Collagen types XII and XIV are present in basement membrane zones during human embryonic development

• Published in: Journal of Molecular Histology Vol. 35; no. 8-9; pp. 803 - 810
• Main Authors: Thierry, Laurice, Geiser, Andrea Sabine, Hansen, Antje, Tesche, Florian, Herken, Rainer, Miosge, Nicolai
• Format: Journal Article
• Language: English
• Published: Netherlands Springer Nature B.V 01.11.2004
• Subjects: Basement Membrane - chemistry; Basement Membrane - metabolism; Cellular biology; Collagen; Collagen - metabolism; Collagen Type XII - metabolism; Embryo, Mammalian - anatomy & histology; Embryo, Mammalian - physiology; Gestational Age; Glycoproteins - metabolism; Humans; Morphogenesis; Proteins; Tissue Distribution
• ISSN: 1567-2379; 1573-6865; 1567-2387
• DOI: 10.1007/s10735-004-1132-y

The collagens constitute a large group of proteins in the extracellular matrix that can be divided into several distinct families. Collagen types XII and XIV belong to a subgroup of non-fibrillar-collagens termed (fibril-associated collagens with interrupted triple-helices) (FACIT) and may be involved in basement membrane regulation providing specific molecular bridges between fibrils and other matrix components. However, the tissue distribution of the two proteins during human embryogenesis is still unclear. As a first step toward the elucidation of their possible cell biological functions, we compared the distribution of the two collagens during human organogenesis at the light microscopical level. We detected specific differences between the expression patterns of the two molecules, which may be related to their respective function within the basement membrane zones during human embryonic development. For example, in the developing intestine, collagen type-XII was present in the basement membrane zones of epithelia and endothelia. However, collagen type-XIV was restricted to the mesothelial basement membrane zones. We conclude that both collagens might well be able to serve different functions during human embryonic development although their structures are highly similar.