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PMID: 11425904 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Intact aggrecan and fragments generated by both aggrecanse and metalloproteinase-like activities are present in the developing and adult rat spinal cord and their relative abundance is altered by injury.

Lemons ML, Sandy JD, Anderson DK, Howland DR

Abstract

Aggrecan is a large proteoglycan (PG) that has been grouped with different PG families on the basis of its physical characteristics. These families include the chondroitin sulfate PGs, which appear to inhibit the migration of cells and axons during development. Although aggrecan has been studied primarily in cartilage, in the present study, tissue samples from developing, mature, and injured-adult rat spinal cords were used to determine whether aggrecan is present in the mammalian spinal cord. By the use of Western blot analysis, tissues were probed with aggrecan-specific antibodies (ATEGQV, TYKHRL, and LEC-7) and aggrecan-specific neoepitope antibodies (NITEGE, FVDIPEN, and TFKEEE) to identify full-length aggrecan and several fragments. Unlike many other aggrecan gene family members, aggrecan species were similar in embryonic day 14, postnatal day 1, and adult spinal cords. Spinal cord injury caused significant decreases in aggrecan. Partial recovery in some aggrecan species was evident by 2 weeks after injury. The presence of specific aggrecan neoepitopes suggested that aggrecan is cleaved in the spinal cord by both a disintegrin and metalloproteinase thrombospondin (also known as aggrecanase) and metalloproteinase-like activities. Many aggrecan species found in the spinal cord were similar to species in cartilage. Additional antibodies were used to identify two other aggrecan gene family members, neurocan and brevican, in the adult spinal cord. These studies present novel information on the aggrecan core protein species and enzymes involved in aggrecan cleavage in vivo in the rat spinal cord throughout development and after injury. They also provide the basis for investigating the function of aggrecan in the spinal cord.

MeSH Terms
Aggrecans Aging/metabolism Animals Antibody Specificity Axotomy Blotting, Western Brevican Cartilage/metabolism Chondroitin Sulfate Proteoglycans/metabolism Endopeptidases/metabolism Epitopes Extracellular Matrix Proteins Female Immunohistochemistry Lectins, C-Type Metalloendopeptidases/metabolism Nerve Tissue Proteins/metabolism Neurocan Organ Specificity Proteoglycans/metabolism Rats Rats, Long-Evans Spinal Cord/embryology,metabolism,pathology Spinal Cord Injuries/metabolism,pathology
Chemicals
Acan protein, rat Aggrecans BCAN protein, human Bcan protein, rat Brevican Chondroitin Sulfate Proteoglycans Epitopes Extracellular Matrix Proteins Lectins, C-Type Nerve Tissue Proteins Neurocan Proteoglycans NCAN protein, human Endopeptidases Metalloendopeptidases aggrecanase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Lemons M L
Department of Neuroscience, University of Florida College of Medicine, Gainesville, Florida 32610-0244, USA.
Sandy J D
Anderson D K
Howland D R
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Article Info
Journal
The Journal of neuroscience : the official journal of the Society for Neuroscience
Abbr.
J Neurosci
ISSN
1529-2401
Published
2001-07-01
Pages
4772-81
Language
English
Region
United States
NLM ID
8102140
PMCID
PMC6762363
Subset
IM
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