scholarly journals Binding of high density lipoprotein to cultured fibroblasts after chemical alteration of apoprotein amino acid residues.

1986 ◽  
Vol 261 (1) ◽  
pp. 495-503 ◽  
Author(s):  
E A Brinton ◽  
J F Oram ◽  
C H Chen ◽  
J J Albers ◽  
E L Bierman
Keyword(s):  
Amino Acid ◽  
High Density Lipoprotein ◽  
Density Lipoprotein ◽  
High Density ◽  
Amino Acid Residues ◽  
Cultured Fibroblasts ◽  
Chemical Alteration

scholarly journals Identification of a Novel Apolipoprotein, ApoN, in Ovarian Follicular Fluid

Endocrinology ◽  
2004 ◽  
Vol 145 (11) ◽  
pp. 5231-5242 ◽  
Author(s):  
Moira K. O’Bryan ◽  
Lynda M. Foulds ◽  
James F. Cannon ◽  
Wendy R. Winnall ◽  
Julie A. Muir ◽  
...  
Keyword(s):  
Amino Acid ◽  
High Density Lipoprotein ◽  
Follicular Fluid ◽  
Low Density Lipoprotein ◽  
Regulatory Protein ◽  
Amino Acid Level ◽  
Density Lipoprotein ◽  
High Density ◽  
Significant Homology ◽  
Ovarian Follicular Fluid

Abstract A novel apolipoprotein, designated ApoN, has been identified in bovine ovarian follicular fluid using chromatographic purification methods, amino acid sequence analysis, molecular biology, and bioinformatics. The apolipoprotein is a hydrophobic 12-kDa protein processed from the C terminus of a 29-kDa precursor expressed in a number of tissues, including the ovary, testis, the anterior chamber of the eye, skeletal muscle, uterus, and liver. Bovine, porcine, and murine ApoN display significant homology at the amino acid level across the entire precursor sequence. Surprisingly, there appears to be no orthologous protein in the human, although an APON-like pseudogene is found on chromosome 12. The N-terminal fragment of the ApoN precursor shows significant homology with the N-terminal sequence of the precursor of the cholesterol transport regulatory protein ApoF, but the corresponding C-terminal sequences of ApoN and ApoF possess no homology. ApoN is present in the high-density lipoprotein fraction of bovine serum and both the high-density lipoprotein and low-density lipoprotein fractions of bovine follicular fluid and is found in several tissues that are associated with local immunological privilege. These data suggest that ApoN may play a role in steroidogenesis and/or immunoregulation in the gonads of nonhuman species, as well as similar roles in other tissues.

Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein

Biochemistry ◽  
1982 ◽  
Vol 21 (14) ◽  
pp. 3298-3303 ◽  
Author(s):  
David C. Parmelee ◽  
Koiti Titani ◽  
Lowell H. Ericsson ◽  
Nils Eriksen ◽  
Earl P. Benditt ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
High Density Lipoprotein ◽  
Density Lipoprotein ◽  
High Density ◽  
Human High Density Lipoprotein

scholarly journals Accumulation of pro-apolipoprotein A-II in mouse senile amyloid fibrils

1997 ◽  
Vol 325 (3) ◽  
pp. 653-659 ◽  
Author(s):  
Keiichi HIGUCHI ◽  
Kumiko KOGISHI ◽  
Jing WANG ◽  
Chen XIA ◽  
Takuya CHIBA ◽  
...  
Keyword(s):  
Amino Acid ◽  
High Density Lipoprotein ◽  
Relative Abundance ◽  
Mouse Liver ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Density Lipoprotein ◽  
Amyloid Protein ◽  
Amino Acid Residues ◽  
Apolipoprotein A

Apolipoprotein A-II (apoA-II), the major apoprotein of serum high-density lipoprotein, is deposited as amyloid fibrils (AApoAII) in murine senile amyloidosis. We have identified and purified a more basic amyloid protein from old-mouse liver. N-terminal sequencing of the protein revealed that the pro-segment of five amino acid residues (Ala-Leu-Val-Lys-Arg) extended from the N-terminal glutamine residue of mature apoA-II protein. MS analysis revealed the deposit of intact pro-apoA-II protein (molecular mass 9319 Da). Antiserum was prepared for staining of the AApoAII amyloid deposition. The relative abundance of pro-apoA-II to mature apoA-II in the amyloid-fibril fraction isolated from livers of mice with severe amyloidosis was 14.1%. The similar abundance of pro-apoA-II in the amyloid fibril fraction from the spleen (16.3%) suggested that deposited pro-apoA-II originated from the blood. The concentration of pro-apoA-II was much lower in the serum (1.5% of mature apoA-II) than in the amyloid-fibril fraction. There was no difference in the content of pro-apoA-II between the amyloidogenetic R1.P1-Apoa2c and amyloid-resistant SAMR1 strains at the age of 3 months. The abundance of pro-apoA-II in the amyloid-fibril fraction compared with the serum suggested that it plays a key role in the initialization of mouse senile amyloidosis.

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