Abstract
Collagens, as extracellular matrix proteins, support cells for structural integrity and contribute to support mammary basic structure and development. This study aims to perform the genomic identification, evolution, and expression analyses of the collagen gene family in water buffalo (Bubalus bubalis) during lactation. A total of 128 buffalo collagen protein sequences were deduced from the 45 collagen genes identified in silico from buffalo genome, which classified into six groups based on their phylogenetic relationships, conserved motifs, and gene structure analyses. The identified collagen sequences were unequally distributed on 16 chromosomes. The tandem duplicated genes were found within three chromosomes, while only one segmental event occurred between Chr3 and Chr8. Collinearity analysis revealed that a total of 36 collagen gene pairs were orthologous between buffalo and cattle genomes despite having different chromosome numbers. Comparative transcription analyses revealed that a total of 23 orthologous collagen genes were detected in the milk samples at different lactation periods between the two species. Notably, the duplicated gene pair of COL4A1-COL4A2 during lactation had a higher mRNA expression level than that of cattle, while a higher expression level of COL6A1-COL6A2 pair was found in cattle compared with that of buffalo. The present study provides useful information for investigating the potential functions of the collagen family in buffalo during lactation and helps in the functional characterization of collagen genes in additional research.
Highlights
Collagens represent the most abundant protein of the extracellular matrix (ECM) in animals.To date, the knowledge about the molecular structure, biosynthesis, and function of the collagen family has emerged [1]
Our results provide some insights into the understanding of the buffalo collagen family affecting mammary gland development and lactation, and present vital evidence for future functional studies
To identify the collagen family members, a total of 128 non-redundant protein sequences encoded by 45 collagen genes were predicted from the buffalo whole genome using the BLAST and HMMER
Summary
Collagens represent the most abundant protein of the extracellular matrix (ECM) in animals. The knowledge about the molecular structure, biosynthesis, and function of the collagen family has emerged [1]. Collagens comprised 28 members in vertebrates, and are multidomain proteins that commonly possessed at least one triple-helical domain. Types I to IV of the collagen family are the most common, each serving different functions with the appropriate structure. IV is an important component of the ECM in the mammary glands [2,3]. Chen et al [4] found the COL4A1 was significantly down regulated in the inflammation-associated fibroblasts extracted from bovine mammary glands with clinical mastitis compared with normal fibroblasts from a slaughtered dairy cow, implying that it might involve the ECM remodeling or immune response. Crisà et al [5]
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