Evolution of The Angiopoietin-Like Gene Family and Their Role in Lipid Metabolism in Pigs

Abstract Background Lipid metabolism is closely associated with various metabolic diseases, such as obesity, cardiovascular disease, diabetes, and cancer. More importantly, it also affects the carcass quality of animals. Angiopoietin-like protein (Angiopoietin-like, ANGPTL) family members are encoded by 8 genes and play an important role in lipid metabolism and angiogenesis. In this study, we first systematically described the phylogenetic characteristics of pig ANGPTL family genes and identified the critical roles of ANGPTL3, ANGPTL4 and ANGPTL8 in the lipid metabolism of pigs. Methods The amino acid sequence analysis, phylogenetic analysis, and chromosome adjacent gene analysis were performed to identify the ANGPTL gene family in pigs. Furthermore, according to the body weight data from 60 Jinhua pigs, different tissues of 6 pigs with average body weight were used to determine the expression profile of ANGPTL1-8. The ileum, subcutaneous fat, and liver of 8 pigs with distinct fatness were selected to analyze the gene expression of ANGPTL3, ANGPTL4, and ANGPTL8. Results Results showed the sequence length of ANGPTLs in pigs was between 1186 and 1991 bp, and the pig ANGPTL family members shared common features with human homologous genes, including the high similarity of the amino acid sequence and chromosome flanking genes. Amino acid sequence analysis showed that ANGPTL1-7 had a highly conserved domain except for ANGPTL8. Phylogenetic analysis showed that each ANGPTL homologous gene was clustered with other mammalian sequences, away from other vertebrates. RT-qPCR analysis showed that ANGPTL family members had different expression patterns in different tissues. ANGPTL3 and ANGPTL8 were mainly expressed in the liver, while ANGPTL4 was expressed in many other tissues, such as the intestine and subcutaneous fat. The expression levels of ANGPTL3 and ANGPTL4 in Jinhua pigs with low propensity for adipogenesis were significantly higher than those of high propensity for adipogenesis. Conclusions These results increase our knowledge about the biological role of the ANGPTL family in this important economic species. In addition, it will also help to better understand the role of ANGPTL3, ANGPTL4 and ANGPTL8 in lipid metabolism of pigs, and provide innovative ideas for develop strategies to improve pig carcass quality.

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Evolution of the Angiopoietin-Like Gene Family and Their Role in Lipid Metabolism in Pigs

10.21203/rs.3.rs-538958/v1 ◽

2021 ◽

Author(s):

Zibin Zheng ◽

Wentao Lyu ◽

Qihua Hong ◽

Hua Yang ◽

Ying Li ◽

...

Keyword(s):

Phylogenetic Analysis ◽

Lipid Metabolism ◽

Amino Acid ◽

Amino Acid Sequence ◽

Subcutaneous Fat ◽

Family Members ◽

Carcass Quality ◽

Amino Acid Sequence Analysis ◽

Different Tissues

Abstract Background: Lipid metabolism is closely associated with various metabolic diseases, such as obesity, cardiovascular disease, diabetes, and cancer. More importantly, it also affects the carcass quality of animals. Angiopoietin-like protein (Angiopoietin-like, ANGPTL) family members are encoded by 8 genes and play an important role in lipid metabolism and angiogenesis. In this study, we first systematically described the phylogenetic characteristics of pig ANGPTL family genes and identified the critical roles of ANGPTL3, ANGPTL4 and ANGPTL8 in the lipid metabolism of pigs.Methods: The amino acid sequence analysis, phylogenetic analysis, and chromosome adjacent gene analysis were performed to identify the ANGPTL gene family in pigs. Furthermore, according to the body weight data from 60 Jinhua pigs, different tissues of 6 pigs with average body weight were used to determine the expression profile of ANGPTL1-8. The ileum, subcutaneous fat, and liver of 8 pigs with distinct fatness were selected to analyze the gene expression of ANGPTL3, ANGPTL4, and ANGPTL8. Results: Results showed the sequence length of ANGPTLs in pigs was between 1186 and 1991 bp, and the pig ANGPTL family members shared common features with human homologous genes, including the high similarity of the amino acid sequence and chromosome flanking genes. Amino acid sequence analysis showed that ANGPTL1-7 had a highly conserved domain except for ANGPTL8. Phylogenetic analysis showed that the ANGPTL homologues identified from 6 species could be divided into two categories. Each ANGPTL homologous gene was clustered with other mammalian sequences, away from other vertebrates. RT-qPCR analysis showed that ANGPTL family members had different expression patterns in different tissues. ANGPTL3 and ANGPTL8 were mainly expressed in the liver, while ANGPTL4 was expressed in many other tissues, such as the intestine and subcutaneous fat. The expression levels of ANGPTL3 and ANGPTL4 in Jinhua pigs with low propensity for adipogenesis were significantly higher than those of high propensity for adipogenesis. Conclusions: These results increase our knowledge about the biological role of the ANGPTL family in this important economic species. In addition, it will also help to better understand the role of ANGPTL3, ANGPTL4 and ANGPTL8 in lipid metabolism of pigs, and provide innovative ideas for develop strategies to improve pig carcass quality.

