title: Caprine articular, meniscus and intervertebral disc cartilage: an integral analysis of collagen network and chondrocytes.
abstract: Cartilage is a tissue with only limited reparative capacities. A small part of its volume is composed of cells, the remaining part being the hydrated extracellular matrix (ECM) with collagens and proteoglycans as its main constituents. The functioning of cartilage depends heavily on its ECM. Although it is known that the various (fibro)cartilaginous tissues (articular cartilage, annulus fibrosus, nucleus pulposus, and meniscus) differ from one each other with respect to their molecular make-up, remarkable little quantitative information is available with respect to its biochemical constituents, such as collagen content, or the various posttranslational modifications of collagen. Furthermore, we have noticed that tissue-engineering strategies to replace cartilaginous tissues pay in general little attention to the biochemical differences of the tissues or the phenotypical differences of the (fibro)chondrocytes under consideration. The goal of this paper is therefore to provide quantitative biochemical data from these tissues as a reference for further studies. We have chosen the goat as the source of these tissues, as this animal is widely accepted as an animal model in orthopaedic studies, e.g. in the field of cartilage degeneration and tissue engineering. Furthermore, we provide data on mRNA levels (from genes encoding proteins/enzymes involved in the synthesis and degradation of the ECM) from (fibro)chondrocytes that are freshly isolated from these tissues and from the same (fibro)chondrocytes that are cultured for 18 days in alginate beads. Expression levels of genes involved in the cross-linking of collagen were different between cells isolated from various cartilaginous tissues. This opens the possibility to include more markers than the commonly used chondrogenic markers type II collagen and aggrecan for cartilage tissue-engineering applications.
authors.affiliation: Department of Oral Cell Biology, Academic Centre for Dentistry Amsterdam (ACTA), University of Amsterdam, Amsterdam, The Netherlands.
authors.forename: Lucienne A
authors.initials: LA
authors.lastname: Vonk
authors.forename: Robert Jan
authors.initials: RJ
authors.lastname: Kroeze
authors.forename: Behrouz Zandieh
authors.initials: BZ
authors.lastname: Doulabi
authors.forename: Roel J
authors.initials: RJ
authors.lastname: Hoogendoorn
authors.forename: Chunling
authors.initials: C
authors.lastname: Huang
authors.forename: Marco N
authors.initials: MN
authors.lastname: Helder
authors.forename: Vincent
authors.initials: V
authors.lastname: Everts
authors.forename: Ruud A
authors.initials: RA
authors.lastname: Bank
mesh_terms: D000596:Amino Acids / Q000235:genetics / Q000502:physiology; D000818:Animals; D002358:Cartilage, Articular / Q000737:chemistry / Q000502:physiology*; D002470:Cell Survival / Q000502:physiology; D019902:Chondrocytes; D018920:Coculture Techniques; D003094:Collagen / Q000032:analysis / Q000235:genetics / Q000502:physiology*; D005260:Female; D020869:Gene Expression Profiling / Q000379:methods; D006041:Goats / Q000502:physiology*; D006901:Hydroxylysine / Q000235:genetics / Q000502:physiology; D006909:Hydroxyproline / Q000235:genetics / Q000502:physiology; D007403:Intervertebral Disc / Q000737:chemistry / Q000502:physiology*; D008592:Menisci, Tibial / Q000737:chemistry / Q000502:physiology*; D012313:RNA / Q000737:chemistry / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D023822:Tissue Engineering / Q000379:methods
chemical_list: D000596:Amino Acids; D006901:Hydroxylysine; D012313:RNA; C015484:pyridinoline; D003094:Collagen; D006909:Hydroxyproline