Bioinformatic Analysis of Insulin-Like Growth Factor I Gene of Three Avain Species

Filed in Articles by on August 18, 2020

Bioinformatic Analysis of Insulin-Like Growth Factor I Gene of Three Avain Species.

ABSTRACT

A lot of attention has been paid to the study of Insulin-like Growth factor 1 (IGF1) due to its function in stimulating systemic body growth and regulating cell growth and development. A bioinformatics study was carried out to investigate the Insulin-like Growth Factor 1 gene of turkey, chicken and quail. A total of 15 insulin-like growth
factor 1 nucleotide sequence and their corresponding protein were obtained from the Genebank (a public domain protein database) and were analyzed using various software tools (Clustal W, MEGA 6, dnaSP, BLAST, phyre2, ExPASy GORIV and Rasmol software) to determine the percent identity and similarities in function of IGF
1 gene, genetic diversity, evolutionary relationship, protein structure prediction and physiochemical properties. The result obtained showed that percent identity and similarity of IGF1 gene in avians ranged from 86-99% and were similar in function. Observed genetic diversity was high within each avian (1.000 in turkey, 0.900 in
chicken and 0.900 in quail). However chicken had the highest haplotype number value (4), this showed that chicken has more variation than turkey and quail IGF1 gene sequence. Phylogenetic analysis showed that the IGF1 in gene sequence of avian were grouped into the same taxon, chicken and quail shared a most recent common
ancestor and were closely related than the IGF1 gene of turkey. The secondary structure analyzed by GORIV (Garnier-Osguthorpe-Robson IV) software tool showed that the alpha helix structure of chicken, turkey and quail occupied (20.92%), (21.57%) and (20.92%) of the IGF1 gene sequences respectively. The results from the
secondary and tertiary structure of IGF1 protein predictions showed that the IGF genes of avian are stable and properly formed. The physiochemical properties showed that chicken, turkey and quail IGF1protein had isoelectric potential (theoretical pI) of 9.25, estimated half-life of 30 hours. In conclusion, the high percent identity and
similarity in function, high genetic diversity observed, a relative relatedness in the phylogentic study and high alpha helix in the protein structure of IGF1 gene seen in this study make the gene highly effective in improving growth, and regulating cellular activities.

TABLE OF CONTENT

Title page………………………………….……………………………………….. i
Certification……………………………………………………………………….. ii
Dedication………………………………………………………………………… .iii
Acknowledgement ………………………………………………………………… iv
Table of content……………………………………………………………………. v
List of tables……………………………………………………………………….. viii
List of figures………………………………………………………………………. ix
List of plates………………………………………………………………………… x
Abstract…………………………………………………………………………….. xi

CHAPTER ONE: GENERAL INTRODUCTION

1.1 Introduction………………………………………………….………………….. 1
1.2 Objectives of the study……………………………………….………………… 3
1.3 Justification…………………………………………….………………………… 3

CHAPTER TWO: LITERATURE REVIEW

2.1 Insulin-like growth factor……………………………………………………….. 4
2.2 Basic biochemistry and physiologic functions………………………………….. 5
2.2.1 Structure and synthesis…………………………….………………………….. 5
2.2.2 Physiologic role and mechanism of action………………………….………… 5
2.2.3 Regulation and differentiation of function……………………………….…… 6
2.3 Pathologic conditions associated with alteration in the IGF system……………. 6
2.3.1 Insulin-like growth factor I……………………………………………………… 6
2.3.2 Insulin-like growth factor II…………………………………………………… 8
2.4 Insulin-like growth factor I as a therapeutic agent………………………………. 8
2.5 The IGF system and muscle development in birds……………………………… 8
2.6 Species specificities of the avian IGF system …………………………………. 9
2.7 Structure of IGF I peptide and gene transcript ………………………………. 10
2.8 IGF1 as a local regulator of muscle growth …………………………………… 11
2.9 Genetic diversity………………………………………………………………. 12
2.10 Protein structure ……………………………………………………………… 12
2.11 Levels of protein Structure ……………………………………………………… 13
2.11.1 Primary structure………………………………………………………….… 13
2.11.2 Secondary structure………………………………………………………… 13
2.11.3 Tertiary structure …………………………………………………………….. 14
2.11.4 Quaternary structure ……………………………………………………….. 14
2.12 Protein structure prediction…………………………………………………… 14
2.13 Bioinformatics ………………………………………………………………… 15
2.13.1 Application of bioinformatics to biotechnology and biomedical sciences…… 15
2.14 Phylogenetics …………………………………………………………………. 18
2.15 Comparative genomics ………………………………………………………….. 19

