Sys-BodyFluid: a systematical database for human body fluid proteome research

Li, Su-Jun; Peng, Mao; Li, Hong; Liu, Boshu; Wang, Chuan; Wu, Jiarui; Li, Yixue; Zeng, Rong

doi:10.1093/nar/gkn849

Cited by 81 publications

(60 citation statements)

References 59 publications

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“…CLU mRNA is also abundant in the human lacrimal glands [148,149], meibomian glands [149] and accessory lacrimal glands of Wolfring [150] and mass spectrometric analyses have demonstrated CLU protein in human tears [151][152][153][154][155][156][157][158][159][160][161][162][163][164]. This localization pattern is consistent with the notion of a protective role for CLU at the fluid-tissue interface of the ocular surface epithelia.…”

Section: Ocular Surface Barrier Function In Dry Eye Diseasesupporting

confidence: 62%

“…CLU has been identified in basal and reflex tear proteomics profiles of normal human subjects [156][157][158][159][160][161][162][163][164], dry eye subjects [151,152,155], and subjects with pterygium, Sjögren's syndrome, diabetes, diabetic retinopathy, and multiple sclerosis [151][152][153][154]164], however the actual concentration of CLU in tears has never been measured. In our recently published paper, we report the first ever measurement of tear CLU concentration [24].…”

Section: Ocular Surface Barrier Function In Dry Eye Diseasementioning

confidence: 99%

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Clusterin in the eye: An old dog with new tricks at the ocular surface

Fini

Bauskar

Jeong

et al. 2016

Experimental Eye Research

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, M. R. (2016). Clusterin in the eye: an old dog with new tricks at the ocular surface. Experimental Eye Research, Clusterin in the eye: an old dog with new tricks at the ocular surface AbstractThe multifunctional protein clusterin (CLU) was first described in 1983 as a secreted glycoprotein present in ram rete testis fluid that enhanced aggregation ('clustering') of a variety of cells in vitro. It was also independently discovered in a number of other systems. By the early 1990s, CLU was known under many names and its expression had been demonstrated throughout the body, including in the eye. Its homeostatic activities in proteostasis, cytoprotection, and anti-inflammation have been well documented, however its roles in health and disease are still not well understood. CLU is prominent at fluid-tissue interfaces, and in 1996 it was demonstrated to be the most highly expressed transcript in the human cornea, the protein product being localized to the apical layers of the mucosal epithelia of the cornea and conjunctiva. CLU protein is also present in human tears. Using a preclinical mouse model for desiccating stress that mimics human dry eye disease, the authors recently demonstrated that CLU prevents and ameliorates ocular surface barrier disruption by a remarkable sealing mechanism dependent on attainment of a critical all-or-none concentration in the tears. When the CLU level drops below the critical all-or-none threshold, the barrier becomes vulnerable to desiccating stress. CLU binds selectively to the ocular surface subjected to desiccating stress in vivo, and in vitro to LGALS3 (galectin-3), a key barrier component. Positioned in this way, CLU not only physically seals the ocular surface barrier, but it also protects the barrier cells and prevents further damage to barrier structure. CLU depletion from the ocular surface epithelia is seen in a variety of inflammatory conditions in humans and mice that lead to squamous metaplasia and a keratinized epithelium. This suggests that CLU might have a specific role in maintaining mucosal epithelial differentiation, an idea that can now be tested using the mouse model for desiccating stress. Most excitingly, the new findings suggest that CLU could serve as a novel biotherapeutic for dry eye disease. Competing Interests: US patent 9,241,974 B2 entitled "Clusterin pharmaceuticals and treatment methods using the same" (inventors: MEF and SJ), assigned to the University of Southern California, is connected with this work. MEF holds a management position with Proteris Biotech, Inc., Pasadena, CA, which is developing Protearin for dry eye based on clusterin. MRW declares that he has no competing interests. Page 3 of 65 AbstractThe multifunctional protein clusterin (CLU) was first described in 1983 as a secreted glycoprotein present in ram rete testis fluid that enhanced aggregation ('clustering') of a variety of cells in vitro. It was also independently discovered in a number of other systems. By the early 1990s, CLU was known under many names and its expression had bee...

