scholarly journals Leptin Gene as Potential Gene for Molecular Selection on Cattle in Indonesia

2018 ◽  
Vol 27 (3) ◽  
pp. 105
Author(s):  
Widya Pintaka Bayu Putra ◽  
Rhesti Indriastuti

<p>Genetic improvement in beef and dairy cattle which can increase meat and milk production can be conducted through livestock selection based on molecular technique using leptin gene. The leptin gene is located on the fourth chromosome and consists of three exons and two introns. The leptin gene serves to produce the leptin hormone secreted by fat tissue. High concentrations of leptin hormone can increase feed intake and body metabolism thereby increasing livestock productivity. This paper describes the leptin gene including structure, mechanism of leptin hormone and polymorphisms in cows. These polymorphisms occur in the promoter, intron and exon sections associated with body and carcass weight and milk production in some cattle breed. Therefore, leptin gene can be used for selection towards increasing cattle productivity. Utilization of leptin gene can be done by single nucleotide polymorphism (SNP) identification on the whole structure of leptin gene and to observe its effect on characteristics of cattle production in Indonesia.</p>

2006 ◽  
Vol 73 (2) ◽  
pp. 193-196 ◽  
Author(s):  
Aileen F Keating ◽  
Terry J Smith ◽  
R Paul Ross ◽  
Michael T Cairns

The bovine β-casein (CSN2) gene has been shown to span a region of 8·5 kb, containing nine exons and eight intervening introns (Bonsing et al. 1988; Martin et al. 2002). The exons range in size from 24 to 498 bp; the introns, however, are much larger and account for 85% of the gene. Twelve genetic variants in the coding sequence of the β-casein gene have been reported (Farrell et al. 2004). The A2 allele of the β-casein gene has been associated with a higher milk production (Lin et al. 1986; Bech & Kristiansen, 1990) while the B variant has been associated with an increase in protein content and better cheesemaking properties (Marziali & Ng-Hang-Kwai, 1986). The β-casein gene codes for a protein of 209 amino acids with varying regions at codons 67, 106 and 122. The A1 variant differs from A2 at position 67, where a histidine replaces a proline (Lien et al. 1992). The β-casein A2 variant has histidine and the A3 variant has glycine at position 106 (Lien et al. 1992); the β-casein A2 variant has serine at position 122 and the β-casein B variant has arginine at this codon (Stewart et al. 1987; Damiani et al. 1992).


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