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Omics score: 0

4Skin_iPS_BioReplica01

ABSTRACT: Hs iPS_vs_HES - 4Skin_iPS_BioReplica01

OTHER RELATED OMICS DATASETS IN: PXD000134PRJNA136559PRJNA142175PRJNA142177

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Others

SUBMITTER: Munoz J, Low TY, Kok YJ, Chin A, Frese CK, Ding V, Choo A, Heck AJ

PROVIDER: PAe003659 | PeptideAtlas | 2011-12-31

REPOSITORIES: PeptideAtlas

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			Action	DRS
	PAe003659_7172_tandem.params	Other
	PAe003659_README	Other
	PAe003659_Search_Results_7172_201211161313.properties	Other
	PAe003659_Search_Results_7172_201211161313.tar.gz	Other
	PAe003659_mzML_201211161132.properties	Other

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1 - 5 of 8

Publications

The quantitative proteomes of human-induced pluripotent stem cells and embryonic stem cells.

Munoz Javier J Low Teck Y TY Kok Yee J YJ Chin Angela A Frese Christian K CK Ding Vanessa V Choo Andre A Heck Albert J R AJ

Molecular systems biology 20111122

Assessing relevant molecular differences between human-induced pluripotent stem cells (hiPSCs) and human embryonic stem cells (hESCs) is important, given that such differences may impact their potential therapeutic use. Controversy surrounds recent gene expression studies comparing hiPSCs and hESCs. Here, we present an in-depth quantitative mass spectrometry-based analysis of hESCs, two different hiPSCs and their precursor fibroblast cell lines. Our comparisons confirmed the high similarity of h ...[more]

PMID: 22108792

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Acute to prolonged lif cycle proteomic profiling of heat shock SGs

Project description:Time-resolved proteomic profiling of SGs from cultured human U2OS cells over a prolonged heat-shock (HS) and a successive recovery period, sampling at the 6 time points of HS exposure (10, 20, 30, 60, 120, 180 min), as well as 2 time points of recovery (5, 10 min). From the sampled cells, we prepared SG samples using a differential centrifugation plus endogenous G3BP1 immunoprecipitation protocol. Peptides were subsequently TMT-labeled and analyzed by quantitative LC-MS/MS. In G3BP1 dataset, rep1-rep3, HS-10, 20, 30, 60, 120, 180, re5, re10, SG-ls, G3BP1-IP samples were labeled with TMT-126, 127N, 127C, 128N, 128C,129N, 129C, 130N, 130C, 131 label Reagents, respectively; G3BP1_HS0 was a dataset created to integrate a non-heat shock control (HS-0) into the G3BP1 dataset, contains HS0, HS10, and HS60, and the results was integrated into the G3BP1 dataset using the ComBat processing, HS-0_rep1, HS-0_rep2, HS-0_rep3, HS-10_rep1, HS-10_rep2, HS-10_rep3, HS-60_rep1, HS-60_rep2, HS-60_rep3 samples were labeled with TMT-126, 127N, 127C, 128N, 128C,129N, 129C, 130N, 130C label Reagents, respectively. In CAPRIN1 dataset, rep1-rep3, HS-0, 10, 20, 30, 60, 120, 180, re5, re10 samples were labeled with TMT-126, 127N, 127C, 128N, 128C,129N, 129C, 130N, 130C label Reagents, respectively.

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Project description:Comparison between Saccharomyces cerevisiae HS 10, HS 34 and HS 12, HS 37

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Protein interactors of 3-O sulfated heparan sulfates in human MCI and age-matched control cerebrospinal fluid

Project description:Heparan (HS) proteoglycans (HSPGs) are common on the cell surface and mediate many physiological processes. Binding of HSPG ligands is determined by the sulfation code on the heparan sulfate chain and the HS chain can be N-/2-O/6-O- or 3-O-sulfated, generating a heterogenous sulfation pattern. 3-O sulfated HS (3S-HS) have been reported to play a role in several pathological processes such as the coagulation system, viral pathogenesis, or in the binding and internalization of tau in Alzheimer’s disease. Few 3S-HS-specific interactors are known and the role of 3S-HS in health and disease is limited, especially in the central nervous system. Using human CSF as a surrogate for the extracellular compartment of the CNS, we determined the interactome of synthetic heparan sulfate oligosaccharides with defined sulfation patterns. These AE-MS studies significantly expand the proteins that can interact with HS and for which 3O sulfation is required. LRP1 was found as a novel 3S-HS interactor, requiring GlcA-GlcNS6S3S for binding, similar to ATIII. Both interactions were validated via Western blot. Our dataset brings forward new HS and 3S-HS ligands which can be pertinent to unravel molecular mechanisms dependent on 3S-HS in (patho)physiological conditions.

2022-08-09 | PXD034935 | Pride

Specific 3-O-sulfated heparan sulfate domains regulate salivary gland basement membrane metabolism and epithelial differentiation [female]

Project description:FGF signaling is essential for salivary gland (SG) development and heparan sulfate (HS) regulation of FGFR function is determined by immense structural diversity of sulfated HS domains. The basement membrane (BM), containing HS proteoglycans, collagens and laminins, separates epithelia from stroma and controls growth factor-matrix cross-talk. 3-O-sulfotransferases generate highly 3-O-sulfated HS domains (3-O-HS) and Hs3st3a1 and Hs3st3b1 are enriched in myoepithelial cells (MECs), which produce BM and are a growth factor signaling hub. To investigate 3-O-HS regulation of MEC function and growth factor signaling, we generated Hs3st3a1;Hs3st3b1 double knockout (DKO) mice. The DKO HS loses specific highly 3-O-sulfated tetrasaccharides, which increases FGF/FGFR-complex binding to HS. During development this leads to increased FGFR-, BM- and MEC-related gene expression. However, in adult DKO SGs the secretory units containing acinar and MECs, have reduced MECs, increased BM and disrupted acinar polarity, resulting in salivary hypofunction. We used defined 3-O-sulfated-HS in FGFR pulldown assays and primary organ cultures to investigate 3-O-HS-dependent mechanisms regulating MEC development. We find that 3-O-HS modulates FGFR signaling to regulate MEC BM synthesis which is critical for secretory unit homeostasis and acinar function. Understanding how sulfated HS regulates development will inform the use of HS mimetics in organ regeneration.

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Specific 3-O-sulfated heparan sulfate domains regulate salivary gland basement membrane metabolism and epithelial differentiation [male]

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