Functional and Comparative Analysis of Two Subtypes of Cofilin Family on Cattle Myoblasts Differentiation

Agricultural meat composition and quality are not independent of the effects of skeletal muscle growth and development in animals. Cofilin is distributed extensively in muscle and non-muscle cells, and its function is tightly regulated in the cell. Cofilin has two variants in mammals, cofilin-1 (CFL...

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Main Authors: Yujia Sun, Yaoyao Ma, Xinyi Wu, Tianqi Zhao, Lu Lu, Zhangping Yang
Format: Article
Language:English
Published: MDPI AG 2022-09-01
Series:Agriculture
Subjects:
Online Access:https://www.mdpi.com/2077-0472/12/9/1420
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author Yujia Sun
Yaoyao Ma
Xinyi Wu
Tianqi Zhao
Lu Lu
Zhangping Yang
author_facet Yujia Sun
Yaoyao Ma
Xinyi Wu
Tianqi Zhao
Lu Lu
Zhangping Yang
author_sort Yujia Sun
collection DOAJ
description Agricultural meat composition and quality are not independent of the effects of skeletal muscle growth and development in animals. Cofilin is distributed extensively in muscle and non-muscle cells, and its function is tightly regulated in the cell. Cofilin has two variants in mammals, cofilin-1 (CFL1, non-muscle type) and cofilin-2 (CFL2, muscle type), and has a dual function on skeletal muscle fibers. Our study examined the expression pattern of CFL1 and CFL2 in different fetal bovine, calf, and adult cattle tissues. The content of the CFL2 gene increased significantly with the increase in cattle age in muscle tissues; CFL1 showed the opposite trend. In muscle tissues, DNA methylation levels of CFL1 and CFL2 were high in fetal bovine, and the mRNA level of CFL2 was significantly lower compared to CFL1. However, DNA methylation levels of CFL2 were lower than CFL1, and the mRNA level of CFL2 was remarkably higher compared to CFL1 in adult cattle. Overexpression of CFL1 or knockdown CFL2 reduced the expression levels of muscle differentiation markers, i.e., MYOD, MYOG, and MYH3. Overexpression of CFL2 or knockdown CFL1 stimulated the expression of these marker genes. Therefore, CFL2 may be superior to CFL1 as a candidate gene for subsequent research on cattle genetics and breeding.
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spelling doaj.art-3a86f7366290424fb5a548f6f47f4d022023-11-23T14:33:39ZengMDPI AGAgriculture2077-04722022-09-01129142010.3390/agriculture12091420Functional and Comparative Analysis of Two Subtypes of Cofilin Family on Cattle Myoblasts DifferentiationYujia Sun0Yaoyao Ma1Xinyi Wu2Tianqi Zhao3Lu Lu4Zhangping Yang5Joint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Institutes of Agricultural Science and Technology Development, Yangzhou University, Yangzhou 225009, ChinaJoint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Institutes of Agricultural Science and Technology Development, Yangzhou University, Yangzhou 225009, ChinaJoint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Institutes of Agricultural Science and Technology Development, Yangzhou University, Yangzhou 225009, ChinaJoint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Institutes of Agricultural Science and Technology Development, Yangzhou University, Yangzhou 225009, ChinaKey Laboratory of Animal Genetics & Breeding and Molecular Design of Jiangsu Province, Yangzhou University, Yangzhou 225009, ChinaJoint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Institutes of Agricultural Science and Technology Development, Yangzhou University, Yangzhou 225009, ChinaAgricultural meat composition and quality are not independent of the effects of skeletal muscle growth and development in animals. Cofilin is distributed extensively in muscle and non-muscle cells, and its function is tightly regulated in the cell. Cofilin has two variants in mammals, cofilin-1 (CFL1, non-muscle type) and cofilin-2 (CFL2, muscle type), and has a dual function on skeletal muscle fibers. Our study examined the expression pattern of CFL1 and CFL2 in different fetal bovine, calf, and adult cattle tissues. The content of the CFL2 gene increased significantly with the increase in cattle age in muscle tissues; CFL1 showed the opposite trend. In muscle tissues, DNA methylation levels of CFL1 and CFL2 were high in fetal bovine, and the mRNA level of CFL2 was significantly lower compared to CFL1. However, DNA methylation levels of CFL2 were lower than CFL1, and the mRNA level of CFL2 was remarkably higher compared to CFL1 in adult cattle. Overexpression of CFL1 or knockdown CFL2 reduced the expression levels of muscle differentiation markers, i.e., MYOD, MYOG, and MYH3. Overexpression of CFL2 or knockdown CFL1 stimulated the expression of these marker genes. Therefore, CFL2 may be superior to CFL1 as a candidate gene for subsequent research on cattle genetics and breeding.https://www.mdpi.com/2077-0472/12/9/1420cofilin-1cofilin-2expression patternDNA methylationmyoblast differentiation
spellingShingle Yujia Sun
Yaoyao Ma
Xinyi Wu
Tianqi Zhao
Lu Lu
Zhangping Yang
Functional and Comparative Analysis of Two Subtypes of Cofilin Family on Cattle Myoblasts Differentiation
Agriculture
cofilin-1
cofilin-2
expression pattern
DNA methylation
myoblast differentiation
title Functional and Comparative Analysis of Two Subtypes of Cofilin Family on Cattle Myoblasts Differentiation
title_full Functional and Comparative Analysis of Two Subtypes of Cofilin Family on Cattle Myoblasts Differentiation
title_fullStr Functional and Comparative Analysis of Two Subtypes of Cofilin Family on Cattle Myoblasts Differentiation
title_full_unstemmed Functional and Comparative Analysis of Two Subtypes of Cofilin Family on Cattle Myoblasts Differentiation
title_short Functional and Comparative Analysis of Two Subtypes of Cofilin Family on Cattle Myoblasts Differentiation
title_sort functional and comparative analysis of two subtypes of cofilin family on cattle myoblasts differentiation
topic cofilin-1
cofilin-2
expression pattern
DNA methylation
myoblast differentiation
url https://www.mdpi.com/2077-0472/12/9/1420
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