| First Author | Schnepp A | Year | 2005 |
| Journal | J Biol Chem | Volume | 280 |
| Issue | 12 | Pages | 11274-80 |
| PubMed ID | 15657052 | Mgi Jnum | J:98018 |
| Mgi Id | MGI:3576962 | Doi | 10.1074/jbc.M414276200 |
| Citation | Schnepp A, et al. (2005) Mouse testican-2. Expression, glycosylation, and effects on neurite outgrowth. J Biol Chem 280(12):11274-80 |
| abstractText | Mouse testican-2 was cloned, sequenced, and shown to be a proteoglycan with a multidomain structure closely similar to that of the human ortholog, previously described as a calcium binding extracellular matrix molecule of the BM-40/SPARC/osteonectin family (Vannahme, C., Schubel, S., Herud, M., Gosling, S., Hulsmann, H., Paulsson, M., Hartmann, U., and Maurer, P. (1999). J. Neurochem. 73, 12-20). Recombinant mouse testican-2 was used to prepare specific antibodies that allowed the detection of testican-2 in various brain structures but also in lung, testis, and in several endocrine glands. Although the testican-2 expressed in EBNA-293 cells carried both heparan sulfate and chondroitin/dermatan sulfate glycosaminoglycan chains, the tissue form always contained only heparan sulfate. Both tissue-derived and recombinant testican-2 carried N-linked glycans. Tissue-derived forms of testican-2 were detected as proteoglycans of varying size, whereas a portion of the molecules produced by EBNA-293 cells were core proteins, lacking glycosaminoglycans. Both the proteoglycan and core protein forms of testican-2 inhibited neurite extension from cultured primary cerebellar neurons and may play regulatory roles in the development of the central nervous system. |
