Secretion and processing of apolipoprotein A-I in the avian sciatic nerve during development

Lemieux, M. Joanne; Mezei, Catherine; Breckenridge, W. C.

doi:10.1002/(sici)1097-4547(19960615)44:6<594::aid-jnr10>3.0.co;2-z

Cited by 6 publications

(3 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Apolipoprotein AI (apo-AI) is a primary protein constituent of high-density lipoprotein (HDL). It was found that the HDL concentration in chick liver and skeletal muscle increased sharply around hatching and then decreased after 1 week of postnatal time. , The Apo-AI mRNA level and its synthesis showed a similar trend. , Apo-AI was also found to be developmentally regulated in the chick sciatic nerve, in parallel with the process of active myelination . R-FABP is the avian counterpart of murine brain FABP implicated in glial cell differentiation and neuronal cell migration.…”

Section: Resultsmentioning

confidence: 91%

“…49,50 Apo-AI was also found to be developmentally regulated in the chick sciatic nerve, in parallel with the process of active myelination. 51 R-FABP is the avian counterpart of murine brain FABP implicated in glial cell differentiation and neuronal cell migration. A study on chick mRNAs level also confirmed the elevation of FABPs in undifferentiated retina from embryonic day 3.5 and a subsequent decrease (50-100-fold) upon tissue maturation through day 7 to day 19.…”

Section: Development Of Chick Retinal Proteomementioning

confidence: 99%

See 1 more Smart Citation

A Chick Retinal Proteome Database and Differential Retinal Protein Expressions during Early Ocular Development

Lam

et al. 2006

J. Proteome Res.

View full text Add to dashboard Cite

Proteomics approach as a research tool has gained popularity in a growing number of basic and clinical researches. However, proteomic research has yet to gain significant momentum in eye research. Hence, we decided to build a retinal proteome database using postnatal retinal tissue from chick, a commonly used animal model in eye research. Employing 2-D gels with the coverage of 3-10 pH gradients, we were able to resolve hundreds of proteins from young chick retinae. Among them, 155 high abundant proteins were identified by Peptide Mass Fingerprinting (PMF) after the Matrix-Assisted Laser Desorption Ionization-Time-of-Flight Mass Spectrometry (MALDI-TOF MS). These proteins were then classified according to their functions. Making use of the retinal database, we were able to identify several differentially expressed proteins that might be involved in early retinal development by comparing the 2-DE maps of chick retinal tissues (3, 10, and 20 days after hatching). With the current proteomics approach, we not only documented the most abundant soluble proteins in the chick retinal tissue, but also demonstrated the dynamic protein expression changes during early ocular development. This represents one of the first steps in building a complete protein database in chick retinae which is applicable to the study of eye diseases from a few selected protein candidates to the whole proteome. Proteomic technology may provide a high throughput platform for advancing eye research in the feasible future.

show abstract

Section: Resultsmentioning

confidence: 91%

Section: Development Of Chick Retinal Proteomementioning

confidence: 99%

A Chick Retinal Proteome Database and Differential Retinal Protein Expressions during Early Ocular Development

Lam

et al. 2006

J. Proteome Res.

View full text Add to dashboard Cite

show abstract

“…Most apoA-I is synthesized in the liver and intestine, although small amounts of apoA-I are produced in avian nerve tissue (10) and kidney (11). ApoA-I is translated as a preproprotein (12) and, after cleavage of the 18-amino acid signal peptide, the proprotein is secreted into the plasma, where the 6-amino acid propeptide is removed by cleavage through an unidentified metalloprotease (13).…”

mentioning

confidence: 99%

Deletion of the propeptide of apolipoprotein A-I reduces protein expression but stimulates effective conversion of preβ-high density lipoprotein to α-high density lipoprotein

Sviridov

Pyle

Jauhiainen

et al. 2000

Journal of Lipid Research

View full text Add to dashboard Cite

The properties of the mature and pro-forms of recombinant apolipoprotein A-I (apoA-I) were compared with those of apoA-I isolated from human plasma. When the synthesis and secretion of pro-and mature forms of apoA-I from a baculovirus/insect cell expression system were compared in parallel experiments, the amount of the pro-form of apoA-I synthesized and secreted was severalfold higher than that of the mature form of apoA-I. A comparison of the properties of the pro-and mature forms of recombinant apoA-I and human plasma apoA-I showed no difference between all three in their secondary structure, their ability to self-associate, lipid-binding capacity, lecithin: cholesterol acyltransferase activation, and binding to the phospholipid transfer protein. The properties of reconstituted high density lipoprotein (HDL) particles formed from the proteins and their ability to promote cholesterol and phospholipid efflux from human skin fibroblasts were also similar. However, their ability to bind to plasma HDL subfractions differed, because twice as much proapoA-I associated with pre ␤ 1 -HDL and pre ␤ 2 -HDL subfractions compared with both mature recombinant and plasma apoA-I. Correspondingly, the amount of proapoA-I in ␣ -HDL subfractions, especially in ␣ 1 -HDL and ␣ 2 -HDL, was decreased. We conclude that while the propeptide of apoA-I is required for the effective synthesis and secretion of apoA-I, cleavage of this peptide is a requisite for the effective interconversion of HDL subfractions. -Sviridov, D., L. E. Pyle, M. Jauhiainen, C. Ehnholm, and N. H. Fidge. Deletion of the propeptide of apolipoprotein A-I reduces protein expression, but stimulates effective conversion of pre ␤ -high density lipoprotein to ␣ -high density lipoprotein.

show abstract

Proteome analysis of chick embryonic cerebrospinal fluid

et al. 2006

View full text Add to dashboard Cite

During early stages of embryo development, the brain cavity is filled with embryonic cerebrospinal fluid (E-CSF), a complex fluid containing different protein fractions that contributes to the regulation of the survival, proliferation and neurogenesis of the neuroectodermal stem cells. Using 2-DE, protein sequencing and database searches, we identified and analyzed the proteome of the E-CSF from chick embryos (Gallus gallus). We identified 26 different gene products, including proteins related to the extracellular matrix, proteins associated with the regulation of osmotic pressure and metal transport, proteins related to cell survival, MAP kinase activators, proteins involved in the transport of retinol and vitamin D, antioxidant and antimicrobial proteins, intracellular proteins and some unknown proteins. Most of these gene products are involved in the regulation of developmental processes during embryogenesis in systems other than E-CSF. Interestingly, 14 of them are also present in adult human CSF proteome, and it has been reported that they are altered in the CSF of patients suffering neurodegenerative diseases and/or neurological disorders. Understanding these molecules and the mechanisms they control during embryonic neurogenesis is a key contribution to the general understanding of CNS development, and may also contribute to greater knowledge of these human diseases.

show abstract

Secretion and processing of apolipoprotein A-I in the avian sciatic nerve during development

Cited by 6 publications

References 37 publications

A Chick Retinal Proteome Database and Differential Retinal Protein Expressions during Early Ocular Development

A Chick Retinal Proteome Database and Differential Retinal Protein Expressions during Early Ocular Development

Deletion of the propeptide of apolipoprotein A-I reduces protein expression but stimulates effective conversion of preβ-high density lipoprotein to α-high density lipoprotein

Proteome analysis of chick embryonic cerebrospinal fluid

Contact Info

Product

Resources

About