Molecular review of prolactin with orthologue comparisons of Homo Sapien, Danio rerio, and Mus musculus.
Andrea Duchow
I. Introduction to the Molecule: Prolactin is a hormone (released by the anterior pituitary gland) that is most commonly known and named for its ability to stimulate lactation in female mammals, but additionally, serves several homeostatic functions and its involvement has been recorded in 300 biological processes (Freeman et. al 2000). Immune responses are enhanced by elevated levels of prolactin and even behavioral effect. For example, expression in rats has demonstrated parental behavior, such as nest building. Additionally, it is important to consider the vital function prolactin orthologues play
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In freshwater, a dilute environment, fish must have the ability to excrete water and either retain or uptake ions against the concentration gradient. Prolactin allows them to accomplish this by reducing water and ion permeability and enhancing the uptake of nearby ions. The contributions of many scientists went into the discovery of human prolactin as an individual pituitary hormone, but one of the most notable contributions was done in the early 1930s by Dr. Oscar Riddle, who developed the crucial pigeon crop sac bioassay that played a role in naming prolactin because the sac thickened and lactated after injections of pituitary extracts (Smith, 2004). In the earliest studies of prolactin, pigeons and doves were used due to the strong relationship Dr. Riddle shared with avian physiologist, Dr. Charles Whitman. This assay, most importantly, allowed prolactin to be identified as an independent pituitary hormone, allowed for the isolation of it from other hormones, and set the foundation for future studies of the physiological effects of prolactin (Smith, 2004). Prior to the 1970s, the existence of human prolactin was doubted to exist, and although it had been identified in various other mammals, endocrinologists believed that human growth hormone (HGH) was …show more content…
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Figure 1. A multiple alignment comparison of orthologues prolactin from a human, zebrafish, and mouse generated using CLUSTAL W (1.83) multiple sequence alignment (Larkin MA et. al 2007). The asterisk denotes identical residue, colons denote similar amino acids, and periods denote slightly similar amino acid residues in all three sequences. The blue box represents a domain predicted to be responsible to the prolactin binding and signaling site on the protein in humans (Cooke et al. 1981). A similar “prolactin-like” region is denoted by a red box on the mouse prolactin sequence (Hagaya et. al 1986). The yellow highlight denotes signal peptides, located before the amino acids in the “prolactin-like” regions of the human and mouse, which are used to specify
Paabo’s team discovered an mtDNA sequence from a finger bone they found from around 40,000 years ago, as carbon dating is one of the most commonly used methods of determining a fossil’s age. (Hammer, 70). Also, Neanderthal mtDNA is differs severely from modern human mtDNA. For example, Microcephalin is a gene for brain size during the development of the organism.
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The main cause of Progeria is a genetic mutation. This disease stems from "a single-nucleotide substitution that leads to aberrant splicing of the LMNA, the gene that encodes for the A-type nuclear lamins."(Kudlow, Kennedy, and Monnat 398) This single-letter misspelling occurs on chromosome 1 of the gene, which codes for lamin A. A point mutation from cytosine to thymine ensues near the end of the LMNA gene, a discovery by the Collins Laboratory. Gly608Gly,the most common mutation, results in "one hundred and fifty nucleotides encoded in exon eleven to be spliced out of the final mRNA and results in a protein that lacks 50 amino acids." (Kudlow, Kennedy, and Monnat 399) Now that the mutation has taken place, the cells begin to synthesize abnormal lamin A proteins known as Progerin. Newly produced Progerin still have the attached farnesyl group engendering the Progerin to connect to the nuclear membrane permanently. Due to thi...
Perform the docking studies of proteasome with normal huntingtin protein, mutated huntingtin protein as well as mutated huntingtin oligomer
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Proteogenomics is a kind of science field that includes proteomics and genomics. Proteomic consists of protein sequence information and genomic consists of genome sequence information. It is used to annotate whole genome and protein coding genes. Proteomic data provides genome analysis by showing genome annotation and using of peptides that is gained from expressed proteins and it can be used to correct coding regions.Identities of protein coding regions in terms of function and sequence is more important than nucleotide sequences because protein coding genes have more function in a cell than other nucleotide sequences. Genome annotation process includes all experimental and computational stages.These stages can be identification of a gene ,function and structure of a gene and coding region locations.To carry out these processes, ab initio gene prediction methods can be used to predict exon and splice sites. Annotation of protein coding genes is very time consuming process ,therefore gene prediction methods are used for genome annotations. Some web site programs provides these genome annotations such as NCBI and Ensembl. These tools shows sequenced genomes and gives more accurate gene annotations. However, these tools may not explain the presence of a protein. Main idea of proteogenomic methods is to identify peptides in samples by using these tools and also with the help of mass spectrometry.Mass spectrometry searches translation of genome sequences rather than protein database searching. This method also annotate protein protein interactions.MS/MS data searching against translation of genome can determine and identify peptide sequences.Thus genome data can be understood by using genomic and transcriptomic information with this proteogenomic methods and tools. Many of proteomic information can be achieved by gene prediction algorithms, cDNA sequences and comparative genomics. Large proteomic datasets can be gained by peptide mass spectrophotometry for proteogenomics because it uses proteomic data to annotate genome. If there is genome sequence data for an organism or closely related genomes are present,proteogenomic tools can be used. Gained proteogenomic data provides comparing of these data between many related species and shows homology relationships among many species proteins to make annotations with high accuracy.From these studies, proteogenomic data demonstrates frame shifts regions, gene start sites and exon and intron boundaries , alternative splicing sites and its detection , proteolytic sites that is found in proteins, prediction of genes and post translational modification sites for protein.
The balance of the thyroid hormone is complicated and involves the participation of different parts of the body (Kaplustin, 2010).
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More than 2 Amino Acids (long chain) = Polypeptide – (Primary Structure - Chain of Amino Acids)
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A polypeptide chain is a series of amino acids that are joined by the peptide bonds. Each amino acid in a polypeptide chain is called a residue. It also has polarity because its ends are different. The backbone or main chain is the part of the polypeptide chain that is made up of a regularly repeating part and is rich with the potential for hydrogen-bonding. There is also a variable part, which comprises the distinct side chain. Each residue of the chain has a carbonyl group, which is good hydrogen-bond acceptor, and an NH group, which is a good hydrogen-bond donor. The groups interact with the functional groups of the side chains and each other to stabilize structures. Proteins are polypeptide chains that have 500 to 2,000 amino acid residues. Oligopeptides, or peptides, are made up of small numbers of amino acids. Each protein has a precisely defined, unique amino acid sequence, referred to as its primary structure. The amino acid sequences of proteins are determined by the nucleotide sequences of genes because nucleotides in DNA specify a complimentary sequence in RNA, which specifies the amino acid sequence. Amino acid sequences determine the 3D structures of proteins. An alteration in the amino acid sequence can produce disease and abnormal function. All of the different ways