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Temporal expression of types XII and XIV collagen mRNA and protein during avian corneal development
Author(s) -
Gordon Marion K.,
Foley Joseph W.,
Linsenmayer Thomas F.,
Fitch John M.
Publication year - 1996
Publication title -
developmental dynamics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.634
H-Index - 141
eISSN - 1097-0177
pISSN - 1058-8388
DOI - 10.1002/(sici)1097-0177(199605)206:1<49::aid-aja5>3.0.co;2-0
Subject(s) - stroma , stromal cell , biology , cornea , fibril , microbiology and biotechnology , extracellular matrix , type i collagen , messenger rna , immunohistochemistry , matrix (chemical analysis) , collagen, type i, alpha 1 , collagen fibril , anatomy , chemistry , biochemistry , immunology , gene , endocrinology , cancer research , chromatography , neuroscience
Using immunohistochemistry and competitive PCR for collagen types XII and XIV, we have followed the expression of these fibril‐associated molecules during development of the avian cornea. By immunofluorescence histochemistry, both molecules are found in the acellular primary stroma and are therefore presumably of epithelial origin. During formation and development of the secondary corneal stroma, which is populated by mesenchymal cells, the molecules generally appear to be spatially segregated from each other. Type XIV collagen is found throughout most of the stroma, and therefore is predominantly a product of stromal fibroblasts. During subsequent compaction of the cornea, an event necessary for corneal transparency, the collagen XIV mRNA level increases dramatically, suggesting that this molecule may play a role in this event. Type XII collagen is more localized, occurring mainly in regions of the secondary stroma where matrices interface, such as where Bowman's membrane and Descemet's membrane abut the orthogonally layered collagen fibrils of the stromal matrix. These interfacial regions are highly stable areas of the cornea as determined previously by protease digestion and thermal denaturation studies. Type XII collagen may be involved in this stabilization. © 1996 Wiley‐Liss, Inc.