Quantitative analysis and comparative regional investigation of the extracellular matrix of the porcine temporomandibular joint disc.
Characterization of the extracellular matrix of the temporomandibular joint (TMJ) disc is crucial to advancing efforts in tissue engineering the disc. However, the current literature is incomplete and often contradictory in its attempts to describe the nature of the TMJ disc matrix. The aim of this study was to identify the variation of key matrix components along the three axes of the porcine disc using ELISAs to quantify these matrix components, immunohistochemistry to identify their regional distribution, and SEM to examine collagen fiber diameter and orientation. The overall GAG content of the TMJ disc (including the dermatan sulfate proteoglycans) was 5.3+/-1.2% of the dry weight. Chondroitin sulfate, which comprised 74% of this total GAG content, was 4.4, 8.2, and 164 times more abundant than dermatan sulfate proteoglycan, keratan sulfate, and hyaluronic acid, respectively. In general, these GAGs were most concentrated in the intermediate zone of the TMJ disc, appearing in dense clusters, and least concentrated in the posterior band. Additionally, chondroitin sulfate was more abundant medially than laterally. Collagen II was discovered in trace amounts, with higher relative amounts in the intermediate zone. Collagen fibers were observed to run primarily in a ring-like fashion around the periphery of the disc and anteroposteriorly through the intermediate zone, with a mean fiber diameter of 18+/-9 mum. Characterization studies of the TMJ disc, including prior biomechanical and cell studies along with the current study of the extracellular matrix, collectively reveal a distinct character of the intermediate zone of the disc compared to its anterior and posterior bands.
Detamore
Michael S
MS
Department of Chemical & Petroleum Engineering, University of Kansas, 1530 W. 15th St., Room 4132, Lawrence, KS 66045-7609, USA. detamore@ku.edu
Orfanos
John G
JG
Almarza
Alejandro J
AJ
French
Margaret M
MM
Wong
Mark E
ME
Athanasiou
Kyriacos A
KA
D000818:Animals; D002417:Cattle; D011508:Chondroitin Sulfate Proteoglycans / Q000737:chemistry; D002809:Chondroitin Sulfates / Q000737:chemistry; D003094:Collagen / Q000737:chemistry; D024043:Collagen Type II / Q000737:chemistry; D003871:Dermatan Sulfate / Q000737:chemistry; D004797:Enzyme-Linked Immunosorbent Assay; D005109:Extracellular Matrix / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000737:chemistry; D006820:Hyaluronic Acid / Q000737:chemistry; D007150:Immunohistochemistry; D007632:Keratan Sulfate / Q000737:chemistry; D008855:Microscopy, Electron, Scanning; D013552:Swine; D019224:Temporomandibular Joint Disc / Q000033:anatomy & histology* / Q000378:metabolism / Q000502:physiology*; D014867:Water / Q000737:chemistry
D011508:Chondroitin Sulfate Proteoglycans; D024043:Collagen Type II; D006025:Glycosaminoglycans; C032649:dermatan sulfate proteoglycan; D014867:Water; D003871:Dermatan Sulfate; D006820:Hyaluronic Acid; D002809:Chondroitin Sulfates; D003094:Collagen; D007632:Keratan Sulfate