Open AccessCollagen XVIII: a Novel Heparan Sulfate Proteoglycan Associated with Vascular Amyloid Depositions and Senile Plaques in Alzheimer's Disease Brains
Author(s) -
Horssen Jack,
Wilhelmus Micha M. M.,
Heljasvaara Ritva,
Pihlajaniemi Taina,
Wesseling Pieter,
Waal Robert M. W.,
Verbeek Marcel M.
Publication year - 2002
Publication title -
brain pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.986
H-Index - 132
eISSN - 1750-3639
pISSN - 1015-6305
DOI - 10.1111/j.1750-3639.2002.tb00462.x
Subject(s) - senile plaques , syndecan 1 , proteoglycan , heparan sulfate , polyclonal antibodies , extracellular matrix , cerebral amyloid angiopathy , pathology , chemistry , perlecan , immunohistochemistry , amyloid (mycology) , alzheimer's disease , glycosaminoglycan , microbiology and biotechnology , antibody , biology , medicine , biochemistry , immunology , disease , cell , dementia
Heparan sulfate proteoglycans (HSPGs) may play a role in the formation and persistence of senile plaques and neurofibrillary tangles in Alzheimer's disease brains. Recently, it has been demonstrated that the human extracellular matrix‐associated molecule collagen XVIII is the first collagen carrying heparan sulfate side‐chains. Two variants of collagen XVIII with both different signal peptides and N‐terminal domains have been described and are referred to as the short and long form. To investigate the distribution of these variants we performed an immunohistochemical analysis by using specific well‐characterized polyclonal antibodies. Anti‐long huXVIII, a polyclonal antibody directed against the long variant of collagen XVIII, weakly stained large cortical and leptomeningeal vessels, whereas small cortical vessels remained unstained. Interestingly, all amyloid‐laden vessels and classic senile plaques were strongly stained. Anti‐all huXVIII, a polyclonal antibody directed against an epitope common to both collagen XVIII variants, intensely stained all types of cerebral blood vessels, cerebral amyloid angiopathy‐affected vessels and classic senile plaques. Collagen XVIII expression was absent in neurofibrillary tangles. We conclude that collagen XVIII is a novel heparan sulfate proteoglycan associated with vascular Aβ and classic senile plaques and that at least the long form of collagen XVIII accumulates in amyloid‐laden vessels and classic senile plaques.