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Identification of the gene encoding 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase in Burkholderia sp. HME13

Bioscience Biotechnology and Biochemistry ◽

10.1093/bbb/zbaa066 ◽

2020 ◽

Vol 85 (3) ◽

pp. 626-629

Author(s):

Hisashi Muramatsu ◽

Hiroki Maguchi ◽

Taisuke Harada ◽

Takehiro Kashiwagi ◽

Chul-Sa Kim ◽

...

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Propionic Acid ◽

Unknown Function ◽

Protein Family ◽

Amino Acid Sequence Analysis ◽

Gene Encoding

ABSTRACT Here, we report the identification of the gene encoding a novel enzyme, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, in Burkholderia sp. HME13. The enzyme converts 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid and H2O to 3-(2,5-dioxoimidazolidin-4-yl) propionic acid and H2S. Amino acid sequence analysis of the enzyme indicates that it belongs to the DUF917 protein family, which consists of proteins of unknown function.

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Amino acid sequence analysis of fragments generated by partial proteolysis from large simian virus 40 tumor antigen.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)70675-9 ◽

1980 ◽

Vol 255 (12) ◽

pp. 5627-5634

Author(s):

M. Schwyzer ◽

R. Weil ◽

G. Frank ◽

H. Zuber

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Tumor Antigen ◽

Simian Virus 40 ◽

Simian Virus ◽

Amino Acid Sequence Analysis

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Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)37791-3 ◽

1988 ◽

Vol 263 (25) ◽

pp. 12559-12563

Author(s):

T L Wasmoen ◽

M P Bell ◽

D A Loegering ◽

G J Gleich ◽

F G Prendergast ◽

...

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Basic Protein ◽

Major Basic Protein ◽

Amino Acid Sequence Analysis ◽

Human Eosinophil ◽

Eosinophil Granule

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Instrumentation in Amino Acid Sequence Analysis

Biochemical Society Transactions ◽

10.1042/bst0040939a ◽

1976 ◽

Vol 4 (5) ◽

pp. 939-940

Author(s):

R. J. WASHINGTON

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Amino Acid Sequence Analysis

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Factor D̄ of the alternative pathway of human complement. Purification, alignment and N-terminal amino acid sequences of the major cyanogen bromide fragments, and localization of the serine residue at the active site

Biochemical Journal ◽

10.1042/bj1870863 ◽

1980 ◽

Vol 187 (3) ◽

pp. 863-874 ◽

Cited By ~ 34

Author(s):

D M Johnson ◽

J Gagnon ◽

K B Reid

Keyword(s):

Amino Acid ◽

Sequence Analysis ◽

Amino Acid Sequence ◽

Alternative Pathway ◽

Amino Acid Sequences ◽

Serine Residue ◽

Amino Acid Sequence Analysis ◽

Terminal Amino Acid ◽

Terminal Amino ◽

Terminal Amino Acid Sequence

The serine esterase factor D of the complement system was purified from outdated human plasma with a yield of 20% of the initial haemolytic activity found in serum. This represented an approx. 60 000-fold purification. The final product was homogeneous as judged by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis (with an apparent mol.wt. of 24 000), its migration as a single component in a variety of fractionation procedures based on size and charge, and its N-terminal amino-acid-sequence analysis. The N-terminal amino acid sequence of the first 36 residues of the intact molecule was found to be homologous with the N-terminal amino acid sequences of the catalytic chains of other serine esterases. Factor D showed an especially strong homology (greater than 60% identity) with rat ‘group-specific protease’ [Woodbury, Katunuma, Kobayashi, Titani, & Neurath (1978) Biochemistry 17, 811-819] over the first 16 amino acid residues. This similarity is of interest since it is considered that both enzymes may be synthesized in their active, rather than zymogen, forms. The three major CNBr fragments of factor D, which had apparent mol.wts. of 15 800, 6600 and 1700, were purified and then aligned by N-terminal amino acid sequence analysis and amino acid analysis. By using factor D labelled with di-[1,3-14C]isopropylphosphofluoridate it was shown that the CNBr fragment of apparent mol.wt. 6600, which is located in the C-terminal region of factor D, contained the active serine residue. The amino acid sequence around this residue was determined.

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