Human DNA Sequence Composed Term Paper

Pages: 4 (1160 words)  ·  Bibliography Sources: 0  ·  File: .docx  ·  Level: College Senior  ·  Topic: Genetics

SAMPLE EXCERPT . . .
These two databases are available for search. To search a sequence against eBLOCKs, please enter your protein sequence in FASTA format and choose either eMOTIF or eMATRIX as your Search Method." (Stanford.edu, 2005)

DNA Sequence

The results of the internet search for this specific DNA sequence came back with a great deal of information which then required additional research. The results identified a serine protease better known as enterokinase or PRSS7. Enterokinase is an intestinal enzyme that helps the body initiate activation of pancreatic proteolytic proenzymes. "Enterokinase is a serine protease of the duodenal brush border membrane that cleaves trypsinogen and produces active trypsin, thereby leading to the activation of many pancreatic digestive enzymes. Overlapping cDNA clones that encode the complete human enterokinase amino acid sequence were isolated from a human intestine cDNA library." (Kitamoto et al., 1995) Dr. Kitamoto also points out that these structural features are conserved among human, bovine, and porcine enterokinase and that they can be detected only in small intestine.

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Chromosome 21 has been identified as the smallest human autosome. "The enterokinase gene was localized to human chromosome 21q21 by fluorescence in situ hybridization." (Kitamoto et al., 1995) Researchers have concluded that Human chromosome 21 is of great importance to the medical research community because there are such a large number of genetic or familial disorders that can be mapped to this chromosome. Although many of these do not pertain directly to the enterokinase gene, chromosome 21 in general have been tied to Down syndrome, five percent of familial amyotrophic lateral sclerosis or motor neuron disease) and even Alzheimer's disease. The chromosomal translocations have also been tied to cancers like Ewing's sarcoma and acute myeloid leukemia.

Term Paper on Human DNA Sequence Composed of Assignment

This serine protease is a part of the intestinal brush border in the small intestine. "Congenital enteropeptidase deficiency is a rare recessively inherited disorder leading, in affected infants, to severe failure to thrive. The genomic structure of the proenteropeptidase gene (25 exons, total gene size 88 kb) was characterized in order to perform DNA sequencing in three clinically and biochemically proved patients with congenital enteropeptidase deficiency who were from two families." (Holzinger et al., 2002) Dr. Holzinger noted that defective alleles provided first evidence that proenteropeptidase-gene mutations are the primary cause of congenital enteropeptidase deficiency.

(UWCM, 2005)

Obviously, enterokinase gene being tied to this chromosome entails a great deal of research interest into the biological functions of the gene and the manner by which it contributes to disease. Defects in PRSS7 therefore are a direct cause of enterokinase deficiency which is a life-threatening intestinal malabsorption disorder. The disorder can be characterized by severe bouts of diarrhea and failure to thrive and thus create a situation of initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase a).

Animals, like humans, have to handle digestion of exogenous macromolecules without destroying endogenous constituents so the serine protease or enterokinase seems to be a fundamental digestive system requirement. In other words, all vertebrates such as mice or dogs have adapted a two step enzymatic cascade that is used to change pancreatic zymogens over to active enzymes in the lumen of the gut as discovered by researchers in Pavlov's laboratory in the early 1900's. "Extracts of the proximal small intestine were shown strikingly to activate the latent hydrolytic enzymes in pancreatic fluid. Pavlov considered this intestinal factor to be an enzyme that activated other enzymes, or a 'ferment of ferments' and named it enterokinase." (Stone, 2002)

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