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Section: Ocular Surface Barrier Function In Dry Eye Diseasesupporting

confidence: 62%

Section: Ocular Surface Barrier Function In Dry Eye Diseasementioning

confidence: 99%

Clusterin in the eye: An old dog with new tricks at the ocular surface

Fini

Bauskar

Jeong

et al. 2016

Experimental Eye Research

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“…Ultimately, a database of all correlations and annotations found using each method from large populations of LC-ESI-MS/MS experiments will be required (Pruess et al, 2003;Zhu et al, 2006;Zhang, Wu, & Li, 2006b). A number of databases listing the proteins identified from blood have already been created Zhang et al, 2006aZhang et al, , 2007Saha, Harrison, & Chen, 2008;Li et al, 2009). Blood likely contains all the proteins expressed in other human tissues and cells .…”

Section: H Blood Protein Peptide and Ion Databasementioning

confidence: 99%

Mass spectrometry of peptides and proteins from human blood

Zhu

Bowden

Zhang

et al. 2010

Mass Spectrometry Reviews

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It is difficult to convey the accelerating rate and growing importance of mass spectrometry applications to human blood proteins and peptides. Mass spectrometry can rapidly detect and identify the ionizable peptides from the proteins in a simple mixture and reveal many of their post-translational modifications. However, blood is a complex mixture that may contain many proteins first expressed in cells and tissues. The complete analysis of blood proteins is a daunting task that will rely on a wide range of disciplines from physics, chemistry, biochemistry, genetics, electromagnetic instrumentation, mathematics and computation. Therefore the comprehensive discovery and analysis of blood proteins will rank among the great technical challenges and require the cumulative sum of many of mankind's scientific achievements together. A variety of methods have been used to fractionate, analyze and identify proteins from blood, each yielding a small piece of the whole and throwing the great size of the task into sharp relief. The approaches attempted to date clearly indicate that enumerating the proteins and peptides of blood can be accomplished. There is no doubt that the mass spectrometry of blood will be crucial to the discovery and analysis of proteins, enzyme activities, and post-translational processes that underlay the mechanisms of disease. At present both discovery and quantification of proteins from blood are commonly reaching sensitivities of ∼1 ng/mL.

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“…c Thermograms of CSF taken from non-GBM neoplastic diseases such as carcinomatosis meningitis from breast cancer (H318 and H339), lung cancer (A570 and H190), melanoma (S259 and S216), and primary CNS lymphoma (S238, S47 and A633) CSF protein content [14]). The number of entries in the CSF database to date exceeds 1,000 proteins and peptides [5,15]. Currently, there are over 500 minor proteins and peptides that are identified in CSF but not detected in blood plasma [16].…”

Section: Dsc As a Diagnostic Toolmentioning

confidence: 99%

Preliminary use of differential scanning calorimetry of cerebrospinal fluid for the diagnosis of glioblastoma multiforme

et al. 2011

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Thermal stability signatures of complex molecule interaction in biological fluids can be measured using a new approach called differential scanning calorimetry (DSC). The thermal stability of plasma proteome has been described previously as a method of producing a disease-specific "signature," termed thermogram, in several neoplastic and autoimmune diseases. We describe the preliminary use of DSC performed on cerebrospinal fluid (CSF) as a diagnostic tool for the identification of patients with glioblastoma multiforme (GBM). Samples of CSF from nine patients with confirmed GBM were evaluated using DSC, and the thermogram signatures evaluated. These thermograms were compared with thermograms of CSF taken from patients with non-neoplastic conditions such as head trauma, hydrocephalus, or CSF leak. Further analysis was also performed on CSF from patients who had non-GBM neoplastic conditions such as carcinomatosis meningitis or central nervous system lymphoma or leukemia. The DSC thermograms of CSF of the patients with GBM were significantly different when compared with other neoplastic and non-neoplastic cases. The melting temperature of the major transition was shifted by 5°C, which makes it easily distinguishable from control cases. Our results are very preliminary, but it appears that the DSC of CSF has potential utility in diagnostics and monitoring disease progression in GBM patients.

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Sys-BodyFluid: a systematical database for human body fluid proteome research

Cited by 81 publications

References 59 publications

Clusterin in the eye: An old dog with new tricks at the ocular surface

Clusterin in the eye: An old dog with new tricks at the ocular surface

Mass spectrometry of peptides and proteins from human blood

Preliminary use of differential scanning calorimetry of cerebrospinal fluid for the diagnosis of glioblastoma multiforme

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