Colocalization in vivo and association in vitro of perlecan and elastin

Abstract

We have colocalized elastin and fibrillin-1 with perlecan in extracellular matrix of tensional and weight-bearing connective tissues. Elastin and fibrillin-1 were identified as prominent components of paraspinal blood vessels, and posterior longitudinal ligament in the human fetal spine and outer annulus fibrosus of the fetal intervertebral disc. We also colocalized perlecan with a synovial elastic basal lamina, where the attached synovial cells were observed to produce perlecan. Elastin, fibrillin-1 and perlecan were co-localized in the intima and media of small blood vessels in the synovium and in human fetal paraspinal blood vessels. Elastic fibers were observed at the insertion point of the anterior cruciate ligament to bone in the ovine stifle joint where they colocalized with perlecan. Elastin has not previously been reported to be spatially associated with perlecan in these tissues. Interactions between the tropoelastin and perlecan heparan sulfate chains were demonstrated using quartz crystal microbalance with dissipation solid phase binding studies. Electrostatic interactions through the heparan sulfate chains of perlecan and core protein mediated the interactions with tropoelastin, and were both important in the coacervation of tropoelastin and deposition of elastin onto perlecan immobilized on the chip surface. This may help us to understand the interactions which are expected to occur in vivo between the tropoelastin and perlecan to facilitate the deposition of elastin and formation of elastic microfibrils in situ and would be consistent with the observed distributions of these components in a number of connective tissues.

Effect of elastin digestion on the quasi-static tensile response of medial collateral ligament

“…This contrasts with prior reports in ligament and tendon of 4–6% by wet weight . The literature on elastin in cruciate and collateral knee ligaments is sparse, with studies focusing on visualizing the elastic network . Our study is a first report of elastin in porcine MCL, so differences could be driven by species or the relative extensibility of the tissue, which is related to overall elastin content.…”

The “other” 15–40%: The Role of Non‐Collagenous Extracellular Matrix Proteins and Minor Collagens in Tendon

“…The altered collagen fibril structure resulted in increased tensile strength. Perlecan can form a network together with fibrillin microfibrils, elastic fibers, and collagen type VI in the PCM/ECM . In addition, perlecan can interact with several ECM proteins and growth factors and can anchor fibrillin microfibrils into the basement membrane in skin .…”

Leptospiral extracellular matrix adhesins as mediators of pathogen-host interactions

“…The elastin results in the assembly of the monomeric precursor tropoelastin (Muiznieks et al, 2010). Elastin proportionally provides a degree of elasticity to the ECM, and further permits molecular interaction with ECM components such as proteoglycans, fibulin, and fibrillin (Hayes et al, 2011).…”