A 2‐D gel reference map of the basic human heart proteome

Polden, Julie; McManus, Ciara A.; Remedios, Cris dos; Dünn, Michael J.

doi:10.1002/pmic.201000182

Cited by 15 publications

(10 citation statements)

References 24 publications

(27 reference statements)

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“…Recently, the Human Proteome Organization (HUPO) launched the Human Proteome Project (HPP), which generated a map of all the proteins in human tissue, both in normal and disease states . The protein map of several human tissues was characterized, including brain , heart , kidney , pancreas , liver , and plasma . Over 1000 human testicular proteins have been identified using 2DE combined with MS or 1D SDS‐PAGE combined with LC .…”

Section: Introductionmentioning

confidence: 99%

Scanning of novel cancer/testis proteins by human testis proteomic analysis

Liu

Lin

et al. 2013

Proteomics

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The testes are where spermatogenesis, the sperm-generating process that is unique to men, occurs. Importantly, human spermatogenesis and tumorigenesis share key similarities. Until now, only a few proteins in the human testis have been identified due to limitations of available technology. In this paper, using an advanced proteomics platform, we have identified 7346 unique proteins within the human testis with a high degree of confidence. Immunohistochemistry data from the Human Protein Atlas database show over 90% (1833/2020) of identified proteins can be detected in the human testis using specific antibodies. To make the data widely available to the scientific community, an online Human Testis Proteome Database (HTPD, http://reprod.njmu.edu.cn/htpd/) was built. Many of the identified human testicular proteins are associated with human infertility, especially human testicular predominantly expressed proteins. We characterized six novel cancer/testis genes (TMPRSS12, TPPP2, PRSS55, DMRT1, PIWIL1, HEMGN), which map to cancer-associated genetic variants positions, in both the cancer and testis tissues using genome-wide analyses. Our results provide a molecular connection between spermatogenesis and tumorigenesis and broaden the range of cancer antigen choice available for immunotherapy.

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Section: Introductionmentioning

confidence: 99%

Scanning of novel cancer/testis proteins by human testis proteomic analysis

Liu

Lin

et al. 2013

Proteomics

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“…This was an example of how the SHB confirmed observations that were discovered using a murine model. The next year, we produced the first 2-D gel reference map of the basic proteins (Polden et al 2011), which remains a valuable reference.…”

Section: Coronary Artery Diseasementioning

confidence: 99%

The Sydney Heart Bank: improving translational research while eliminating or reducing the use of animal models of human heart disease

Remedios

Lal

et al. 2017

Biophys Rev

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The Sydney Heart Bank (SHB) is one of the largest human heart tissue banks in existence. Its mission is to provide high-quality human heart tissue for research into the molecular basis of human heart failure by working collaboratively with experts in this field. We argue that, by comparing tissues from failing human hearts with age-matched non-failing healthy donor hearts, the results will be more relevant than research using animal models, particularly if their physiology is very different from humans. Tissue from heart surgery must generally be used soon after collection or it significantly deteriorates. Freezing is an option but it raises concerns that freezing causes substantial damage at the cellular and molecular level. The SHB contains failing samples from heart transplant patients and others who provided informed consent for the use of their tissue for research. All samples are cryopreserved in liquid nitrogen within 40 min of their removal from the patient, and in less than 5-10 min in the case of coronary arteries and left ventricle samples. To date, the SHB has collected tissue from about 450 failing hearts (>15,000 samples) from patients with a wide range of etiologies as well as increasing numbers of cardiomyectomy samples from patients with hypertrophic cardiomyopathy. The Bank also has hearts from over 120 healthy This article is part of a Special Issue on 'IUPAB Edinburgh Congress' edited by Damien Hall.Electronic supplementary material The online version of this article

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“…Peptide mass fingerprints of such lower mass HspB5 spots in the mouse eye lens suggest truncation from both the N-and C-terminal ends of the protein (Hoehenwarter et al 2008). In one study of the human heart, an HspB5 form with an estimated Mr of 30 kDa was identified that is clearly above the size of the HspB5 monomer (Polden et al 2011). However, identity of this or any other HspB5 species listed in Table 1 with HspB5L-P44 can be excluded, based on the different masses and isoelectric points.…”

Section: Hspb5 Speciation As Found In Proteome Databasesmentioning

confidence: 99%

Small heat shock protein speciation: novel non-canonical 44 kDa HspB5-related protein species in rat and human tissues

Benndorf

Gilmont

Hirano

et al. 2018

Cell Stress and Chaperones

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When analyzing small stress proteins of rat and human tissues by electrophoretic methods followed by western blotting, and using the anti-HspB1/anti-HspB5 antibody clone 8A7, we unexpectedly found a protein with a molecular mass of ~44 kDa. On two-dimensional gels, this protein resolved into four distinct species. Electrophoretic and immunological evidence suggests that this 44 kDa protein is a derivative of HspB5, most likely a covalently linked HspB5 dimer. This HspB5-like 44 kDa protein (HspB5L-P44) is particularly abundant in rat heart, brain, and renal cortex and glomeruli. HspB5L-P44 was also found in human brains, including those from patients with Alexander disease, a condition distinguished by cerebral accumulation of HspB5. Gray matter of such a patient contained an elevated amount of HspB5L-P44. A spatial model of structurally ordered dimeric HspB5 α-crystallin domains reveals the exposed and adjacent position of the two peptide segments homologous to the HspB1-derived 8A7 antigen determinant peptide (epitope). This explains the observed extraordinary high avidity of the 8A7 antibody towards HspB5L-P44, as opposed to commonly used HspB5-specific antibodies which recognize other epitopes. This scenario also explains the remarkable fact that no previous study reported the existence of HspB5L-P44 species. Exposure of rat endothelial cells to UV light, an oxidative stress condition, temporarily increased HspB5L-P44, suggesting physiological regulation of the dimerization. The existence of HspB5L-P44 supports the protein speciation discourse and fits to the concept of the protein code, according to which the expression of a given gene is reflected only by the complete set of the derived protein species.

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A 2‐D gel reference map of the basic human heart proteome

Cited by 15 publications

References 24 publications

Scanning of novel cancer/testis proteins by human testis proteomic analysis

Scanning of novel cancer/testis proteins by human testis proteomic analysis

The Sydney Heart Bank: improving translational research while eliminating or reducing the use of animal models of human heart disease

Small heat shock protein speciation: novel non-canonical 44 kDa HspB5-related protein species in rat and human tissues

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