LECSTER is the largest, open-access searchable database of lectin characterizations, clinical correlates and citations on the Internet.

Programmed and curated by Peter D'Adamo.

Copyright 2001-2011.

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Total number of records: 619 Matching records: 1

Homo sapiens :

Molecular structure of

Homo sapiens

Lecster ID:351 Edit Entry
Source Organism:
Species:Homo sapiens
Common Nomenclature:Brevican
Class:Soluble C-lectin ('Lecticans')
Index Nomenclature:LECh.Xxx.Xxx.xx.Xxxx
Characterization Notes:A proteoglycan core peptide. Brevican is a member of the chondroitin sulphate (CS) proteoglycan family, which also includes versican/PG-M, neurocan and neurocan. BEHAB/brevican is an extracellular matrix component associated with invasive glioma. See: Clin Neurosurg 2000;47:72-82 These proteoglycans are characterized by the presence of a hyaluronan-binding domain and a C-type lectin domain in their core proteins. Through these domains, lecticans interact with carbohydrate and protein ligands in the extracellular matrix and act as linkers of these extracellular matrix molecules. See: Cell Mol Life Sci 2000 Feb;57(2):276-89 Brevican may play a role in maintaining the extracellular environment of mature brain as a major constituent of the adult brain extracellular matrix. See: Perspect Dev Neurobiol 1996;3(4):307-17
Biological Activity:Aggrecan, versican, neurocan, and brevican are important components of the extracellular matrix in various tissues. Their amino-terminal globular domains bind to hyaluronan, but the function of their carboxyl-terminal globular domains has long remained elusive.aggrecan, versican, and brevican lectin domains bind fibulin-2, whereas neurocan does not. As expected for a C-type lectin, the interactions are calcium-dependent, with K(D) values in the nanomolar range as measured by surface plasmon resonance.
Source Tissue:
References:J Biol Chem 2001 Jan 12;276(2):1253-61

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2015-1-27: Current Date 5:54:44 GMT: Current Time

By Peter D'Adamo. Copyright 2001-2011.