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Testican‐3: a brain‐specific proteoglycan member of the BM ‐40/ SPARC /osteonectin family
Author(s) -
Hartmann Ursula,
Hülsmann Hanni,
Seul Judith,
Röll Sandra,
Midani Heven,
Breloy Isabelle,
Hechler Daniel,
Müller Regina,
Paulsson Mats
Publication year - 2013
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/jnc.12212
Subject(s) - osteonectin , proteoglycan , extracellular matrix , extracellular , versican , microbiology and biotechnology , chemistry , glycoprotein , biochemistry , glycosaminoglycan , perlecan , perineuronal net , biology , enzyme , alkaline phosphatase , osteocalcin
The testicans are a three‐member family of secreted proteoglycans structurally related to the BM‐40/secreted protein acidic and rich in cystein (SPARC) osteonectin family of extracellular calcium‐binding proteins. In vitro studies have indicated that testicans are involved in the regulation of extracellular protease cascades and in neuronal function. Here, we describe the biochemical characterization and tissue distribution of mouse testican‐3 as well as the inactivation of the corresponding gene. The expression of testican‐3 in adult mice is restricted to the brain, where it is located diffusely within the extracellular matrix, as well as associated with cells. Brain‐derived testican‐3 is a heparan sulphate proteoglycan. In cell culture, the core protein is detected in the supernatant and the extracellular matrix, whereas the proteoglycan form is restricted to the supernatant. This indicates possible interactions of the testican‐3 core protein with components of the extracellular matrix which are blocked by addition of the glycosaminoglycan chains. Mice deficient in testican‐3 are viable and fertile and do not show an obvious phenotype. This points to a functional redundancy among the different members of the testican family or between testican‐3 and other brain heparan sulphate proteoglycans.