Human protein index

Anderson NG, Anderson L. The human protein index. Clin Chem 28 739-748, 1982. Blake CCF, Johnson LN. Protein structure. Trends Biochem Sci April 147-151, 1987. Branden C, Tooze J. Introduction to Protein Structure. New York Garland, 1991. 

Currently, neither defined performance criteria nor external proficiency testing is available for 2-D laboratories. The absence of such criteria results in an overall lack of standardization that adversely affects Interlaboratory data comparison, which is essential to conduct a large multicenter project such as the Human Protein Index."... 

Anderson, N. G., A. Matheson, and N. L. Anderson. 2001, Back to the future the human protein index (HPI) and the agenda for post-proteomic biology. Proteomics 1 3-12. 

Grammer LC, Harris KE, Malo JL, et al. 1990. The use of an immunoassay index for antibodies against isocyanate human protein conjugates and application to human isocyanate disease. J Allergy Clin Immunol 86(1)94-98. 

More members of the dysbindin protein family are known in humans than in any other species at present. In articular, there are eight human proteins with dysbindin domains listed by the National Center for Biotechnology Information (NCBI http //www.ncbi.nlm.nih.gov/) and/or by the Universal Protein Resource (UniProt http //www.pir.uniprot.org/index.shtml). They are schematically shown in Figure 2.2-1, which... 

Based on International Protein Index (IPI) human sequence database via... 

In cases where there is no relevant animal species for preclinical studies due to species specificity or neutralisation of activity, the ICH guideline indicates that the use of homologous proteins (species-specific animal proteins) may be considered. However, inference of safety or therapeutic index to humans must be made with caution as biodistribution, activity and clearance may not be analogous to the human protein in humans. 

A protein with the innocuous name p53 is one of the most frequently cited biological molecules in the Science Citation Index. The "p" in p53 stands for protein and "53" indicates a molecular mass of 53 kDa. The p53 protein plays a fundamental role in human cell growth and mutations in this protein are frequently associated with the formation of tumors. It is estimated that of the 6.5 million people diagnosed with one or another form of cancer each year about half have p53 mutations in their tumor cells and that the vast majority of these mutations are single point mutations. 

The smdy of tissue protein breakdown in vivo is difficult, because amino acids released during intracellular breakdown of proteins can be extensively reutilized for protein synthesis within the cell, or the amino acids may be transported to other organs where they enter anabohc pathways. However, actin and myosin are methylated by a posttranslational reaction, forming d-methylliistidine. During intracellular breakdown of actin and myosin, 3-methylhistidine is released and excreted into the urine. The urinary output of the methylated amino acid provides a rehable index of the rate of myofibrillar protein breakdown in the musculature of human subjects. 

Ferritin is another protein that is important in the metabolism of iron. Under normal conditions, it stores iron that can be called upon for use as conditions require. In conditions of excess iron (eg, hemochromatosis), body stores of iron are greatly increased and much more ferritin is present in the tissues, such as the liver and spleen. Ferritin contains approximately 23% iron, and apoferritin (the protein moiety free of iron) has a molecular mass of approximately 440 kDa. Ferritin is composed of 24 subunits of 18.5 kDa, which surround in a micellar form some 3000-4500 ferric atoms. Normally, there is a little ferritin in human plasma. However, in patients with excess iron, the amount of ferritin in plasma is markedly elevated. The amount of ferritin in plasma can be conveniently measured by a sensitive and specific radioimmunoassay and serves as an index of body iron stores. 

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