. -Schultz, C. J., E. J. Blanchette-Mackie, and R. O. Scow. Adrenal and liver in normal and cld/cld mice synthesize and secrete hepatic lipase, but the lipase is inactive in cld / cld mice.

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The biochemistry of white and brown adipocytes analysed from a selection of proteins

Ricquier¹,

Cassard-Doulcier²

1994

EJB Reviews 1993

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Characterization of lipoprotein lipase activity, secretion, and degradation at different sites of post-translational processing in primary cultures of rat adipocytes.

Cited by 38 publications

References 26 publications

Stable secretion of a soluble, oligomeric form of rabies virus glycoprotein: influence of N-glycan processing on secretion

Stable secretion of a soluble, oligomeric form of rabies virus glycoprotein: influence of N-glycan processing on secretion

Adrenal and liver in normal and cld/cld mice synthesize and secrete hepatic lipase, but the lipase is inactive in cld/cld mice

The biochemistry of white and brown adipocytes analysed from a selection of proteins

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