CHAPTER THREE: MATERIALS AND METHOD

3.1 Location of study and retrieval of IGF I gene sequence …………………………. 21
3.2 Multiple sequence alignment ………………………………………………….. 21
3.3 Determination of genetic diversity of IGF I gene of turkey, chicken and quail.. 21
3.4 Determination of evolutionary relationship…………………………………….. 21
3.4.1 Determination of percent identity and similarity……………………………… 21
3.4.2 Phylogenetic analysis……………………………………………………………. 22
3.5 Prediction of protein structure …………………………………………………. 22
3.6 Determination of physiochemical properties …………………………………… 22

CHAPTER FOUR: RESULT AND DISCUSSION

4.1 Retrieval of nucleotide and amino acid sequences of IGF I gene…………….. 23
4.2 Percentage identity and similarities of IGF I gene among avian species……… 24
4.2.1 Percentage identity of IGF I gene among avian species ……………….…… 24
4.2.2 Percentage similarities of IGF I gene among avian species…………………. 25
4.3 Genetic diversity of IGF I gene on three avian species……………………….. 26
4.4 Evolutionary relationship study of IGF I gene on three avian species ………. 28
4.5 Secondary and tertiary protein structure IGF I protein of three avian species… 30
4.5.1 Secondary protein structure of IGF I protein……………………………….. 30
4.5.2 Tertiary protein structures of IGF I protein of chicken, turkey and quail…… 31
4.6 Physiochemical properties of chicken, turkey and quail IGF I protein………. 36

CHAPTER FIVE: CONCLUSION AND RECOMMENDATION

5.1 Conclusion and recommendation ……………………………………………. 38
References ……………………………………………………………………….. 39

INTRODUCTION

Insulin-like growth factors (IGF1) are naturally occurring protein capable of stimulating cellular growth, proliferation and differentiation.

According to Hegarty et al. (2006), IGF1 are proteins which are important for regulating a variety of cellular processes.

Insulin-like growth factor-1 is a mediator of many biological effects; it increases the absorption of glucose, stimulates myogenesis, inhibits cell cycle genes, increases the synthesis of lipids, and stimulates the production of progesterone in the synthesis of DNA, RNA and protein (Etherton, 2004).

Due to these biological functions, IGF1 is being considered as a candidate gene for predicting growth and meat quality traits in the animal genetic development scheme (Andrade et al., 2008).

IGF1 is produced primarily by the liver as an endocrine hormone as well as in target tissues in a paracrine or autocrine manner (Kemp, 2007).

Its production is stimulated by growth hormone and can be retarded by under-nutrition, growth insensitivity or lack of growth hormone receptors (Flier and Underhill, 2006).

Growth hormone is made in the anterior pituitary gland and released into the blood stream and then stimulates the liver to produce IGF1 (Akinfenwa et al., 2011).

Then IGF1 stimulates systemic body growth and has growthpromoting effects on almost every cell in the body system (Yilmaz et al., 2011). Deficiency of either growth hormone or IGF1 therefore results in diminished stature (Akinfenwa et al., 2011).

Different researchers have established a link between the concentration of the circulating IGF1 and growth trait in many livestock species and laboratory animals (Bertlett and Tom, 2005; Bunter et al., 2005; Hegarty et al., 2006).

REFERENCES

Akinbiyi, J.A. (2014). Bioinformatics Analysis of interferon Gene in Bovids. Ms.c Dessertation, University of Nigeria Nsukka (Unpublished).
Akinfenwa, M.O., Peter, S.O., Adenaike, A.S., Obetoh, J.O. and Ikeobi, C.O.N. (2011). Bioinformatics analysis of insulin-like growth factor-1 (IGFI) in five mammalian species. Proceedings of the 16th Annual Conference of the Animal Science Association (ASAAN) September 12th, 2011, K.S.U, Anyigba, Nigeria P 19-21
Alberts, Bruce; Alexander Johnson; Julian Lewis; Martin Raff; Keith Roberts; Peter Walters (2002). “The Shape and Structure of Proteins”. Molecular Biology of the Cell; Fourth Edition. New York and London: Garland Science. ISBN 0-8153-3218-1.
Amills, M., Jimenez, N., Villalba, D., Tor, M., Molina, E., Cubilo, D. (2003). Identification of three single nucleotide polymorphisms in the chicken insulin-like growth factor 1 and 2 genes and their associations with growth and feeding traits. Poult Sci. 82:1485- 1493.
Andrade, P.C., Gross, D.A., Paz, C.C. and Alenca, M.M. (2008). Association of an insulinlike growth factor-1 gene Micro satellite with phenotypic variation and estimated breeding values of growth traits in canchim cattle. Animal Genetics 39: 480-485.
Andreas, D., Baxevanis, B.F. and Francis, O. (2001). Bioinformatics: A Practical Guide to the Analysis of Genes and Proteins, Second Edition. ISBNs: 0-471-38390-2 (Hardback); 0-471-38391-0 (Paper); 0-471-22392-1 (Electronic) Animal QTL D Abase (2011): http//www.animal geneome org.

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