Attachment sites of the coracoclavicular ligaments are characterized by fibrocartilage differentiation: a study on human cadaveric tissue

Scand J Med Sci Sports. 2012 Feb;22(1):12-7. doi: 10.1111/j.1600-0838.2010.01142.x. Epub 2010 Jun 18.

Abstract

We analyzed the immunohistochemical labeling patterns of the extracellular matrix of the coracoclavicular ligaments (CCL) in order to relate the molecular composition of the attachment sites to their mechanical environment. Ligaments were exposed from 12 fresh-frozen human cadaveric samples (four males, mean age: 48.6 ± 12.1 years). Cryosection of methanol-fixed and decalcified tissue was cut and sections were labeled with a panel of monoclonal antibodies directed against collagens, proteoglycans and proteins of vascular components. Attachment sites of both ligaments showed characteristic fibrocartilaginous labeling of collagen type II, aggrecan and link protein in all samples. Labeling for type II collagen was most conspicuous at the insertion of the coracoid process. Morphometry of adjacent samples revealed a fibrocartilage zone of 10-15% in relationship with the ligament proper, where labeling for type II collagen, aggrecan and link protein was negative. The presence of fibrocartilage at both entheses of the trapezoid and conoid ligament suggests that the CCL complex is subject to shear/compression forces. A variable fibrocartilage differentiation at the entheses of both ligaments may be related to the marked change in loading and insertion angle that the ligaments undergo during shoulder movement.

MeSH terms

  • Adult
  • Aggrecans / analysis
  • Biomechanical Phenomena / physiology
  • Cadaver
  • Clavicle
  • Collagen Type II / analysis
  • Extracellular Matrix / chemistry*
  • Extracellular Matrix Proteins / analysis
  • Female
  • Fibrocartilage / anatomy & histology
  • Fibrocartilage / chemistry
  • Humans
  • Immunohistochemistry
  • Ligaments / anatomy & histology*
  • Ligaments / blood supply
  • Ligaments / chemistry*
  • Male
  • Middle Aged
  • Proteoglycans / analysis
  • Scapula
  • Shoulder / blood supply
  • Shoulder / physiology

Substances

  • Aggrecans
  • Collagen Type II
  • Extracellular Matrix Proteins
  • Proteoglycans
  • link protein