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Expanding the chondroitin glycoproteome of Caenorhabditis elegans.

Artikel i vetenskaplig tidskrift
Författare Fredrik Noborn
Alejandro Gomez Toledo
Waqas Nasir
Jonas Nilsson
Tabea Dierker
Lena Kjellén
Göran Larson
Publicerad i The Journal of biological chemistry
Volym 293
Nummer/häfte 1
Sidor 379-389
ISSN 1083-351X
Publiceringsår 2018
Publicerad vid Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin
Sidor 379-389
Språk en
Länkar dx.doi.org/10.1074/jbc.M117.807800
www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord chondroitin, proteoglycan, Caenorhabditis elegans, nano-scale liquid chromatography, tandem mass spectrometry,
Ämneskategorier Cell- och molekylärbiologi, Cellbiologi, Kemi

Sammanfattning

Chondroitin sulfate proteoglycans (CSPGs) are important structural components of connective tissues in essentially all metazoan organisms. In vertebrates, CSPGs are involved also in more specialized processes such as neurogenesis and growth factor signaling. In invertebrates, however, knowledge of CSPGs core proteins and proteoglycan-related functions is relatively limited, even for Caenorhabditis elegans. This nematode produces large amounts of non-sulfated chondroitin in addition to low-sulfated chondroitin sulfate chains. So far, only nine core proteins (CPGs) have been identified, some of which have been shown to be involved in extracellular matrix formation. We recently introduced a protocol to characterize proteoglycan core proteins by identifying CS-glycopeptides with a combination of biochemical enrichment, enzymatic digestion, and nano-scale liquid chromatography MS/MS analysis. Here, we have used this protocol to map the chondroitin glycoproteome in C. elegans, resulting in the identification of 15 novel CPG proteins in addition to the nine previously established. Three of the newly identified CPGs displayed homology to vertebrate proteins. Bioinformatics analysis of the primary protein sequences revealed that the CPG proteins altogether contained 19 unique functional domains, including Kunitz and endostatin domains, suggesting direct involvement in protease inhibition and axonal migration, respectively. The analysis of the core protein domain organization revealed that all chondroitin attachment sites are located in unstructured regions. Our results suggest that CPGs display a much greater functional and structural heterogeneity than previously appreciated and indicate that specialized proteoglycan-mediated functions evolved early in metazoan evolution.

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